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 .
Election/Restrictions
Applicant’s election without traverse of SEQ ID NO: 2 in the reply filed on June 4, 2026, is acknowledged. The elected species was searched and prior art was found. In addition, prior art was found on each of SEQ ID NOs: 3-9. Therefore, the election of species requirement mailed April 30, 2026, is withdrawn.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
Claims 13-23 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Xu et al. (US 2019/0134161 A1).
Xu et al. teach methods of treating diseases related to glucose metabolism such as nonalcoholic fatty liver disease, obesity, overweight, and elevated lipid levels comprising administering a therapeutically effective amount of a conjugate comprising a glucagon mutant and one or more polyethylene glycols to a subject in need thereof ([0031]-[0036], [0039], Examples 18-21). Xu et al. teach that the glucagon mutant has a substitution, addition, or modification at one or more positive of native glucagon1 so that a side chain of at least one amino acid in the glucagon contains a sulfhydryl group, and the polyethylene glycol is conjugated to the glucagon via the sulfhydryl group ([0017]-[0020], [0022], Table 1, Examples 18-21).
Xu et al. teach the following embodiments of glucagon mutants (Table 1):
PB-702, SEQ ID NO: 3, wherein the amino group at the side chain of the lysine at the 12th position of the sequence is connected with a cysteine group via an amide bond, which is identical to instant SEQ ID NO: 4;
PB-703, SEQ ID NO: 4, wherein glutamine at the 24th position of the sequence is substituted with cysteine, which is identical to instant SEQ ID NO: 6;
PB-740, SEQ ID NO: 5, wherein a cysteine residue is added after the 29th amino acid, which is identical to SEQ ID NO: 8;
PB-741, SEQ ID NO: 6, wherein the side chain -C(=O)NH2 group of the glutamine at the 24th position is modified to -C(=O)NHCH2CH2SH, which is identical to instant SEQ ID NO: 2.
Xu et al. teach the following embodiments of glucagon mutants conjugated to polyethylene glycol (Table 1):
PB-707, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon;
PB-708, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-25 KD via ppMAL at the sulfhydryl in the glucagon;
PB-709, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-30 KD via ppMAL at the sulfhydryl in the glucagon;
PB-713, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-40 KD via ppMAL at the sulfhydryl in the glucagon;
PB-721, which is PB-740 (instant SEQ ID NO: 8) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon; and
PB-722, which is PB-741 (instant SEQ ID NO: 2) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon.
Therefore, Xu et al. teach all of the limitations of claim 13.
Regarding claim 14, Xu et al. teach (Table 1)
a) PB-703, wherein glutamine at the 24th position of glucagon is substituted with cysteine; and
b) PB-740, wherein cysteine is added after the 29th position of glucagon.
Regarding claim 15, Xu et al. teach (Table 1)
a) PB-702, wherein a sulfhydryl containing group is connected to the side chain of lysine at the 12th position of glucagon; and
b) PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon.
Regarding claim 16, Xu et al. teach (Table 1)
d) PB-702, wherein a sulfhydryl containing group is connected to the side chain of lysine at the 12th position of glucagon; and
f) PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon.
Regarding claim 17, Xu et al. teach PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon (Table 1).
Regarding claims 18-20, Xu et al. teach (Table 1)
a) PB-702, wherein a sulfhydryl containing group is connected to the side chain of lysine at the 12th position of glucagon, wherein the sulfhydryl containing group is a cysteine group, which is -C(=O)CH(NH2)CH2SH, which corresponds to claimed formula -C(=O)-Z1-SH wherein Z1 is an amino-substituted C2 alkyl; and
b) PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon, wherein the sulfhydryl containing group is -CH2CH2SH, which corresponds to claimed formula -Z1-SH wherein Z1 is C2 alkyl.
With respect to claim 21, Xu et al. teach (Table 1):
PB-741, which is identical to instant SEQ ID NO: 2;
PB-702, which is identical to instant SEQ ID NO: 4;
PB-703, which is identical to instant SEQ ID NO: 6; and
PB-740, which is identical to instant SEQ ID NO: 8.
With respect to claim 22, Xu et al. teach (Table 1):
PB-707, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon;
PB-708, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-25 KD via ppMAL at the sulfhydryl in the glucagon;
PB-709, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-30 KD via ppMAL at the sulfhydryl in the glucagon;
PB-713, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-40 KD via ppMAL at the sulfhydryl in the glucagon;
PB-721, which is PB-740 (instant SEQ ID NO: 8) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon; and
PB-722, which is PB-741 (instant SEQ ID NO: 2)conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon.
The species with PEG 23 KD, 25 KD, 30 KD, and 40 KD fall within the claimed ranges.
Xu et al. also teach that the molecular weight of PEG may be 2 kDa to about 50 kDa, preferably about 3 kDa to about 40 kDa, more preferably about 4 kDa to about 35 kDa, even more preferably about 5 kDa to about 30 kDa, for example, about 5 kDa, about 10 kDa, about 15 kDa, about 20 kDa, 21 kDa, 22 kDa, 23 kDa, 24 kDa, about 25 kDa, 26 kDa, 27 kDa, 28 kDa, 29 kDa, about 30 kDa, about 35 kDa, about 40 kDa and about 45 kDa, or any value between the above molecular weight values ([0015]).
Regarding claim 23, Wu et al. teaches PB-722, which is PB-741 conjugated to mPEG-23 KD via ppMAL (Table 1). PB-741 is identical to instant SEQ ID NO: 2, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon. ppMAL is the maleide linker shown in the claim.
Claims 13-14, 22, and 24-25 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Kim et al. (US 2019/0119347 A1).
Kim et al. teach methods of treating diseases related to glucose metabolism such as congenital hyperinsulinemia and hypoglycemia-associated with congenital hyperinsulinemia comprising administering a therapeutically effective amount of a conjugate comprising a glucagon to a subject in need thereof ([0019]-[0028], [0556]-[0559]). Kim et al. teach that the glucagon mutant may have a substitution or addition at one or more position of native glucagon so that a side chain of at least one amino acid in the glucagon contains a sulfhydryl group (see SEQ ID NOs: 2-44, especially SEQ ID NO: 37 of Kim et al.). Kim et al. teach that the conjugate may comprise the glucagon and a polyethylene glycol polymer ([0188]). Kim et al. teach that the polyethylene glycol may be conjugated via a sulfhydryl group in the glucagon ([0208]).
Kim et al. reduce to practice an embodiment wherein the glucagon mutant is SEQ ID NO: 37 (Example 7). The alignment of instant SEQ ID NO: 1 and prior art SEQ ID NO: 37 is as follows:
Instant SEQ ID NO: 1 HSQGTFTSDY SKYLDSRRAQ DFVQWLMNT
Kim SEQ ID NO: 37 YXQGTFTSDY SKYLDERRAK EFVQWLMNTC
Compared to instant SEQ ID NO: 1, SEQ ID NO: 37 of Kim et al. includes the addition of a cysteine, which contains a sulfhydryl side chain, after position 29. In addition, SEQ ID NO: 37 contains amino acid substitutions at positions 1, 2, 16, 20, and 21. These additional substitutions are not excluded by instant claim 13 because the claim allows for substitution, addition, or modification at one or more positions so long as at least one amino acid side chain has a sulfhydryl.
Kim et al. teach the preparation of a conjugate including glucagon SEQ ID NO: 37, PEG, and an immunoglobulin Fc region (Example 17). First, a 10 kDa PEG having a maleimide group and an aldehyde group, respectively, at both ends was conjugated to the cysteine residue of glucagon derivative (SEQ ID NO: 37) ([0680]). Then the mono-pegylated glucagon derivative was reacted with an immunoglobulin Fc ([0681]). The result is a long-acting conjugate of SEQ ID NO: 37 ([0683]). The additional immunoglobulin Fc region is not excluded by instant claim 13.
Kim et al. teach a method of treating obesity (Example 3), acute hypoglycemia (Example 4), and chronic hypoglycemia in congenital hyperinsulinemia (Example 5).
Therefore, Kim et al. satisfy all of the limitations of instant claim 13.
Regarding claim 14, Kim et al. teach b) SEQ ID NO: 37, wherein cysteine is added after the 29th position of glucagon (Example 17).
With respect to claim 22, Kim et al. teach 10 KDa PEG, which falls within the claimed ranges (Example 17).
With respect to claims 24-25, Kim et al. teach treatment of chronic hypoglycemia in congenital hyperinsulinemia (Example 5).
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 13-29 are rejected under 35 U.S.C. 103 as being unpatentable over Kim et al. (US 2019/0119347 A1) in view of Xu et al. (US 2019/0134161 A1).
The factual inquiries for establishing a background for determining obviousness under pre-AIA 35 U.S.C. 103(a) are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Determining the scope and contents of the prior art.
Kim et al. teach the treatment of glucose metabolic diseases, especially congenital hyperinsulinemia and hypoglycemia-associated with congenital hyperinsulinemia ([0013]-[0016]). Kim et al. teach that glucagon can be used as a treatment for these conditions but that its use is limited by its short half-life, which necessitates frequent administration ([0018]). To solve this problem, Kim et al. developed long-acting conjugates of glucagon to treat hyperinsulinemia and hypoglycemia-associated with congenital hyperinsulinemia ([0019]-[0028], [0556]-[0559]).
Kim et al. teach that the long-acting conjugates of glucagon comprise a glucagon mutant with a substitution or addition at one or more positions of native glucagon so that a side chain of at least one amino acid in the glucagon contains a sulfhydryl group (see SEQ ID NOs: 2-44, especially SEQ ID NO: 37 of Kim et al.). Kim et al. teach that the conjugate may comprise the glucagon mutant and a polyethylene glycol polymer ([0188]). Kim et al. teach that the polyethylene glycol may be conjugated via a sulfhydryl group in the glucagon ([0208]).
Kim et al. reduce to practice an embodiment wherein the glucagon mutant is SEQ ID NO: 37 (Example 7). The alignment of instant SEQ ID NO: 1 and prior art SEQ ID NO: 37 is as follows:
Instant SEQ ID NO: 1 HSQGTFTSDY SKYLDSRRAQ DFVQWLMNT
Kim SEQ ID NO: 37 YXQGTFTSDY SKYLDERRAK EFVQWLMNTC
Compared to instant SEQ ID NO: 1, SEQ ID NO: 37 of Kim et al. includes the addition of a cysteine, which contains a sulfhydryl side chain, after position 29. In addition, SEQ ID NO: 37 contains amino acid substitutions at positions 1, 2, 16, 20, and 21.
Kim et al. teach the preparation of a conjugate including glucagon SEQ ID NO: 37, PEG, and an immunoglobulin Fc region (Example 17). First, a 10 kDa PEG having a maleimide group and an aldehyde group, respectively, at both ends was conjugated to the cysteine residue of glucagon derivative (SEQ ID NO: 37) ([0680]). Then the mono-pegylated glucagon derivative was reacted with an immunoglobulin Fc ([0681]). The result is a long-acting conjugate of SEQ ID NO: 37 ([0683]).
Kim et al. teach a method of treating obesity (Example 3), acute hypoglycemia (Example 4), and chronic hypoglycemia in congenital hyperinsulinemia (Example 5).
Ascertaining the differences between the prior art and the claims at issue.
Kim et al. does not reduce to practice embodiments wherein the long-acting glucagon conjugate comprises instant SEQ ID NOs: 2, 4, 6, or 8 (or the C-terminal amidated forms thereof, SEQ ID NOs: 3, 5, 7, 9).
Resolving the level of ordinary skill in the pertinent art.
Xu et al. teach methods of treating diseases related to glucose metabolism such as nonalcoholic fatty liver disease, obesity, overweight, and elevated lipid levels comprising administering a therapeutically effective amount of a conjugate comprising a glucagon mutant and one or more polyethylene glycols to a subject in need thereof ([0031]-[0036], [0039], Examples 18-21). Xu et al. teach that the glucagon mutant has a substitution, addition, or modification at one or more positive of native glucagon so that a side chain of at least one amino acid in the glucagon contains a sulfhydryl group, and the polyethylene glycol is conjugated to the glucagon via the sulfhydryl group ([0017]-[0020], [0022], Table 1, Examples 18-21).
Xu et al. teach that the glucagon conjugates are long-acting ([0085]).
Xu et al. teach the following embodiments of glucagon mutants (Table 1):
PB-702, SEQ ID NO: 3, wherein the amino group at the side chain of the lysine at the 12th position of the sequence is connected with a cysteine group via an amide bond, which is identical to instant SEQ ID NO: 4;
PB-703, SEQ ID NO: 4, wherein glutamine at the 24th position of the sequence is substituted with cysteine, which is identical to instant SEQ ID NO: 6;
PB-740, SEQ ID NO: 5, wherein a cysteine residue is added after the 29th amino acid, which is identical to SEQ ID NO: 8;
PB-741, SEQ ID NO: 6, wherein the side chain -C(=O)NH2 group of the glutamine at the 24th position is modified to -C(=O)NHCH2CH2SH, which is identical to instant SEQ ID NO: 2.
Xu et al. teach the following embodiments of glucagon mutants conjugated to polyethylene glycol (Table 1):
PB-707, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon;
PB-708, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-25 KD via ppMAL at the sulfhydryl in the glucagon;
PB-709, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-30 KD via ppMAL at the sulfhydryl in the glucagon;
PB-713, which is PB-703 (instant SEQ ID NO: 6) conjugated to mPEG-40 KD via ppMAL at the sulfhydryl in the glucagon;
PB-721, which is PB-740 (instant SEQ ID NO: 8) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon; and
PB-722, which is PB-741 (instant SEQ ID NO: 2) conjugated to mPEG-23 KD via ppMAL at the sulfhydryl in the glucagon.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to substitute the long-acting glucagon conjugates taught by Xu et al. for the long-acting glucagon conjugates in the method of treating congenital hyperinsulinemia and hypoglycemia associated with congenital hyperinsulinemia taught by Kim et al. The rationale for obviousness is simple substitution of one known element for another to obtain predictable results (MPEP § 2143.01(B)). The relevant findings for this rationale are as follows.
(1) The prior art contained a device (method, product, etc.) which differed from the claimed device by the substitution of some components (step, element, etc.) with other components. In the instant case, the primary reference teaches a method of treating congenital hyperinsulinemia and hypoglycemia associated with congenital hyperinsulinemia which differs from the claimed methods by the substitution of glucagon conjugates comprising instant SEQ ID NOs: 2-9 for glucagon conjugated comprising a different sequence, SEQ ID NO: 37 of Kim et al. Therefore, prior art contained a method which differed from the claimed method by the substitution of some step with other steps.
(2) The substituted components and their functions were known in the art. Xu et al. teach Xu et al. teach the following embodiments of glucagon mutants (Table 1): PB-741, which is identical to instant SEQ ID NO: 2; PB-702, which is identical to instant SEQ ID NO: 4; PB-703, which is identical to instant SEQ ID NO: 6; and PB-740, which is identical to instant SEQ ID NO: 8. Xu et al. teach the following embodiments of glucagon mutants conjugated to polyethylene glycol (Table 1): PB-707, which is instant SEQ ID NO: 6 conjugated to mPEG-23 KD via ppMAL; PB-708, which is instant SEQ ID NO: 6 conjugated to mPEG-25 KD via ppMAL; PB-709, which is instant SEQ ID NO: 6 conjugated to mPEG-30 KD via ppMAL; PB-713, which is instant SEQ ID NO: 6 conjugated to mPEG-40 KD via ppMAL; PB-721, which is instant SEQ ID NO: 8 conjugated to mPEG-23 KD via ppMAL; and PB-722, which is instant SEQ ID NO: 2 conjugated to mPEG-23 KD via ppMAL. These embodiments are the substituted components. The function of glucagon conjugates is known in the art because Xu et al. teach that the can be used to treat metabolic disorders ([0031]-[0036], [0039], Examples 18-21) and that they are long-acting ([0085]). Therefore, the substituted components and their functions were known in the art.
(3) One of ordinary skill in the art could have substituted one known element for another, and the results of the substitution would have been predictable. One of ordinary skill in the art would expect that the glucagon conjugates of Xu et al. performs the function of modulating the glucagon receptor and having long-acting activity in the combination because this is the function taught by Xu et al. ([0085] and [0031]-[0036], [0039], Examples 18-21). Therefore, one of ordinary skill in the art could have substituted one known element for another, and the results of the substitution would have been predictable.
(4) Whatever additional findings based on the Graham factual inquiries may be necessary, in view of the facts of the case under consideration, to explain a conclusion of obviousness. The data presented in the specification are consistent with the prior art and therefore are not unexpected.
The rationale to support a conclusion that the claim would have been obvious is that the substitution of one known element for another yields predictable results to one of ordinary skill in the art. Therefore, claim 13 is obvious over the cited art.
Regarding claim 14, Xu et al. teach (Table 1)
a) PB-703, wherein glutamine at the 24th position of glucagon is substituted with cysteine; and
b) PB-740, wherein cysteine is added after the 29th position of glucagon.
Regarding claim 15, Xu et al. teach (Table 1)
a) PB-702, wherein a sulfhydryl containing group is connected to the side chain of lysine at the 12th position of glucagon; and
b) PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon.
Regarding claim 16, Xu et al. teach (Table 1)
d) PB-702, wherein a sulfhydryl containing group is connected to the side chain of lysine at the 12th position of glucagon; and
f) PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon.
Regarding claim 17, Xu et al. teach PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon (Table 1).
Regarding claims 18-20, Xu et al. teach (Table 1)
a) PB-702, wherein a sulfhydryl containing group is connected to the side chain of lysine at the 12th position of glucagon, wherein the sulfhydryl containing group is a cysteine group, which is -C(=O)CH(NH2)CH2SH, which corresponds to claimed formula -C(=O)-Z1-SH wherein Z1 is an amino-substituted C2 alkyl; and
b) PB-741, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon, wherein the sulfhydryl containing group is -CH2CH2SH, which corresponds to claimed formula -Z1-SH wherein Z1 is C2 alkyl.
With respect to claim 21, Xu et al. teach (Table 1): PB-741, which is identical to instant SEQ ID NO: 2; PB-702, which is identical to instant SEQ ID NO: 4; PB-703, which is identical to instant SEQ ID NO: 6; and PB-740, which is identical to instant SEQ ID NO: 8.
It would have been further obvious to use the C-terminal amidated versions of each of these peptides (instant SEQ ID NOs: 3, 5, 7, and 9) because Kim et al. teach that the glucagons can have a C-terminal carboxy or amide group ([0181]).
With respect to claim 22, Xu et al. teach (Table 1): PB-707, which is SEQ ID NO: 6 conjugated to mPEG-23 KD via ppMAL; PB-708, which is SEQ ID NO: 6 conjugated to mPEG-25 KD via ppMAL; PB-709, which is SEQ ID NO: 6 conjugated to mPEG-30 KD via ppMAL; PB-713, which is SEQ ID NO: 6 conjugated to mPEG-40 KD via ppMAL; PB-721, which is SEQ ID NO: 8 conjugated to mPEG-23 KD via ppMAL; and PB-722, which is SEQ ID NO: 2 conjugated to mPEG-23 KD via ppMAL. The species with PEG 23 KD, 25 KD, 30 KD, and 40 KD fall within the claimed ranges.
Xu et al. also teach that the molecular weight of PEG may be 2 kDa to about 50 kDa, preferably about 3 kDa to about 40 kDa, more preferably about 4 kDa to about 35 kDa, even more preferably about 5 kDa to about 30 kDa, for example, about 5 kDa, about 10 kDa, about 15 kDa, about 20 kDa, 21 kDa, 22 kDa, 23 kDa, 24 kDa, about 25 kDa, 26 kDa, 27 kDa, 28 kDa, 29 kDa, about 30 kDa, about 35 kDa, about 40 kDa and about 45 kDa, or any value between the above molecular weight values ([0015]).
Regarding claim 23, Wu et al. teaches PB-722, which is PB-741 conjugated to mPEG-23 KD via ppMAL (Table 1). PB-741 is identical to instant SEQ ID NO: 2, wherein a sulfhydryl containing group is connected to the side chain of glutamine at the 24th position of glucagon. ppMAL is the maleide linker shown in the claim.
Regarding claims 24-29, Kim et al. teach treatment of chronic hypoglycemia in congenital hyperinsulinemia (Example 5).
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHRISTINA M MARCHETTI BRADLEY whose telephone number is (571)272-9044. The examiner can normally be reached Monday-Friday, 8:30 am - 5 pm.
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CHRISTINA M MARCHETTI BRADLEY
Primary Examiner
Art Unit 1654
/CHRISTINA BRADLEY/Primary Examiner, Art Unit 1654
1 Native glucagon in Xu et al. is SEQ ID NO: 2, which is identical to instant SEQ ID NO: 1.
Prosecution Insights