DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s amendment and remarks filed on 4/13/2026 are acknowledged. Claim 1 is amended. Claim 2 is cancelled. Claims 1 and 3-24 are currently pending.
Election/Restrictions
Applicant’s election of SEQ ID NO:11 in the reply filed on 4/13/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). Claims 3-5 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Claims 1 and 6-24 are currently under examination.
Information Disclosure Statement
The information disclosure statements filed on 7/18/2023, 10/31/2023, and 8/22/2024 have been considered. Signed copies are enclosed.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), first paragraph:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1 and 6-24 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The specification discloses a series of variants with defined sequences that have been tested and found to be alkali stable. However, no variants beyond these are shown to be alkali stable or to even bind to immunoglobulins. Therefore, most of these peptides have no disclosed correlation between their structure and function. The claim requires that the peptide exhibit immunoglobulin binding and alkali stability, but the specification provides no guidance regarding which variants, beyond those specifically disclosed, are capable of the required function. Therefore, the specification provides insufficient written description to support the genus encompassed by the claim. Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that
"applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed." (See page 1117.) The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." (See Vas-Cath at page 1116.)
With the exception of the sequences tested in the specification, the skilled artisan cannot envision the detailed chemical structure of the encompassed polypeptides, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. The nucleic acid and/or protein itself is required. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481, 1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404. 1405 held that:
...To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines Inc. , 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli , 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2datl966.
Protein chemistry is probably one of the most unpredictable areas of biotechnology. Consequently, the effects of sequence dissimilarities upon protein structure and function cannot be predicted. Bowie et al. (Science, 1990, 247:1306-1310; IDS filed 7/18/2023) teach that an amino acid sequence encodes a message that determines the shape and function of a protein and that it is the ability of these proteins to fold into unique three-dimensional structures that allows them to function and carry out the instructions of the genome and further teaches that the problem of predicting protein structure from sequence data and in turn utilizing predicted structural determinations to ascertain functional aspects of the protein is extremely complex (column 1, page 1306). Bowie et al. further teach that while it is known that many amino acid substitutions are possible in any given protein, the position within the protein's sequence where such amino acid substitutions can be made with a reasonable expectation of maintaining function are limited. Certain positions in the sequence are critical to the three dimensional structure/function relationship and these regions can tolerate only conservative substitutions or no substitutions at all (column 2, page 1306). The sensitivity of proteins to alterations of even a single amino acid in a sequence are exemplified by Burgess et al. (J. Cell Biol. 111:2129-2138, 1990; IDS filed 7/18/2023) who teach that replacement of a single lysine reside at position 118 of acidic fibroblast growth factor by glutamic acid led to the substantial loss of heparin binding, receptor binding and biological activity of the protein and by Lazar et al. (Mol. Cell. Biol., 8:1247-1252, 1988; IDS filed 7/18/2023) who teach that in transforming growth factor alpha, replacement of aspartic acid at position 47 with alanine or asparagine did not affect biological activity while replacement with serine or glutamic acid sharply reduced the biological activity of the mitogen. These references demonstrate that even a single amino acid substitution will often dramatically affect the biological activity and characteristics of a protein. Clearly, it could not be predicted that polypeptide or a variant that shares only partial homology with a disclosed protein will function in a given manner.
Therefore, only the sequences shown in the specification to have immunoglobin binding and alkali stability, but not the full breadth of the claims, meet the written description provision of 35 USC 112, first paragraph. The species specifically disclosed are not representative of the genus because the genus is highly variant. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 USC 112 is severable from its enablement provision. (See page 1115).
The following is a quotation of 35 U.S.C. 112(b):
(B) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1 and 7-24 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Regarding claim 1, the phrase "such as" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1, 6-16, 18-21, and 24 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Rodrigo et al (WO2015/005859; IDS filed 7/8/2023).
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support.
Rodrigo et al disclose a method of isolating an immunoglobulin by purifying a sample comprising an immunoglobulin with a separation matrix then cleaning the matrix with a cleaning liquid (see page 13, line 30-page 14, line 15). The cleaning liquid comprises .1-2 M NaOH (see page 14, lines 29-30). It is noted that while the instant claims require that the cleaning liquid comprise at least 50% of an aqueous alkali metal hydroxide solution, for most of the claims, there is no limit on the molar concentration of the alkali metal hydroxide. Once the alkali metal hydroxide solution is added to the cleaning solution, the cleaning solution will be 100% an aqueous alkali metal hydroxide solution, just at a lower concentration. Therefore, the percentage limitation is essentially meaningless. As such, the cleaning liquid disclosed by Rodrigo et al includes 100% of an aqueous alkali metal hydroxide solution. The separation matrix comprises immunoglobulin-binding protein A variants that have improved alkaline stability (see page 4, lines 5-7 and 20-25).
As the claimed protein A domains have no defined amino acids, with an essentially unlimited number of mutations any Fc binding domain meets the limitations of the claims. Rodrigo et al disclose SEQ ID NO:2, which is an alkali-stable Fc binding domain of Spa. The polypeptides can be multimers, including dimers, trimers, tetramers, pentamers, and hexamers (see page 9, lines 15-20). The multimers are coupled to the support by a thioether link and a C-terminal cysteine residue (see page 12, lines 5-30). The matrix can comprise 6-11 mg/ml of multimer (see page 11, lines 30-31). The porous support is highly cross-linked agarose beads (see page 12, lines 23-30). The contact time of the NaOH cleaning liquid can be 10 minutes (see page 20, lines 5-7). If the invention works as applicant claims, this contact time necessarily results in the reduction recited in claim 19. The method steps can be repeated at least 10 times (see page 14, lines 30-34).
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim(s) 1, 6-16, and 18-24 are rejected under 35 U.S.C. 103 as being unpatentable over Rodrigo et al (WO2015/005859; IDS filed 7/18/2023).
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support.
Rodrigo et al disclose a method of isolating an immunoglobulin by purifying a sample comprising an immunoglobulin with a separation matrix then cleaning the matrix with a cleaning liquid (see page 13, line 30-page 14, line 15). The cleaning liquid comprises .1-2 M NaOH (see page 14, lines 29-30). It is noted that while the instant claims require that the cleaning liquid comprise at least 50% of an aqueous alkali metal hydroxide solution, for most of the claims, there is no limit on the molar concentration of the alkali metal hydroxide. Once the alkali metal hydroxide solution is added to the cleaning solution, the cleaning solution will be 100% an aqueous alkali metal hydroxide solution, just at a lower concentration. Therefore, the percentage limitation is essentially meaningless. As such, the cleaning liquid disclosed by Rodrigo et al includes 100% of an aqueous alkali metal hydroxide solution. The separation matrix comprises immunoglobulin-binding protein A variants that have improved alkaline stability (see page 4, lines 5-7 and 20-25).
As the claimed protein A domains have no defined amino acids, with an essentially unlimited number of mutations any Fc binding domain meets the limitations of the claims. Rodrigo et al disclose SEQ ID NO:2, which is an alkali-stable Fc binding domain of Spa. The polypeptides can be multimers, including dimers, trimers, tetramers, pentamers, and hexamers (see page 9, lines 15-20). The multimers are coupled to the support by a thioether link and a C-terminal cysteine residue (see page 12, lines 5-30). The matrix can comprise 6-11 mg/ml of multimer (see page 11, lines 30-31). The porous support is highly cross-linked agarose beads (see page 12, lines 23-30). The contact time of the NaOH cleaning liquid can be 10 minutes (see page 20, lines 5-7). If the invention works as applicant claims, this contact time necessarily results in the reduction recited in claim 19. The method steps can be repeated at least 10 times (see page 14, lines 30-34).
Rodrigo et al differs from the instant invention in that, while they disclose repeating the method multiple times, they do not state that different immunoglobulins should be used.
It would have been obvious to one of ordinary skill in the art, at the time of invention, to use the cleaned/sanitized matrix for additional immunoglobulins because the point of cleaning/sanitizing a matrix is to make it suitable for re-use. Using the matrix for additional samples and immunoglobulins would reduce costs.
One would have had a reasonable expectation of success because Rodrigo et al state that the matrix can be re-used after cleaning.
Claim(s) 1 and 6-24 are rejected under 35 U.S.C. 103 as being unpatentable over Rodrigo et al (WO2015/005859; IDS filed 10/23/2018) in view of Application Note 18-1124-57 AI 2014; IDS filed 7/18/2023).
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support.
Rodrigo et al disclose a method of isolating an immunoglobulin by purifying a sample comprising an immunoglobulin with a separation matrix then cleaning the matrix with a cleaning liquid (see page 13, line 30-page 14, line 15). The cleaning liquid comprises .1-2 M NaOH (see page 14, lines 29-30). It is noted that while the instant claims require that the cleaning liquid comprise at least 50% of an aqueous alkali metal hydroxide solution, for most of the claims, there is no limit on the molar concentration of the alkali metal hydroxide. Once the alkali metal hydroxide solution is added to the cleaning solution, the cleaning solution will be 100% an aqueous alkali metal hydroxide solution, just at a lower concentration. Therefore, the percentage limitation is essentially meaningless. As such, the cleaning liquid disclosed by Rodrigo et al includes 100% of an aqueous alkali metal hydroxide solution. The separation matrix comprises immunoglobulin-binding protein A variants that have improved alkaline stability (see page 4, lines 5-7 and 20-25).
As the claimed protein A domains have no defined amino acids, with an essentially unlimited number of mutations any Fc binding domain meets the limitations of the claims. Rodrigo et al disclose SEQ ID NO:2, which is an alkali-stable Fc binding domain of Spa. The polypeptides can be multimers, including dimers, trimers, tetramers, pentamers, and hexamers (see page 9, lines 15-20). The multimers are coupled to the support by a thioether link and a C-terminal cysteine residue (see page 12, lines 5-30). The matrix can comprise 6-11 mg/ml of multimer (see page 11, lines 30-31). The porous support is highly cross-linked agarose beads (see page 12, lines 23-30). The contact time of the NaOH cleaning liquid can be 10 minutes (see page 20, lines 5-7). If the invention works as applicant claims, this contact time necessarily results in the reduction recited in claim 19. The method steps can be repeated at least 10 times (see page 14, lines 30-34).
Rodrigo et al differs from the instant invention in that, while they disclose repeating the method multiple times, they do not state that different immunoglobulins should be used.
It would have been obvious to one of ordinary skill in the art, at the time of invention, to use the cleaned/sanitized matrix for additional immunoglobulins because the point of cleaning/sanitizing a matrix is to make it suitable for re-use. Using the matrix for additional samples and immunoglobulins would reduce costs.
One would have had a reasonable expectation of success because Rodrigo et al state that the matrix can be re-used after cleaning.
Rodrigo et al also differs from the instant invention in that they do not disclose the cleaning liquid to further comprise a C2-C7 alcohol.
Application Note 18-1124-57 discloses that the antimicrobial action of sodium hydroxide can be enhanced by the addition of ethanol to the NaOH solution (see page 3, column 1).
It would have been obvious to one of ordinary skill in the art, at the time of invention, to include ethanol in the cleaning liquid because the antimicrobial action of sodium hydroxide can be enhanced by the addition of ethanol.
One would have had a reasonable expectation of success because Application Note 18-1124-57 states that ethanol increases the antimicrobial effect.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/process/file/efs/guidance/eTD-info-I.jsp.
Claims 1 and 6-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 11753438. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-9, 12-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of U.S. Patent No. 10,703,774. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-10, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-29 of U.S. Patent No. 10,654,887. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-10, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-31 of U.S. Patent No. 10,711,035. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-10, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-31 of U.S. Patent No. 10,513,537. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-9, 11-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-23 of U.S. Patent No. 10,730,908. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-9, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-15 of U.S. Patent No. 11667671. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-10, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-31 of U.S. Patent No. 10995113. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-10, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-38 of U.S. Patent No. 12134633. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-10, 13-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-40 of U.S. Patent No. 11685764. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-29 of U.S. Patent No. 12037359. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11 of U.S. Patent No. 12448411. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Claims 1, 6-16, 18, 21, and 24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 11623941. Although the claims at issue are not identical, they are not patentably distinct from each other for the following reasons.
The instant claims are drawn to methods of cleaning a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains coupled to a porous support. The alkali-stabilized Protein A domains comprise mutants of a parental Fc- binding domain of Staphylococcus Protein A (SpA), wherein the parental Fc binding domain has various specific sequence requirements. The claims encompass an undefined number of possible polypeptides. The claims only define the parent polypeptide that is then mutated. Since there is no limit to the mutations that can be present, the mutant is completely undefined by anything other than its alkali stability and ability to bind to Fc domains.
The patented claims specifically recite each of the limitations of the instant claims. Therefore, the instant claims are anticipated.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Brian J Gangle whose telephone number is (571)272-1181. The examiner can normally be reached M-F, 9-6:30.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Anne Gussow can be reached at 571-272-6047. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/BRIAN GANGLE/Primary Examiner, Art Unit 1645
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