Full opinion text
MEMORANDUM AND ORDER WILLIAM G. YOUNG, District Judge. Amgen Inc. (“Amgen”) sought declaratory relief to prevent F. Hoffmann-LaRoche Limited, Roche Diagnostics GmbH, and Hoffmann-La Roche Inc. (collectively, “Roche”) from marketing a drug that infringes U.S. Patent Nos. 5,441,868, 5,547,-933, 5,618,698, 5,621,080, 5,756,349, and 5,955,422. These patents relate to Am-gen’s recombinant erythropoietin (“EPO”), a naturally occurring protein that stimulates the production of red blood cells. Amgen, Inc. v. Hoechst Marion Roussel, Inc., 3 F.Supp.2d 104, 106 (D.Mass.1998). The jury found for Amgen across the board, upholding the validity of the claims-in-suit for the '422, '933, '868, '698, and '349 patents and finding that Roche literally infringed all of the claims-in-suit except for claim 12 of the '933 patent, which it found infringed by the doctrine of equivalents. Jury Verdict [Doc. No. 1542] at 2-3. The Court writes to explain its rulings on various pre-trial motions for summary judgment, specifically its findings and rulings that the Amgen patents survive Roche’s obviousness-double patenting contentions, to resolve various post-trial motions, and to explain the decision to grant Amgen’s request for a permanent injunction. Due to the sheer number, the Court will not be able to address every motion. Therefore, all motions not already granted and not resolved herein are denied. After explaining the grant of summary judgment on the issue of obviousness-type double patenting, the Court will address post-trial motions in three groups: validity, infringement, and injunctive relief. Regarding validity, the Court will write to explain three decisions. Primarily, the Court concluded that the source “purified from mammalian cells grown in culture” limits claim 1 of the '422 patent. As shall be discussed, the undisputed record revealed that none of the prior art, including the Goldwasser study, satisfied this limitation. Second, sufficient evidence supported the jury’s finding that the term “human erythro-poietin,” found in claim 1 of the '422 patent and claims 3, 7, and 9 of the '933 patent, is not indefinite, even though the specifications do not specify whether the glycopro-tein described therein would be 165 or 166 amino acids in length. Next, the Court will write to explain its grant of summary judgment to Amgen with respect to infringement of claim 1 of the '422 patent, see Electronic Order August 28, 2007, and the decision to uphold the jury’s finding that Roche literally infringed claim 3 of the '933 patent. See Jury Verdict at 2. As shall be discussed below, Amgen patented recombinant EPO by reference to a specific amino acid sequence. See Amgen, Inc. v. F. Hoffmann-La Roche Ltd,., 494 F.Supp.2d 54, 63 (D.Mass.2007) [hereinafter “Amgen Mark-man”]. Pegylation — the chemical reaction that attaches PEG to EPO via a single bond to form CERA, the active ingredient in MIRCERA — does not alter EPO’s amino acid sequence. See Trial Ex. 53, Roche’s Biologic License Application at 00004027 [hereinafter “Roche BLA”]. The attachment of PEG to EPO does not place MIRCERA beyond the boundary of the claims because “the specification expressly contemplates that additional molecules may be attached to ‘human erythropoiet-in.’ ” Amgen Markman, 494 F.Supp.2d at 63 (emphasis omitted). Thus, any minor modification of EPO that does not alter the specific amino acid sequence — such as the displacement of a single hydrogen atom — is immaterial and does not preclude a finding of infringement. Finally, Amgen has satisfied all four factors necessary for a permanent injunction set forth in eBay Inc. v. MercExchange, L.L.C., 547 U.S. 388, 126 S.Ct. 1837, 164 L.Ed.2d 641 (2006). Failure to issue a permanent injunction would cause irreparable, immeasurable harm, for which there is no adequate remedy at law. Given that Roche infringes Amgen’s valid patents, and in light of the harms that will be discussed, the balance of hardships clearly favors Amgen. Moreover, the Court has concluded that “the public interest would not be disserved by a permanent injunction.” Id. at 391, 126 S.Ct. 1837. The record compiled over the course of a four-day evidentiary proceeding reveals no benefit to patient health or the public coffers so great as to outweigh the public’s interest in a robust patent system. 1. BACKGROUND “Erythropoiesis, the production of red blood cells, occurs continuously throughout the human life span to offset cell destruction.” '422 Patent col. 5 ll. 41-^13. “EPO is a protein hormone” that regulates eryth-ropoiesis. Lodish Decl. [Doc. No. 513] ¶ 13. Produced in the kidneys, EPO circulates in the blood stream, id. ¶ 15, and, “Mike a key in a lock,” id. ¶ 14, binds with EPO receptors located on erythroid progenitor cells in the bone marrow, id. ¶ 17. When EPO binds to the EPO receptor it “initiated the signaling pathway that ultimately leads to red blood cell production.” Id. ¶ 24. Red blood cells, of course, contain hemoglobin, the body’s vehicle for transporting oxygen. Id. ¶ 15. “In healthy humans, the amount of EPO in circulation in the bloodstream is exquisitely regulated to produce just the required numbers of red cells.” Id. Diseases or disorders affecting the kidneys often result in an EPO deficit, which leads to a low level of red blood cells, a condition generally referred to as anemia. Amgen Inc. v. Hoechst Manon Roussel, Inc., 314 F.3d 1313, 1321 (Fed.Cir.2003) [hereinafter “Amgen II"]. For some time preceding the 1980s, the medical community believed that the introduction of additional EPO into a patient’s bloodstream could combat the effects of anemia by stimulating the production of additional red blood cells. See id. Nevertheless, a generation of researchers grappled with how to introduce exogenous EPO into the bloodstream of anemic patients. Id. Some of America’s most accomplished researchers believed they could isolate and purify EPO that had exited the body in urine. Id. Others attempted to obtain EPO from plasma. Id. These approaches proved “unsuccessful because such recovery employed techniques that were complicated, yet still resulted in a low-yield, high-impurity, or unstable EPO end product. Similar attempts using antibody techniques failed because of difficulty in providing for the large-scale isolation of quantities of EPO from mammalian sources sufficient for further analysis, clinical testing, or therapeutic use.” Id. (internal citation omitted). As of 1984, mass production of erythropoietin from recombinant DNA was not possible. Amgen, Inc. v. Hoechst Marion Roussel, Inc., 457 F.3d 1293, 1303-04 (Fed.Cir.2006) (hereinafter “Am-gen IV”). In this case, Roche’s anticipation defense focused on a clinical study supervised by Dr. Eugene Goldwasser. Dr. Goldwasser’s study, which began in 1979-1980, attempted to treat three anemic patients with EPO purified from human urine. Amgen, Inc. v. Hoechst Marion Roussel, Inc., 126 F.Supp.2d 69, 111 (D.Mass.2001) [hereinafter “Amgen I”]. The results of the Goldwasser study were mixed and are still a matter of dispute. While experts debate whether and to what extent an increase in reticulocyte count may be attributed to Dr. Goldwasser’s urinary EPO, Dr. Goldwasser, who characterized the study as a failure, has admitted that the study did not actually increase patient hematocrit, the primary indicator of health benefits for erythropoiesis-stimu-lating agents (“ESAs”). Id. at 111-12. Moreover, due to a shortage of urine from aplastic anemia patients, the study never expanded beyond the three patients. Id. at 112. In 1983, a team of Amgen researchers led by Dr. Fu-Kuen Lin identified a means of producing recombinant erythropoietin. Amgen II, 314 F.3d at 1321. Rather than attempting to obtain EPO from natural sources such as human urine, Lin identified human and monkey EPO and was “able to determine the entire DNA sequence of human EPO and from that, its predicted amino acid sequence.” Id. at 1321-22. Next, Lin generated an expression vector that he could inject into a host Chinese hamster ovary (“CHO”) cell and that would yield a protein with the amino acid sequence of human EPO. Id. Because the protein has the requisite amino acid sequence, it performed the key-in-lock function of EPO and stimulated erythro-poiesis. Amgen’s recombinant EPO revolutionized the treatment available for anemia and other blood disorders. See id. at 1321. To say that the cluster of patents protecting EPO in the United States has been a financial boon to Amgen would be like observing that Standard Oil had done pretty well in the oil business. See Amgen I, 126 F.Supp.2d at 77 (noting that EPO-GEN, the first commercial embodiment of Amgen’s patents, is one of the most successful blockbuster drugs in the history of the American pharmaceutical industry). Of course, Rockefeller never figured out how to produce a limitless supply of his product in a petri dish. A. Production and Patenting of EPO Example 10 of the patent’s specification discloses the method for producing EPO. The process begins with the: transfection (introduction) of exogenous DNA into host [CHO] cells. The CHO host cell, using its own transcription machinery, then expresses human rEPO in abundance, which then accumulates in the host cell cytoplasm or in the culture media. ['933 patent] col. 37, lines 43-49. The rEPO so recovered has the same or similar amino acid sequences and biological properties as naturally occurring human EPO, but differs in its “glycosylation,” i.e., in the patterns of branched carbohydrate chains that attach to the protein. [Id.] col. 10, lines 34-41. Amgen II, 314 F.3d at 1321-22 (footnote supplied). Of utmost importance to this case is the protein this process produces. Graphically depicted, the protein, also referred to as a polymer or a polypeptide, resembles a loosely coiled chain. Pl.’s Stat. Mat. Facts [Doc. No. 512] at 1. Every protein is comprised of a specific amino acid sequence; each amino acid represents a link in the chain. See id. at 1-2. The term “amino acid sequence” refers to the order in which each of the particular amino acids are linked to form the protein. See BRuce Alberts et al. Molecular biology of the Cell 140 (4th ed.2002). Perhaps the best way to understand the manner in which a specific amino acid sequence represents a particular protein is by analogy. While the English language has an alphabet of 26 letters, there are twenty amino acids. See '422 Patent col. 1 ll. 63-67. As particular letter combinations in a certain order form a word in the English language, each unique sequence of amino acids forms a different protein. Just as “cat” cannot be spelled c-t-a, the desired protein may only be expressed if the amino acids are in order. Depending upon the type of cell that generates the protein, human EPO consists of 165 or 166 amino acid residues. PL’s Stat. Mat. Facts [Doc. No. 512] at 1-2. The precise order of the amino acid sequence is critical because “even a single change in the amino acid sequence of the [EPO protein] or receptor can inhibit binding” and prevent the stimulation of erythropoiesis. Lodish Decl. ¶ 14. Also critical to this case is the manner in which these amino acids bond. Each amino acid is bookended by a carbon-terminal (“c-terminal”) on one end and a nitrogen-terminal (“n-terminal”) on the other. The term “n-terminal” refers to a configuration of a nitrogen atom bonded to two or three hydrogen atoms. Alberts, supra, at 131. In the case of EPO, the nitrogen in the n-terminal is bonded to two hydrogen atoms. See PL’s Stat. Mat. Facts ¶ 26. A c-terminal is a similar configuration with a carbon atom serving as the base, and, in the case of EPO, oxygen and hydrogen atoms attached. See id. When amino acids bond together to form a protein, the n-terminal of one bonds with the c-terminal of another. See id. The bond formed between the carbon from the c-terminal and the nitrogen from the n-terminal of the two amino acids is a peptide bond. Alberts, supra, at 132. The bonding process results in the displacement of one or two hydrogen atoms from the n-terminal and an oxygen or an oxygen and a hydrogen atom from the c-terminal. See PL’s Stat. Mat. Facts ¶26. These bonds are replicated at every spot where one amino acid attaches to another along the sequence. At the end, the first amino acid retains an unbonded n-terminal, while the final amino acid has an unbonded c-terminal. Id. ¶ 2. After the protein is produced in the ribosome, it is secreted into the endoplasmic reticulum where it undergoes gly-cosylation, a process where sugars attach to the polypeptide backbone. Alberts, supra, at 702. When a protein is formed in a mammalian host cell, it is called a glyco-protein. Lodish Deck ¶ 20. The EPO protein has four sites where chains of carbohydrates (sugar residues) can be attached, and three of these sites are n-terminals. Id. Glycosylation can affect inter alia a protein’s three-dimensional structure. See Alberts, supra, at 702. “The three dimensional structure of a protein reflects its primary structure (amino acid sequence), secondary structure (localized folding of parts of the polypeptide chain), and tertiary structure (long-range folding).” Lodish Deck ¶ 18. Amgen’s patents teach EPO by reference to recombinant EPO’s primary structure without mentioning the other aspects of structure potentially affected by glycosylation. B. Amgen Claimed Its Patents By RefERENCE TO EPO’S AMINO ACID SequenCE Amgen obtained a total of seven product and process patents by reference to the amino acid sequence. As the Court noted in claim construction, “[t]he patent itself is silent as to ... any structural characteristic beyond the required amino acid sequence.” Amgen Markman, 494 F.Supp.2d at 63. The specification: does not define “erythropoietin” by reference to the presence or absence of any attached molecules, such as the carbohydrate that can be attached to EPO proteins for glycosylated EPO. In fact, the specification expressly contemplates that additional molecules may be attached to “human erythropoietin.” By implication, therefore, those additional molecules are not part of the amino acid structure that comprises the claimed product. Id. (internal citation omitted). It follows that modifications not affecting the amino acid sequence are immaterial. C. The Market for Erythropoiesis Stimulating Agents (“ESAs”) Since obtaining its patents, Amgen has developed two drugs to treat anemia and anemia-related diseases, EPOGEN and Aranesp. Anemia can result from excessive loss of blood, from chemotherapy in cancer patients (because some chemotherapeutic agents destroy not only cancer cells, but also the bone marrow where blood cell formation occurs), and from chronic kidney disease (“CKD”), a progressive decline in kidney function leading to the buildup of waste products in the blood. Bernheim Expert Rep. ¶ 25. Patients with 85-95% loss of kidney function are said to experience end-stage kidney failure, commonly called end-stage renal disease (“ESRD”). Chertow Expert Rep. ¶¶ 16-17. Available in the United States since the 1960s, dialysis removes waste products in the blood of ESRD patients whose kidneys cannot perform that function on their own. Id. ¶ 18. Although dialysis cleanses a patient’s blood, it does not aid production of erythropoietin. Id. While the development of dialysis treatments in the 1960s likely extended the lives of many ESRD patients, the anemia in these people persisted, resulting in symptoms of weakness, fatigue, and lack of energy, requiring either patient acceptance of continued morbidity or some form of treatment. Id.; Fishbane Expert Rep. ¶ 20. Recombinant EPO met the previously unmet needs of CKD and ESRD patients for an erythro-poiesis stimulating agent. In 1989, Amgen launched epoetin alfa, or EPOGEN, which served both CKD and ESRD patients. In the mid-1990s, Am-gen developed a second-generation ESA, darbepoetin alfa, branded Aranesp. Bern-heim Expert Report ¶ 35. The key difference between these drugs is how frequently patients must take them. For patients receiving epoetin alfa (EPOGEN) two to three times per week and switching to Aranesp, the label provides that Aranesp be administered either subcutaneously or intravenously once weekly. For patients initiating treatment for correction of anemia, the recommended dosing is also one administration per week. For maintenance patients who had been receiving EPOGEN once per week, however, the label provides that Aranesp can be administered once every two weeks. Fishbane Expert Rep. ¶ 24. Although the Aranesp label does not provide for less frequent dosing than once every two weeks, for some CKD patients there is off-label usage at once per month. Id.; Chertow Expert Rep. ¶ 19. Anemia drugs are sold in two markets, CKD and ERSD, based upon patient need. In the United States, Amgen markets Ara-nesp primarily for use in the CKD market segment and markets EPOGEN primarily for use by ESRD patients. Remedy Trial Tr. vol. 1 [Doc. 1737] at 44-46; Berheim Expert Rep. ¶ 37. With the exception of Johnson & Johnson, which obtained limited market entry via a license agreement, Amgen, by virtue of its patents, has a monopoly over both markets. In 2006, annual net sales of Aranesp in the United States were over $2,800,000,000, greater than those of EPOGEN and the Johnson & Johnson drug, Procrit, which each had annual sales of approximately $2,400,000,000. Bernheim Expert Rep. ¶ 37. D. Production of MIRCERA Roche sought to break Amgen’s monopoly by introducing MIRCERA into the market of ESAs. CERA, the active ingredient in MIRCERA, is an acronym for Continuous Erythropoietin Receptor Activator, referring to the fact that CERA has a longer half-life than either darbepoetin alfa (Aranesp) or epoetin alfa (EPOGEN or Procrit). Fishbane Expert Rep. ¶ 30. While Aranesp has been approved only for dosing every two weeks, MIRCERA received FDA approval to provide correction of anemia with once-every-two-week dosing and to maintain stable hemoglobin levels with once-monthly or once-every-two-week dosing in all CKD patients. As shall be described below, Roche formed MIRC-ERA by attaching a sugar to EPO in order to extend the protein’s half-life in the body. 1. The active ingredient in MIRC-ERA, CERA, is formed via a chemical reaction that bonds PEG to EPO MIRCERA is the branded name for me-thoxy polyethylene glycol-epoetin beta. Epoetin beta, the starting ingredient for CERA, is a protein that is materially indistinguishable from the EPO in EPOGEN or Aranesp. See Lodish Decl. ¶ 41 (“Roche’s manufacturing process for producing the recombinant EPO in [CERA] closely tracks the teachings of Example 10 of Amgen’s [p]atents.”). Like Amgen’s EPO, epoetin beta is a recombinant EPO formed by injecting DNA encoding human EPO into a CHO cell. Id. ¶ 42 (citing Ex. 8 at ITC-R-BLA-000046667). And, like Am-gen’s EPO, “[t]he resulting glycosylated human EPO polypeptide product contains the identical amino acid sequence as naturally occurring human EPO.” Id. ¶ 47. In order to form CERA, Roche subjects epoetin beta to a chemical reaction with a polyethylene glycol polymer (“PEG”), id. ¶ 48, attaching PEG to epoetin beta at one of “9 potential pegylation sites on human EPO — the N-terminal amino group [or one of] the 8 epsilon-amino groups of lysines.” Id. ¶ 52. The net result of the reaction is “a single bond between one carbon atom of [the PEG] molecule and one amino nitrogen of EPO.” Id. ¶ 50. According to Roche’s own analysis, pegylation does not affect epoetin beta’s amino acid sequence, glycosylation, or carbohydrate structure. Trial Tr. at 2743; see also Lodish Decl. ¶ 53. Prior to marketing or this litigation, Roche referred to CERA as peg-EPO. See Trial Tr. at 2738-40. Pegylation — the attachment of PEG to a protein — is a familiar technique in the pharmaceutical and cosmetic industry. PL’s Stat. Undisp. Mat. Facts ¶40. In theory, the addition of PEG, an inert polymer, to a therapeutic protein, such as EPO, can expand the drug’s life in the body and reduce levels of toxicity, allowing for extended dosing intervals. Id. ¶¶ 39-40; Lodish Decl. ¶ 31. The technique was first employed as early as 1977, and EPO is only one of a number of human proteins that have been pegylated. Lodish Decl. ¶ 30. II. OBVIOUSNESS DOUBLE PATENTING Since the inception of the Republic, our patent system “has been about the difficult business ‘of drawing a line between the things which are worth to the public the embarrassment of an exclusive patent, and those which are not.’ ” Bonito Boats, Inc. v. Thunder Craft Boats, Inc., 489 U.S. 141, 148, 109 S.Ct. 971, 108 L.Ed.2d 118 (1989)(quoting 18 WRITINGS of Thomas JeffeRSON 335 (Memorial ed.1904)). Codified at 35 U.S.C. §§ 102(a)-(b), the novelty requirement reflects Congress’s determination that the public will not pay the dear price of a 17-year monopoly for information that is already available to the public. See id. “The nonobviouness requirement extends the field of un-patentable material beyond that which is known to the public under § 102, to include that which could readily be deduced from publicly available material by a person of ordinary skill in the pertinent field of endeavor.” Id. at 150, 109 S.Ct. 971. Obviousness double patenting (“ODP”) is a judicially devised species of obviousness that prevents inventors from over-extending the term of exclusivity by patenting subtle variations of the same device. Applied Materials, Inc. v. Advanced Semiconductor Materials Am., Inc., 98 F.3d 1563, 1568 (Fed.Cir.1996). At summary judgment, Roche invoked ODP, averring that the claims-in-suit were obvious over claim 10 of the '016 patent because it contained the term “erythro-poietin from a mammalian cell culture supernatant fluid.” See Mem. Supp. Sum. J. of ODP Over '016 [Doc. No. 491] at 1-2; see also Mot. Summ. J. Of ODP Over '016 [Doc. 490]. Amgen then moved for summary judgment of no ODP over both the '016 and '008 patents [Doc. No. 498], Without explanation, the Court denied Roche’s motion for summary judgment but granted Amgen’s cross-motions for summary judgment for no obviousness-type double patenting on the eve of trial. The Court now writes to explain that decision. The Court determined that the two-way test was applicable to the '016 claims because the '016 patent disclosed a follow-on invention that issued after the underlying claims due to a restriction order imposed by the Patent and Trade Office (“PTO”). Applying the two-way test, the claims-in-suit were not obvious over claim 10 of the '016 patent because the metes and bounds of the claim are readily discernable without reference to the specification and are clearly drawn to a seven-step process for purifying EPO. Claim 10 is clearly not drawn to the protein itself or to the process of its production. In addition, because the order in which Amgen’s patents issued was a function of a restriction requirement imposed by the PTO, and because the claims at issue are consonant with those restrictions, the claims of the '933, '422, and '349 patents are immune from ODP over the '008 patent under the terms of 35 U.S.C. § 121. A. The Legal Framework An ODP inquiry is comprised of two steps. “First, as a matter of law, a court construes the claim in the earlier patent and the claim in the later patent and determines the differences. Second, the court determines whether the differences in subject matter between the two claims render the claims patentably distinct.” Eli Lilly and Co. v. Barr Labs., Inc., 251 F.3d 955, 968 (Fed.Cir.2001)(internal citations omitted). Defendants who seek to invalidate a particular claim via ODP must prove by clear and convincing evidence that the original claim and the allegedly duplicative claim are not patent-ably distinct. Symbol Techs., Inc. v. Opti- con, Inc., 935 F.2d 1569, 1580 (Fed.Cir.1991). It is also important to note that where the metes and bounds are discerna-ble from the face of the claim, the ODP inquiry focuses on what is claimed without reference to the disclosure. See General Foods Corp. v. Studiengesellschaft Kohle mhH, 972 F.2d 1272, 1281 (Fed.Cir.1992)(“[T]he disclosure of a patent cited in support of a double patenting rejection cannot be used as though it were prior art, even where the disclosure is found in the claims.”) (emphasis in original). 1. The “One-Way” and “Two-Way” Tests There are two ways that a court can conduct the ODP analysis. In most cases, courts employ a “one-way” test where the court compares the claims according to the order in which the patents issued. “A later claim that is not patent-ably distinct from an earlier claim in a commonly owned patent is invalid for obvious-type double patenting.” Eli Lilly, 251 F.3d at 968. If the scope of the application and the patent claims is not identical, the court must ask whether the later patent’s claim defines merely an obvious variation of the earlier patent’s claim. See In re Goodman, 11 F.3d 1046, 1052 (Fed.Cir.1993). Although the one-way test applies in the large majority of cases, the Federal Circuit created a “two-way” test that applies in a narrow set of circumstances. In re Berg, 140 F.3d 1428, 1432 (Fed.Cir.1998). The two-way test is a response to the reality that the Patent Office is perennially underfunded and slow. See id. These indisputable facts cause various anomalies, including the issuance of patents in an order other than that which the inventor intended. In rare cases, quirks in the application process may cause a patent covering a subsequently conceived follow-on invention to issue before the patent covering the underlying invention. The two-way test seeks to prevent rejections for obviousness-type double patenting when the applicants filed first for a basic invention and later for an improvement, but, through no fault of the applicants, the PTO decided the applications in reverse order of filing, rejecting the basic application although it would have been allowed if the applications had been decided in the order of their filing. Id. Where patents have issued out of order, the examiner will employ the one-way test, but “the examiner also asks whether the patent claims are obvious over the application claims. If not, the application claims later may be allowed.” Id. In this case, Amgen asks the Court to apply the two-way test. The determination of whether the one-way or two-way test applies is matter of law. Id. The two-way test must be used if: (1) the applicant could not have filed both claims together in the earlier-filed application; and (2) the applicant did not cause the later filed claim to issue first by delaying examination of the earlier-filed claim during the period when both applications were pending before the PTO (the “co-pendency period”). See, e.g., In re Emert, 124 F.3d 1458, 1461 (Fed.Cir.1997); Engineered Prods. Co. v. Donaldson Co., 225 F.Supp.2d 1069, 1111 (N.D.Iowa 2002), vacated in part on other grounds, 147 Fed.Appx. 979 (Fed.Cir.2005). 2. The Safe Harbor Provision, 35 U.S.C. § 121 The two-way test is not the only mechanism devised to protect inventors from inadvertent inequities arising from the PTO’s application process. Congress enacted a safe harbor, codified at 35 U.S.C. § 121, which provides: If two or more independent and distinct inventions are claimed in one application, the Director may require the application to be restricted to one of the inventions. If the other invention is made the subject of a divisional application which complies with the requirements of section 120 of this title it shall be entitled to the benefit of the filing date of the original application. A patent issuing on an application with respect to which a requirement for restriction under this section has been made, or on an application filed as a result of such a requirement, shall not be used as a reference either in the Patent and Trademark Office or in the courts against a divisional application or against the original application or any patent issued on either of them, if the divisional application is filed before the issuance of the patent on the other application. B. The Prosecution History Reveals THAT THE PTO, NOT AMGEN, DICTATED the Order or Form in which its Patents Issued Dr. Lin filed U.S. Patent Application No. 06/675,298 on November 30, 1984. See Moore Decl. [Doc. No. 501] Ex. H-1, U.S. Patent Application No. 06/675,298, at AM670167625. On June 20, 1985, two other Amgen researchers, Drs. Lai and Strickland, filed U.S. Patent Application No. 06/747,119. Claim 10 of the '119 application is drawn to a specific seven-step process for purifying recombinant EPO. See Lodish Deck [Doc. No. 502] ¶ 48. The claim does not describe a product or teach a process for producing EPO from mammalian cells. Lodish Deck ¶44. It is undisputed that Drs. Lai and Strickland did not conceive of the process described in the '119 application until after Dr. Lin filed the '298 application. See Strickland Deck [Doc. No. 503] ¶¶ 11-16. On July 3, 1986, shortly after Drs. Lai and Strickland filed the '119 application, the PTO imposed a restriction requirement on the '298 application. Pursuant to 35 U.S.C. § 121, the PTO mandated that Amgen divide the claims in the '298 application into distinct groups based on subject matter: I) polypeptides; II) DNA; III) plasmids; IV) cells; V) pharmaceutical composition; and VI) assay. See Lodish Deck ¶ 17. As a result of the restriction requirement, Amgen elected to allow its DNA (restriction Group II) claims to proceed to examination in the '298 application. Id. ¶ 20. All of the elected claims fit into restriction Group II. See Lodish Deck ¶ 25. In addition, on October 23, 1987, Amgen filed two divisional applications, U.S. Patent Application Nos. 07/113,178 and 07/113,179. All of the claims in the '178 and '179 applications were taken from the '298 application. See Pb’s Stat. Undisp. Mat. Facts [Doc. No. 500] ¶¶ 4-5. The '178 application contained claims drawn to a polypeptide (restriction Group I) and a pharmaceutical composition (restriction Group VI). See Moore Deck Ex. I, U.S. Patent Application No. 07/113,178, at AM-ITC 00941037-45, AM-ITC 00941076-77; Moore Deck Ex. H-8, Office Action, July 3, 1986, at 2. The '179 application included claim 1 from the '298 application, which was placed in restriction Group I. See Moore Deck Ex. J, U.S. Patent Application No. 07/113,179 at AM-ITC 004539820-90, AM-ITC 00454000-01; Moore Deck Ex H-8, Office Action, July 3, 1986, at 2. On May 19, 1987, while Amgen and the PTO were still sorting Amgen’s applications into restriction groups, Drs. Lai and Strickland’s '119 application issued as U.S. Patent No. 4,667,016. Ph’s Stat. Undisp. Mat. Facts ¶ 9. The '298 application issued as U.S. Patent No. 4,703,008, but not until October 27, 1987, see id. ¶ 1, four days after Amgen filed the '178 and '179 applications, see id. ¶¶ 4-5. The '178 and '179 applications subsequently issued as the '933, '349, and '422 patents. The claims in these patents are not drawn to restriction Group II. See Lodish Decl. ¶¶ 26-34. C. The Court Granted Amgen’s Motion for Summary Judgement and Denied Roche’s Because There Was No Genuine Issue of Material Fact THAT THE CLAIMS-IN-SuiT WERE Not Invalid for ODP Over the '016 Patent Claims Roche moved for summary judgment on the ground that claim 10 of Drs. Lai and Strickland’s '016 patent rendered the claims-in-suit obvious because claim 10 contains the term “recombinant erythro-poietin from a mammalian cell culture supernatant fluid.” See Def.’s Mem. Supp. Sum. J. at 1-2. As shall be explained, the Court must employ the two-way test in evaluating this claim because the '016 patent was a subsequently conceived follow-on invention that issued before the claims-in-suit due to the PTO’s imposition of the 1986 restriction requirement. Under the two-way test, it is clear that claim 10 of the '016 patent and the claims-in-suit are not identical in scope. They are in fact drawn to very different subject matter, and the differences are not merely obvious variations. As a threshold matter, it is important to note that when deciding a motion for summary judgment, the Court “must view the evidence presented through the prism of the substantive evidentiary burden.” Anderson v. Liberty Lobby, Inc., 477 U.S. 242, 254, 106 S.Ct. 2505, 91 L.Ed.2d 202 (1986). Here, Roche bears the burden of proving ODP by clear and convincing evidence, “a heavy and unshifting burden.” Symbol Techs., 935 F.2d at 1580. Moreover, since the PTO — on two separate occasions — rejected Roche’s ODP argument and determined that Dr. Lin’s claims are patentably distinct from the '016 claims, Roche bears an even heavier burden in proving ODP based on the '016 claims. See Amgen I, 126 F.Supp.2d at 105 (Where the asserted grounds for invalidity were reviewed by the PTO, “the challenger has the added burden of overcoming the deference that is due to a qualified government agency presumed to have properly done its job.”) (internal quotation omitted). Roche cannot overcome that burden. 1. The two-way test applies in evaluating whether the claims-in-suit are invalid over the claim 10 of the '016 patent While courts generally apply the “one-way” test, the Federal Circuit has recognized special circumstances in which the “two-way” test is to be applied. Eli Lilly, 251 F.3d at 968-969. The two-way test should apply where an underlying claim and a follow-on claim issue in reverse order through no fault of the paten-tee. See In re Berg, 140 F.3d at 1432. In order to apply the two-way test, the Court must determine that Amgen (1) could not have filed the '119 application together with the '298 application and (2) did not cause the '016 patent to issue first by delaying examination of the '298 application during the co-pendency period. See id.; see also In re Emert, 124 F.3d at 1461; Engineered Prods., 225 F.Supp.2d at 1111. The Court was satisfied that both of these criteria were met. As noted above, the first filing involved Lin’s invention of recombinant EPO as described in the '298 application. See Moore Decl. Ex. H-l, U.S. Patent Application No. 06/675,298, at AM670167625. Even though the '016 patent issued prior to the claims in suit, the undisputed record reveals that Lai & Strickland’s EPO purification process was a subsequently conceived follow-on invention. See Strickland Decl. ¶¶ 11-16. Thus, it was impossible for Amgen to have filed claim 10 of the '016 patent as part of Lin’s November 30, 1984 '298 application that gave rise to the claims-in-suit. Roche does not dispute this fact, but contends that it is sufficient that the '016 claims and Dr. Lin’s claims could have been combined together in a continuation-in-part application filed some time after Dr. Lin’s earlier filed '298 application. See Def.’s Mem. Supp. Sum. J. at 14. This argument rests on Roche’s contention that the '119 application (from which the '016 patent claims priority) constitutes the “earlier filed application.” The undisputed facts, however, are that the claims-in-suit claim priority from the '298 application. Thus, Dr. Lin’s '298 application, filed November 30, 1984, is the one deemed “earlier filed” as compared to the '119 application, which was not filed until June 20, 1985. See 35 U.S.C. § 120. Therefore, the first requirement of the two-way test is satisfied. Second, Amgen did not delay examination of Dr. Lin’s earlier-filed '298 application during the “co-pendency” period or cause the later-filed '016 patent to issue before Dr. Lin’s patents-in-suit. Dr. Lin’s '298 application was filed on November 30, 1984. Moore Decl. Ex H-l, U.S. Patent Application No. 06/675,298, at AM67067625. The patents-in-suit issued between 1996 and 1999. See U.S. Patent No. 5,547,933 (issued August 20, 1996); U.S. Patent No. 5,756,349 (issued May 26, 1998); U.S. Patent No. 5,955,422 (issued September 21, 1999). The '119 application was filed on June 20, 1985, and the '016 patent issued on May 19, 1987. See U.S. Patent No. 4,667,016. Thus, the relevant co-pendency period is from June 20, 1985 (the '016 filing date) to May 19, 1987 (the '016 issuance date). During the co-pen-dency period, Amgen did not request or receive any extensions of time to prosecute Dr. Lin’s '298 application, nor did it delay examination of the '298 application in any other manner to cause the '016 patent to issue first. Instead, the record suggests that Amgen made efforts to accelerate examination of the '298 application. See, e.g., Moore Decl. Ex. H-5, Petition to Make Special. Thus, it was the PTO, not Amgen, that caused the later-filed '016 patent to issue before Dr. Lin’s '298 application. The Court therefore will apply the two-way test. 2. Roche’s argument that the '016 patent discloses “purified recombinant EPO” fails because ODP analysis is confined to an examination of the claim At its essence the ODP inquiry asks: “Is the same invention being claimed twice?” Gen. Foods, 972 F.2d at 1278. Claim 10 of the '016 patent is drawn to a seven-step process for recovering a purified recombinant EPO. Claim 10 does not purport to teach the production of recombinant EPO. Lodish Decl. ¶ 44. “Recombinant erythropoietin” is a different invention than the recovery process taught in claim 10. The Court must therefore conclude that the scope of claim 10 is not identical to the scope of the claims-in-suit. See In re Goodman, 11 F.3d at 1052. Despite Roche’s urging, the Court cannot conclude that these differences are obvious. Roche’s argument that claim 10 is obvious over the claims-in-suit because it contains the term “recombinant erythropoietin” is premised on the fatally flawed assumption that the Court must look to '016 patent specification — including the earlier teachings of Dr. Lin’s own patent application as incorporated by reference in the '016 specification — as though they both constituted prior art to Dr. Lin’s '298 patent claims. To the contrary, the Federal Circuit has made clear that “[d]ouble patenting is altogether a matter of what is claimed.” Gen. Foods, 972 F.2d at 1277. “[T]he disclosure ... cannot be used as though it were prior art, even where the disclosure is found, in the claims.” Id. at 1281 (emphasis in original); see also In re Braat, 937 F.2d 589, 594 n. 5 (Fed.Cir.1991). As the Court of Customs & Patent Appeals explained in In re Aldrich, 55 C.C.P.A. 1431, 398 F.2d 855 (C.C.P.A.1968): Obviousness-type double patenting rejections ... are based on the premise that an applicant is claiming no more than an obvious variation — which would be obvious to anyone of ordinary skill in the art — of an invention on which a patent has already been granted.... To that end, patent claims are looked to only to see what has been patented, the subject matter which has been protected, not for something one may find to be disclosed by reading them. Id. at 859. Thus, the '016 patent and Dr. Lin’s application incorporated therein are not prior art for purposes of the two-way ODP analysis. In fact, Dr. Lin’s patent applications were not publicly disclosed or available as prior art as of the date of the Lai & Stickland EPO purification invention reflected in the '016 patent (the legally relevant date for the ODP analysis). As far as the ordinarily skilled artisan at the time was concerned, there was no “recombinant erythropoietin.” Nevertheless, in support of its argument that the Court ought look to the specification, Roche relies on Geneva Pharmaceuticals, Inc. v. GlaxoSmithKline PLC, 349 F.3d 1373 (Fed.Cir.2003). In Geneva the Federal Circuit analyzed the claims’ scope and utility ,by looking not only to the claims themselves but also to the specifications. The Federal Circuit explained: [T]his court does not consider the Fleming claim in a vacuum, as a simple compound, without considering the compound’s disclosed utility.Standing alone, that claim does not adequately disclose the patentable bounds of the invention. Therefore, this court examines the specifications of both patents to ascertain any overlap in the claim scope for the double patenting comparison. A person of ordinary skill in the art reviewing the disclosure of the Fleming patent would recognize a single use for potassium clavulanate, administration to patients to combat bacteria that produce [betaj-lactamase.... The Fleming patent discloses no other use. The '720 patent simply claims that use as a method. Id. at 1385 (emphasis added)(internal citations omitted). Geneva is inapposite. Here, unlike Geneva, the limitations adequately set forth the metes and bounds of the claim. And it is clear that the claim is drawn to a particular purifying recombinant EPO that has already been produced. The claim does not describe the polypeptide or the process by which it is made. Geneva is inapplicable because the sole utility of the '016 patent is purifying EPO for the patents in suit. In fact, even if Roche is right that the '016 and the current patents literally overlap — all mentioning EPO — it does not follow that the patents in suit are the “single use” for EPO. Thus, claim 10 and the claims-in-suit are patentably distinct. On the basis of this conclusion, the Court denied Roche’s motion for summary judgment on ODP [Doc. No. 490] with respect to the '016 patent and granted Amgen’s [Doc. No. 498]. D. The Court GraNted Amgen’s Cross Motion for Partial Summary Judgment of No ODP Over the Claims in the '008 Patent beoause Amgen was Entitled to the Safe Harbor Codified at 35 U.S.C. § 121 The third sentence of 35 U.S.C. § 121 provides: A patent issuing on an application with respect to which a requirement for restriction under this section has been made, or on an application filed as a result of such a requirement, shall not be used as a reference either in the Patent and Trademark Office or in the courts against a divisional application or against the original application or any patent issued on either of them, if the divisional application is filed before the issuance of the patent on the other application. The applicability of this safe harbor provision is matter of law. “In addition to the express requirements of section 121, [the Federal Circuit has] construed the statute to require consonance: the applicant must maintain the line of demarcation between the independent and distinct inventions that prompted the restriction requirement.” Pfizer, Inc. v. Teva Phams. USA Inc., 518 F.3d 1353, 1359 (Fed.Cir.2008). Thus, the Court must determine 1) whether the three applications at issue were in fact filed in response to a PTO imposed restriction requirement; and 2) whether Amgen remained faithful to the restriction requirements. As set forth below, the Court concludes that Amgen has satisfied both the statutes strictures as well as the consonance requirement. 1. Amgen filed the '178 and '179 applications in response to the PTO-imposed restriction requirement After the PTO imposed the 1986 restriction requirement, Amgen restricted the claims prosecuted in Dr. Lin’s '298 application to one invention (Lin’s DNA claims), which ultimately issued as the '008 patent. It filed two divisional applications, the '178 and '179, which ultimately issued as the '933, '422, and '349 patents. The undisputed evidence shows that both the '178 and '179 applications were filed as a result of the PTO’s 1986 restriction requirement. Thus, Amgen has met its burden with respect to the first part of the safe harbor inquiry. The Court now considers whether Amgen maintained consonance. 2. Amgen satisfied the consonance requirement As noted above, claims in a divisional application are only immune from an obviousness-type double patenting rejection when strict consonance exists between the earlier restriction requirement and the claims later prosecuted. Bristol-Myers Squibb Co. v. Pharmachemie B.V., 361 F.3d 1343, 1348 (Fed.Cir.2004); Geneva Pharms., Inc. v. GlaxoSmithKline PLC, 349 F.3d at 1381; Gerber Garment Tech., Inc. v. Lectra Sys., Inc., 916 F.2d 683, 688 (Fed.Cir.1990). “Consonance requires that the line of demarcation between the ‘independent and distinct inventions’ that prompted the restriction requirement be maintained.... Where that line is crossed the prohibition of the third sentence of Section 121 does not apply.” Gerber, 916 F.2d at 688. “[N]ew or amended claims in a divisional application are entitled to the benefit of [section] 121 if the claims do not cross the line of demarcation drawn around the invention elected in the restriction requirement.” Symbol Techs., 935 F.2d at 1579. In delineating the scope of the groups, the proper point of reference is the actual restriction groupings (i.e., the substance of the claims in each restriction group), not the examiner’s written descriptions thereof. Texas Instruments Inc. v. ITC, 988 F.2d 1165, 1179 (Fed.Cir.1993). Here, the '933, '349 and '422 patent claims are consonant with the PTO’s 1986 restriction requirement. See Pl.’s Rep. Br. Supp. Sum. J. No ODP [Doc. 676] at 3-12. Under 35 U.S.C. § 121, the 1986 restriction requirement mandated that Amgen confine its inventions to the following groups: I. Claims 1-13, 16, 39-41, 47-54 and 59, drawn to polypeptide, classified in Class 260, subclass 112. II. Claims 14, 15, 17-36, 58 and 61-72, drawn to DNA, classified in Class 536, subclass 27. III. Claims 37-38, drawn to plasmid, classified in Class 435, subclass 240. ' IV. Claims 42-46, drawn to cells, classified in Class 435, subclass 240. V. Claims 55-57, drawn to pharmaceutical composition, classified in Class 435, subclass 177. VI. Claim 60, drawn to assay, classified in Class 435, subclass 6. Lodish Decl. Ex. E-l, '298 Prosecution, Paper 8 at 2. Amgen elected claims falling within restriction Group II for further examination in the '298 application. See Lodish Decl. ¶ 20. Amgen then filed the '178 and '179 applications by submitting a copy of the '298 application (as originally filed) and canceling certain of the '298 claims so that only subsets of those claims were included in the '178 and '179 applications as filed. See Moore Decl. Ex. P-1, Patent and TRADEMARK OFFICE, MANUAL OF PATENT EXAMINING Proceduee § 201.06(a) (5th Ed.1983) (outlining regulations for “[e]on-tinuing or divisional application^] for invention disclosed in a prior application”). In keeping with the 1986 restriction requirement and the election of Group II, Amgen canceled all claims belonging to Group II and selected only claims belonging to the non-elected restriction groups for filing in the '178 and '179 applications. The '178 application as filed contained original claims 1-13, 16, 39-41, 47-49, and 55-57, which the PTO had assigned to restriction Groups I and V. See Moore Decl. Ex. I, U.S. Patent Application No. 07/113,178, at AMITC 00941037-45, AM-ITO 00941076-77; Moore Decl. Ex H-8, Office Action, July 3, 1986, at 2. The '179 application as filed contained original claim I, which the PTO had assigned to restriction Group I. See Moore Decl. Ex. J, U.S. Patent Application No. 07/113,179 at AM-ITC 004539820-90, AM-ITC 00454000-01; Moore Decl. Ex H-8, Office Action, July 3, 1986, at 2. The Court is satisfied that Amgen complied with the restriction requirements. To begin, the '298 claims, which issued as the '008 patent, fall within elected Group II. Lodish Decl. ¶ 25. Moreover, the claims-in-suit fall within the scope of the non-elected restriction groups. '933 claims 1-8 (EPO glycoproteins and glyco-protein products) are drawn to “polypeptide”; '933 claims 9-14 and '422 claims 1-2 (pharmaceutical compositions and methods of using same) are drawn to “pharmaceutical composition”; and '349 claims 1-7 (vertebrate cells for producing EPO and processes for using same) fall within the scope of Group IV because they are drawn to “cells.” See id. ¶¶ 26-34. None of these claims cross the line of demarcation drawn around the elected Group II. See id. Roche argues that Amgen cannot avail itself of section 121’s safe harbor because its prosecutions were not consonant with the restriction requirement. First, Roche contends that Amgen broke consonance by prosecuting claims from Group I and Group V in a single application. Def.’s Mem. Opp. Sum. J. Of No ODP [Doc. No. 568] at 2. Similarly, Roche maintains that during the prosecution of the '422 patent Amgen broke consonance by combining claims from Group V and Group VII in the same application. Id. In addition, Roche avers that Amgen vitiated the restriction requirement by claiming a “non-naturally occurring glycoprotein” in claim 7 of the '933 patent. See id. Finally, Roche contends that Amgen violated the restriction requirement by converting verbrate cell claims into a process claim during the prosecution of the '349 patent. Id. The process claims of the '349 patent, Roche argues, belong in the elected Group II. See id. To begin, Roche’s argument that Amgen broke consonance by including claims in multiple restriction groups in the same application lacks legal foundation. Under Roche’s theory, Amgen was required to maintain strict consonance by filing a divisional application for claims within each restriction group. Roche cites no case for this proposition. The reason they are unable to do so is that the available Federal Circuit precedent indicates that “new or amended claims in a divisional application are entitled to the benefit of [section] 121 if the claims do not cross the line of demarcation drawn around the invention elected in the restriction requirement.” Symbol Techs., 935 F.2d at 1579. Roche does not allege that the '933 or '422 claims blurred the line of demarcation around the elected Group II. Thus, the Court cannot conclude that the '422 and '933 forfeited the shelter provided by section 121. Roche’s claim that the '933 patent broke consonance by claiming a non-naturally occurring glycoprotein is also unpersuasive. Roche argues that the only polypeptides that satisfy the strictures of Group I are those that are isolated from a natural source; the “non-naturally occurring gly-coprotein” taught in claim 7, Roche emphasizes, can only be obtained with recombinant DNA. Roche maintains that once Amgen modified gylcoprotein with “non-naturally occurring” the claim was no longer drawn to a polypeptide (Group I)) but instead to a DNA sequence (Group II). Were the Court’s examination confined solely to the Examiner’s written description of the groups, Roche’s argument would have considerable force. The rela-vant line of demarcation, however, is “the grouping restriction actually imposed by the examiner.” Texas Instruments, 988 F.2d at 1179. Roche does not dispute that the Examiner assigned some claims to Group I that were from non-naturally occurring sources. Thus, the Court cannot conclude that the inclusion of the term “non-naturally occurring” broke consonance. Finally, Roche contends that Amgen broke consonance by separating the '349 patent into Group IV. Roche maintains that the '349 patent belongs in Group II because Amgen added claim 7, a claim drawn to the recombinant process of using vertebrate cells to produce EPO. Roche is mistaken. As noted above, restriction Group II was comprised of claims drawn to DNA, while Group IV was drawn to cells. Lodish Decl. ¶¶23, 29. The mere addition of a process claim does not transform a Group IV claim into a Group II claim. As Amgen notes, “only 4 of the 35 claims assigned to Group II were process claims.” PL’s Rep. Br. Supp. Sum. J. No ODP at 9. Moreover, the common feature of the Group II claims is that they “require[] a specific, purified, and isolated DNA sequence, encoding either human or monkey erythropoietin or an analog polypeptide related to erythropoietin in both structure and function.” Lodish Decl. ¶ 21. Claims 1-3, referenced in the process taught in claim 7, merely require that the EPO DNA in the vertebrate cells “be transcriptionally controlled by ‘non-human DNA sequences.’ ” Lodish Decl. ¶ 30. In short, because the focus remains on the cells, the inclusion of claim 7 does not cause the '349 claim to stray over the line of demarcation into Group II. Accordingly, on the record before the Court, there were no genuine issues of fact to be decided and, thus, the Court granted Amgen’s motion for summary judgment and held that Section 121 “insulates the ensuing patents from the charge of double patenting.” Applied Materials, 98 F.3d at 1568. Given these rulings, the Court believed that it had put paid to the ODP issues in this case. The Court was wrong. After extensive argument during the final pretrial conference, Roche convinced the Court that there remained genuine issues of material fact for trial upon what the parties came to call Roche’s theories 3 and 4. E. FINDINGS AND RlJLINGS AFTER TRIAL And so the trial came. The Court was somewhat surprised (and concerned) that Roche focused heavily in its opening to the jury on double patenting issues, as though this were some sort of equitable defense. 1. Jury or Non-jury? After careful reflection, the Court ruled on September 7, 2007 that obviousness double patenting ought not be submitted to the jury. “Determining what is patented by correct claim interpretation is essential to [the] determination of obviousness-type double patenting issues.” Gen. Foods, 972 F.2d at 1279 (capitalization altered). It is the Court’s role, not the jury’s, to determine the metes and bounds of the claimed inventions. See Markman v. Westview Instruments, Inc., 517 U.S. 370, 384-91, 116 S.Ct. 1384, 134 L.Ed.2d 577 (1996). Accordingly, because “[d]ouble-patenting is altogether a matter of what is claimed,” Gen. Foods, 972 F.2d at 1277, obviousness-type double patenting is an issue for the Court. Other district courts have agreed, ruling that decisions regarding the ODP defense should be made by a judge, not a jury. See, e.g., Engineered Prods., 313 F.Supp.2d at 993 (“[T]he double-patenting defense will be tried to the court because it is a question of law.”); Applera Corp. v. MJ Research Inc., 363 F.Supp.2d 261, 262 (D.Conn.2005) (explaining that the Court reached “findings of fact and conclusions of law” regarding ODP based upon, inter alia, deposition testimony not introduced at trial as well as evidence submitted at trial). For these reasons, the Court here concluded that the ODP issue presented a matter for the Court. After conducting hearings outside the presence of the jury, the Court carefully reviewed both ODP arguments that Roche put forward on the basis of the entire trial record. For purposes of simplicity the Court and the parties referred to these arguments as theories number 3 and 4. The Court presents its findings and rulings below. 2. Roche’s Theory Number 3 Roche’s theory number three argues that the asserted '868 and '698 claims are invalid for ODP over the '008 claims. The parties agree that the safe harbor provision delineated in section 121 does not apply to these claims. See, e.g., Resp. to Roche’s Proposed Findings and Conclusions [Doc. 1628] ¶ 5. In order for section 121 to apply, the '868 and '698 patents would have to derive from a patent application that was subject to a restriction requirement; furthermore, the claims of the '868 and the '698 patents would have to address an invention distinct from the elected invention prosecuted by way of the original application. See, e.g., Gerber, 916 F.2d at 688. Here, however, both the '008 claims and the asserted claims of the '868 and '698 patents fall within Group II of the PTO’s 1986 Restriction Requirement. Therefore, because section 121 does not apply as between patents that contain claims belonging to the same restriction group, no safe harbor protection exists. When a claim is not immunized from allegations of obviousness-type double-patenting due to section 121, the question becomes whether the defendant has met its burden of proving the ODP defense. As with other affirmative defenses of invalidity, the defendant bears the burden of proving ODP by clear and convincing evidence. Symbol Techs., 935 F.2d at 1580. As described part III.A, the ODP analysis entails two steps. First, the Court construes the claims and determines whether there are any differences. Eli Lilly, 251 F.3d at 968. Second, to the extent that differences exist, the Court must determine whether the distinctions are sufficient to render the claims patent-ably distinct. Id. The Court will consider the '868 patent first: [23. A procaryotic or eucaryotic host cell transformed or transfected with a DNA sequence according to claim 7 ... in a manner allowing the host cell to express said polypeptide.] 25. A transformed or transfected mammalian host cell according to claim 24. 27. A transformed or transfected CHO cell according to claim 25. Roche argues that the '008 claims provided: (1) a “mammalian host cell” (2) that is “transformed or transfected” (3) with “a purified and isolated DNA sequence consisting essentially of a DNA sequence encoding a polypeptide having an amino acid sequence sufficiently duplica-tive of that of erythropoietin.” Roche further asserts that '008 claims provide that (4) the cell is transfected in such a way “to allow possession of the biological property” of erythropoietin, which is (5) stimulating red blood cell formation, or “causing bone marrow cells to increase production of reti-culocytes and red blood cells.” Def.’s Mem. on ODP [Doc. 1550] at 14-15. Roche reasons that claim 1 of the '868 patent therefore simply tells one skilled in the art to “take the cells that were claimed in the '008 patent and grow them, let[ting] them do what they normally do.” Id. at 15 (quoting testimony of Dr. Lowe). Similarly, Roche asserts that claim 2 of the '868 patent, which specifically contemplates using CHO cells, is obvious given the fact that the '008 patent also claimed the use of CHO cells. Id. Amgen, on the other hand, argues that the differences between the. patents are “several” and “significant.” PL’s Mem. on No ODP [Doc. 1310] at 40. In particular, Amgen asserts that the '868 patent claims (1) processes for making (2) isolatable quantities of a glycosylated EPO polypeptide (3) having the in vivo biological activity of causing bone marrow cells to increase production of reticulocytes and red blood cells, while the claims of the '008 patent claim only certain DNA molecules and certain cells transformed or transfected with said DNA molecules. Id. (asserting that, unlike the '868 patent, the '008 patent does not “claim a process for producing anything”). In other words, Amgen explains, “the '008 claims are directed to purified and isolated DNA sequences and cells into which such DNA sequences have been introduced. In contrast, the '868 claims 1 and 2 are process claims that recite the steps required to produce a glycosylated polypeptide having specified characteristics.” Id. at 41 (emphasis added). “Unlike the asserted claims of the '868 patent, none of the '008 claims require: (1) that the recited host cell actually express any EPO polypeptide; (2) that the recited host cell actually express a glycosylated EPO polypeptide; (3) that the host cell be capable of producing an isolatable amount of a glycosylated EPO polypeptide; and (4) that any glycosylated EPO isolated from cells grown in culture have the stated in vivo function.” Id. These differences, according to Amgen, render the '868 claims distinct from the '008 claims. The Court agrees. Simply having the starting material (which is reflected in the '008 patent) and knowing that, in theory, it can be used to create proteins is not the equivalent of having an actual process that successfully does so. See id. at 40 (quoting testimony of Dr. Lodish). Roche has failed to meet its burden of demonstrating by clear and convincing evidence that no patentable difference exists between the '008 and '868 patents. Accordingly, the Court finds that the '868 claims are not anticipated by the '008 patent and rules that the '868 claims are d