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 .
DETAILED ACTION
Application Status
This application is a 371 of PCT/JP2020/043691, filed on 05/24/2022.
Claims 1-8, 9, 10-11 and 12 are currently pending.
The preliminary amendment filed on 05/24/2022, amending claims 5, 9 and 10 is acknowledged.
Election/Restriction
Applicant's election without traverse of Group I, Claims 1-4, drawn to an adeno-associated virus (AAV)-binding protein which is selected from any one of the following (i) to (iii): (i) an AAV-binding protein comprising at least amino acid residues from serine at position 312 to aspartic acid at position 500 of an amino acid sequence set forth in SEQ ID NO: 1, wherein at least any one of the following amino acid substitutions (1) to (137) is present at the amino acid residues from positions 312 to 500: (1) a substitution of glycine with serine at position 390 of SEQ ID NO: 1, ---- (134) a substitution of valine with glutamic acid or isoleucine at position 499 of SEQ ID NO: 1; ii an AAV-binding protein comprising at least amino acid residues from serine at position 312 to aspartic acid at position 500 of the amino acid sequence set forth in SEQ ID NO: 1, wherein at least any one of the amino acid substitutions (1) to (134) is present at the amino acid residues from positions 312 to 500, wherein one or more of substitutions, deletions, insertions, and additions of one or several amino acid residues are further present at one or several positions other than the amino acid substitutions shown in (1) to (134), and wherein the AAV-binding protein has AAV-binding activity; and (iii) an AAV-binding protein comprising an amino acid sequence, wherein the amino acid sequence has 70% or more homology to an entire amino acid sequence in which at least any one of the amino acid substitutions (1) to (134) is present in an amino acid sequence ranging from serine at position 312 to aspartic acid at position 500 of the amino acid sequence set forth in SEQ ID NO: 1, wherein the at least any one of the amino acid substitutions remains in the amino acid sequence, and wherein the AAV-binding protein has AAV-binding activity, and species claim 1(i)(1), i.e., AAV-binding protein comprising a substitution of glycine (G) with serine (S) at position 390 of SEQ ID NO: 1, which is also present in claim 1 (ii)(1), claim 1(iii)(1), claim 2(iv) to (vi), claim 3(A) to (K), and claim 4 (SEQ ID Nos: 18 to 76) also comprises the same substitution at same position, which are within elected claim 1(i)(1) in the response filed on 08/29/2025 is acknowledged.
Claims 5-12 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim.
The requirement is still deemed proper and is therefore made FINAL.
Claims 1-4 are present for examination.
Priority
Acknowledgement is made of applicants claim for foreign priority under 35 U.S.C. 119(a)-(d) to foreign patent applications JAPAN 2019-212020, filed on 11/25/2019, and JAPAN 2020-165229, filed on 09/30/2020 without English translation.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on 08/19/2022, 01/16/2024, and 08/02/2024 are acknowledged. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are considered by the examiner. The signed copies of 1449 are enclosed herewith.
Drawings
Drawings submitted on 05/24/2022 are accepted by the Examiner.
Claim Rejections - 35 USC § 112(b), or Pre-AIA 35 USC § 112, Second Paragraph
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 1-4 is rejected under 35 U.S.C. 112 (b), or second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
Claims 1-2 and 4 are indefinite in the recitation “70% or more”, which is confusing and the metes and the bounds of the term “more” is not clear to the Examiner because the term “more” does not have any boundary and unknown rendering the term “more” unclear and confusing. Furthermore the phrase “more”, which could be 71%, 72, 73, ------ 99%, and the specification does not have any definition of such phrase. The phrase can be corrected to “at least 70%”. Clarification is required.
Claims 1-4 are rejected under 35 U.S.C. 112(b), as being indefinite and vague for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
Claim 1, 2 and 4 are indefinite in the recitation “comprising at least amino acid residues from serine at position 312 to aspartic acid at position 500 of an amino acid sequence set forth in SEQ ID NO: 1” in the context of adeno-associated virus (AAV)- binding protein, which is confusing. The phrase is unclear and does not make sense because it looks like some word is missing after the phrase “at least” and before “amino acid”, which makes incomplete sentence, as for example if it was written as “comprising at least one amino acid residues from serine at position 312 to aspartic acid at position 500 of an amino acid sequence set forth in SEQ ID NO: 1”, could make sense and definite. It is suggested that applicant clarify the meaning of the phrase. Appropriate correction and clarification are required.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph 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.
A. Written Description
Claims 1-4 are rejected under 35 U.S.C. 112(a), 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.
Claims 1, 2 and 4 are directed to an adeno-associated virus (AAV)-binding protein which is selected from any one of the following (i) to (iii): (i) an AAV-binding protein comprising at least amino acid residues from serine at position 312 to aspartic acid at position 500 of an amino acid sequence set forth in SEQ ID NO: 1, wherein at least any one of the following amino acid substitutions (1) to (137) is present at the amino acid residues from positions 312 to 500: (1) a substitution of glycine with serine at position 390 of SEQ ID NO: 1, (2) a substitution of isoleucine with phenylalanine at position 319 of SEQ ID NO: 1, (3) a substitution of leucine with proline at position 321 of SEQ ID NO: 1, (4) a substitution of proline with leucine at position 322 of SEQ ID NO: 1, (5) a substitution of asparagine with aspartic acid or serine at position 324 of SEQ ID NO: 1, (6) a substitution of glutamine with arginine at position 327 of SEQ ID NO: 1, (7) a substitution of asparagine with aspartic acid or tyrosine at position 329 of SEQ ID NO: 1, (8) a substitution of alanine with glycine at position 330 of SEQ ID NO: 1, (9) a substitution of tyrosine with cysteine at position 331 of SEQ ID NO: 1, (10) a substitution of valine with glutamine at position 332 of SEQ ID NO: 1, (11) a substitution of leucine with valine or proline at position 333 of SEQ ID NO: 1, (12) a substitution of glutamine with arginine at position 334 of SEQ ID NO: 1, (13) a substitution of proline with leucine at position 337 of SEQ ID NO: 1, (14) a substitution of lysine with arginine or glutamic acid at position 338 of SEQ ID NO: 1, (15) a substitution of glutamic acid with glycine at position 340 of SEQ ID NO: 1, (16) a substitution of threonine with alanine at position 341 of SEQ ID NO: 1, (17) a substitution of tyrosine with cysteine, histidine, or asparagine at position 342 of SEQ ID NO: 1, (18) a substitution of threonine with methionine at position 343 of SEQ ID NO: 1, (19) a substitution of tyrosine with histidine at position 344 of SEQ ID NO: 1, (20) a substitution of aspartic acid with asparagine at position 345 of SEQ ID NO: 1, (21) a substitution of tryptophan with leucine or arginine at position 346 of SEQ ID NO: 1, (22) a substitution of glutamine with leucine or proline at position 347 of SEQ ID NO: 1, (23) a substitution of leucine with proline at position 348 of SEQ ID NO: 1, (24) a substitution of isoleucine with threonine at position 349 of SEQ ID NO: 1, (25) a substitution of threonine with methionine at position 350 of SEQ ID NO: 1, (26) a substitution of histidine with leucine at position 351 of SEQ ID NO: 1, (27) a substitution of proline with leucine at position 352 of SEQ ID NO: 1, (28) a substitution of arginine with cysteine at position 353 of SEQ ID NO: 1, (29) a substitution of aspartic acid with glycine at position 354 of SEQ ID NO: 1, (30) a substitution of tyrosine with histidine, asparagine, or cysteine at position 355 of SEQ ID NO: 1, (31) a substitution of serine with cysteine at position 356 of SEQ ID NO: 1, (32) a substitution of glycine with cysteine at position 357 of SEQ ID NO: 1, (33) a substitution of histidine with arginine or leucine at position 363 of SEQ ID NO: 1, (34) a substitution of serine with proline at position 364 of SEQ ID NO: 1, (35) a substitution of glutamine with arginine at position 365 of SEQ ID NO: 1, (36) a substitution of isoleucine with threonine at position 366 of SEQ ID NO: 1, (37) a substitution of leucine with proline at position 367 of SEQ ID NO: 1, (38) a substitution of lysine with arginine at position 368 of SEQ ID NO: 1, (39) a substitution of leucine with glutamine or proline at position 369 of SEQ ID NO: 1, (40) a substitution of serine with alanine at position 370 of SEQ ID NO: 1, (41) a substitution of lysine with glutamic acid at position 371 of SEQ ID NO: 1, (42) a substitution of threonine with alanine at position 373 of SEQ ID NO: 1, (43) a substitution of leucine with proline at position 376 of SEQ ID NO: 1, (44) a substitution of tyrosine with cysteine at position 377 of SEQ ID NO: 1, (45) a substitution of phenylalanine with serine at position 379 of SEQ ID NO: 1, (46) a substitution of valine with alanine at position 381 of SEQ ID NO: 1, (47) a substitution of glutamic acid with glycine at position 384 of SEQ ID NO: 1, (48) a substitution of asparagine with serine at position 387 of SEQ ID NO: 1, (49) a substitution of histidine with glutamine, leucine, or arginine at position 389 of SEQ ID NO: 1, (50) a substitution of glutamic acid with lysine at position 391 of SEQ ID NO: 1, (51) a substitution of tyrosine with cysteine at position 393 of SEQ ID NO: 1, (52) a substitution of valine with alanine at position 396 of SEQ ID NO: 1, (53) a substitution of lysine with glutamic acid or arginine at position 399 of SEQ ID NO: 1, (54) a substitution of arginine with serine at position 406 of SEQ ID NO: 1, (55) a substitution of valine with alanine at position 412 of SEQ ID NO: 1, (56) a substitution of glutamine with leucine at position 415 of SEQ ID NO: 1, (57) a substitution of phenylalanine with serine at position 416 of SEQ ID NO: 1, (58) a substitution of glutamine with leucine at position 441 of SEQ ID NO: 1, (59) a substitution of tyrosine with phenylalanine at position 442 of SEQ ID NO: 1, (60) a substitution of lysine with arginine at position 448 of SEQ ID NO: 1, (61) a substitution of glutamic acid with glycine at position 453 of SEQ ID NO: 1, (62) a substitution of lysine with arginine at position 455 of SEQ ID NO: 1, (63) a substitution of glutamic acid with glycine at position 458 of SEQ ID NO: 1, (64) a substitution of alanine with serine at position 461 of SEQ ID NO: 1, (65) a substitution of serine with arginine at position 476 of SEQ ID NO: 1, (66) a substitution of leucine with proline at position 477 of SEQ ID NO: 1, (67) a substitution of asparagine with aspartic acid at position 487 of SEQ ID NO: 1, (68) a substitution of asparagine with aspartic acid at position 492 of SEQ ID NO: 1, (69) a substitution of isoleucine with asparagine or serine at position 319 of SEQ ID NO: 1, (70) a substitution of threonine with isoleucine at position 320 of SEQ ID NO: 1, (71) a substitution of lysine with glutamic acid at position 323 of SEQ ID NO: 1, (72) a substitution of leucine with glutamine or proline at position 328 of SEQ ID NO: 1, (73) a substitution of tyrosine with histidine at position 331 of SEQ ID NO: 1, (74) a substitution of valine with alanine or glutamic acid at position 332 of SEQ ID NO: 1, (75) a substitution of proline with glutamine at position 336 of SEQ ID NO: 1, (76) a substitution of proline with glutamine at position 337 of SEQ ID NO: 1, (77) a substitution of lysine with asparagine at position 338 of SEQ ID NO: 1, (78) a substitution of tyrosine with arginine at position 342 of SEQ ID NO: 1, (79) a substitution of threonine with serine at position 350 of SEQ ID NO: 1, (80) a substitution of isoleucine with phenylalanine at position 366 of SEQ ID NO: 1, (81) a substitution of valine with alanine at position 383 of SEQ ID NO: 1, (82) a substitution of glutamine with arginine at position 386 of SEQ ID NO: 1, (83) a substitution of histidine with aspartic acid at position 389 of SEQ ID NO: 1, (84) a substitution of glycine with cysteine at position 392 of SEQ ID NO: 1, (85) a substitution of valine with alanine at position 394 of SEQ ID NO: 1, (86) a substitution of isoleucine with valine at position 409 of SEQ ID NO: 1, (87) a substitution of serine with glycine at position 476 of SEQ ID NO: 1, (88) a substitution of threonine with serine at position 490 of SEQ ID NO: 1, (89) a substitution of serine with proline at position 312 of SEQ ID NO: 1, (90) a substitution of alanine with serine at position 313 of SEQ ID NO: 1, (91) a substitution of valine with aspartic acid at position 317 of SEQ ID NO: 1, (92) a substitution of glutamine with proline at position 318 of SEQ ID NO: 1, (93) a substitution of threonine with alanine at position 320 of SEQ ID NO: 1, (94) a substitution of lysine with arginine at position 323 of SEQ ID NO: 1, (95) a substitution of valine with alanine or glutamic acid at position 326 of SEQ ID NO: 1, (96) a substitution of glutamine with histidine or leucine at position 327 of SEQ ID NO: 1, (97) a substitution of asparagine with histidine or isoleucine at position 329 of SEQ ID NO: 1, (98) a substitution of valine with alanine at position 332 of SEQ ID NO: 1, (99) a substitution of glutamic acid with glycine or valine at position 335 of SEQ ID NO: 1, (100) a substitution of glutamic acid with valine at position 340 of SEQ ID NO: 1, (101) a substitution of threonine with proline at position 341 of SEQ ID NO: 1, (102) a substitution of threonine with serine at position 343 of SEQ ID NO: 1, (103) a substitution of tyrosine with phenylalanine at position 344 of SEQ ID NO: 1, (104) a substitution of tryptophan with cysteine at position 346 of SEQ ID NO: 1, (105) a substitution of methionine with leucine at position 359 of SEQ ID NO: 1, (106) a substitution of glutamic acid with lysine or valine at position 360 of SEQ ID NO: 1, (107) a substitution of glycine with cysteine at position 361 of SEQ ID NO: 1, (108) a substitution of lysine with glutamic acid, asparagine, or glycine at position 362 of SEQ ID NO: 1, (109) a substitution of serine with leucine at position 364 of SEQ ID NO: 1, (110) a substitution of lysine with asparagine or aspartic acid at position 371 of SEQ ID NO: 1, (111) a substitution of leucine with proline or glutamine at position 372 of SEQ ID NO: 1, (112) a substitution of proline with leucine at position 374 of SEQ ID NO: 1, (113) a substitution of glutamic acid with glycine or valine at position 378 of SEQ ID NO: 1, (114) a substitution of phenylalanine with tyrosine or cysteine at position 379 of SEQ ID NO: 1, (115) a substitution of lysine with glutamic acid at position 380 of SEQ ID NO: 1, (116) a substitution of valine with aspartic acid at position 381 of SEQ ID NO: 1, (117) a substitution of isoleucine with valine at position 382 of SEQ ID NO: 1, (118) a substitution of glutamic acid with valine at position 384 of SEQ ID NO: 1, (119) a substitution of valine with aspartic acid or isoleucine at position 394 of SEQ ID NO: 1, (120) a substitution of asparagine with serine at position 395 of SEQ ID NO: 1, (121) a substitution of threonine with serine at position 397 of SEQ ID NO: 1, (122) a substitution of glutamic acid with valine at position 401 of SEQ ID NO: 1, (123) a substitution of arginine with histidine at position 403 of SEQ ID NO: 1, (124) a substitution of arginine with histidine at position 406 of SEQ ID NO: 1, (125) a substitution of glutamine with arginine at position 415 of SEQ ID NO: 1, (126) a substitution of threonine with alanine at position 426 of SEQ ID NO: 1, (127) a substitution of glutamine with leucine or arginine at position 432 of SEQ ID NO: 1, (128) a substitution of glutamine with arginine at position 441 of SEQ ID NO: 1, (129) a substitution of histidine with leucine at position 443 of SEQ ID NO: 1, (130) a substitution of lysine with glutamic acid at position 448 of SEQ ID NO: 1, (131) a substitution of isoleucine with valine at position 456 of SEQ ID NO: 1, (132) a substitution of aspartic acid with asparagine at position 483 of SEQ ID NO: 1, (133) a substitution of serine with leucine at position 488 of SEQ ID NO: 1, (134) a substitution of valine with glutamic acid or isoleucine at position 499 of SEQ ID NO: 1; (ii) an AAV-binding protein comprising at least amino acid residues from serine at position 312 to aspartic acid at position 500 of the amino acid sequence set forth in SEQ ID NO: 1, wherein at least any one of the amino acid substitutions (1) to (134) is present at the amino acid residues from positions 312 to 500, wherein one or more of substitutions, deletions, insertions, and additions of one or several amino acid residues are further present at one or several positions other than the amino acid substitutions shown in (1) to (134), and wherein the AAV-binding protein has AAV-binding activity; and (iii) an AAV-binding protein comprising an amino acid sequence, wherein the amino acid sequence has 70% or more homology to an entire amino acid sequence in which at least any one of the amino acid substitutions (1) to (134) is present in an amino acid sequence ranging from serine at position 312 to aspartic acid at position 500 of the amino acid sequence set forth in SEQ ID NO: 1, wherein the at least any one of the amino acid substitutions remains in the amino acid sequence, and wherein the AAV-binding protein has AAV-binding activity.
The Court of Appeals for the Federal Circuit has held that a “written description of an invention involving a chemical genus, like a description of a chemical species, ‘requires a precise definition, such as by structure, formula [or] chemical name,’ of the claimed subject matter sufficient to distinguish it from other materials.” University of California v. Eli Lilly and Co., 1997 U.S. App. LEXIS 18221, at *23, quoting Fiers v. Revel, 25 USPQ2d 1601, 1606 (Fed. Cir. 1993). To fully describe a genus of genetic material, which is a chemical compound, applicants must (1) fully describe at least one species of the claimed genus sufficient to represent said genus whereby a skilled artisan, in view of the prior art, could predict the structure of other species encompassed by the claimed genus and (2) identify the common characteristics of the claimed molecules, e.g., structure, physical and/or chemical characteristics, functional characteristics when coupled with a known or disclosed correlation between function and structure, or a combination of these (paraphrased from Enzo Biochemical).
Thus, Claims are drawn to any adeno-associated virus (AAV)-binding protein, which is selected from any one of the following (i) to (iii): (i) an AAV-binding protein comprising at least amino acid residues from serine at position 312 to aspartic acid at position 500 of an amino acid sequence set forth in SEQ ID NO: 1, wherein the AAV-binding protein, which is at least 70% homology to SEQ ID NO: 1, derived from many unknown sources having any structural feature having respective AAV-binding activity, i.e., 30% non-homologous protein that encompasses many AAV-binding protein derived from many unknown sources and many mutants, variants, and fragments thereof, i.e., No Structure-Function correlation, which is required to fulfill the Written Description requirement.
As discussed in the written description guidelines the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A representative number of species means that the species, which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
Thus, Claims are drawn to any adeno-associated virus (AAV)-binding protein, which is at least 70% homology to SEQ ID NO: 1 derived from many unknown sources having any structural feature having respective enzymatic activity, i.e., 30% non-homologous protein that encompasses many AAV-binding protein derived from many unknown sources and many mutants, variants, and fragments thereof, i.e., 30% non-homologous protein that encompasses many AAV-binding protein derived from many unknown sources and many mutants, variants, and fragments thereof, which can have wide variety of unknown structures, whose structures are not fully described in the specification. No information, beyond the characterization of AAV-binding proteins has been provided, which would indicate that applicants had possession of the claimed genus of AAV-binding proteins.
Furthermore, the genus of genes and encoded polypeptides and functional homologs or variants required in the claimed invention is an extremely large structurally and functionally variable genus. While the argument can be made that the recited genus of polypeptides and encoding polynucleotides are adequately described by the disclosure of the structures of prior art, i.e., genes associated with the production of amino acids, since one could use structural homology to isolate those polypeptides and the encoding polynucleotide recited in the claims. However, the art clearly teaches the “Practical Limits of Function Prediction”: Whisstock et al., (2003) highlight the difficulties associated with “Prediction of protein function from protein sequence and structure”; “To reason from sequence and structure to function is to step onto much shakier ground”, closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function, in such cases, assignment of function on the basis of homology, in the absence of direct experimental evidence, will give the wrong answer, it is difficult to state criteria for successful prediction of function, since function is in principle a fuzzy concept. Given three sequences, it is possible to decide which of the three possible pairs is most closely related. Given three structures, methods are also available to measure and compare similarity of the pairs. However, in many cases, given three protein functions, it would be more difficult to choose the pair with most similar function, although it is possible to define metrics for quantitative comparisons of different protein sequences and structures, this is more difficult for proteins of different functions, in families of closely related proteins, mutations usually conserve function but modulate specificity i.e., mutations tend to leave the backbone conformation of the pocket unchanged but to affect the shape and charge of its lining, altering specificity, although the hope is that highly similar proteins will share similar functions, substitutions of a single, critically placed amino acid in an active-site residue may be sufficient to alter a protein’s role fundamentally (see, whole document). This finding is reinforced in the following scientific teachings for specific proteins in the art that suggest, even highly structurally homologous polypeptides do not necessarily share the same function and many functionally similar proteins will have little or no structural homology to disclosed proteins. For example, proteins having similar structure have different activities (structure does not always correlate to function); Witkowski et al., (1999) teaches that one conservative amino acid substitution transforms a -ketoacyl synthase into a malonyl decarboxylase and completely eliminates -ketoacyl synthase activity. Similarly, the art also teaches that functionally similar molecules have different structures; Kisselev L., (2002) teach that polypeptide release factors in prokaryotes and eukaryotes have same function but different structures.
As stated, no information, beyond the characterization of few AAV-binding proteins has been provided, which would indicate that applicants had possession of the claimed genus of AAV-binding proteins.us. The specification does not contain sufficient disclosure of the structure with function of all the AAV-binding proteins within the scope of the claimed genus. The genus of polypeptides claimed is a large variable genus including many mutants, variant and fragments thereof, which can have wide variety of structures. Therefore, many structurally unrelated AAV-binding proteins within the scope of these claims. The specification discloses the structure of only few representative species of the claimed genus with mutations, which is insufficient to put one of skill in the art in possession of the attributes and features of all species within the claimed genus. Therefore, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
Conclusion
Status of the claims:
Claims 1-4 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to IQBAL H CHOWDHURY whose telephone number is (571)272-8137. The examiner can normally be reached on M-F, at 9:00-5:00 PM.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath N. Rao, can be reached on 571-272-0939. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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Iqbal H. Chowdhury, PhD.
Primary Patent Examiner
Art Unit 1656 (Recombinant Enzymes and Protein Crystallography)
US Patent and Trademark Office
Ph. (571)-272-8137 and Fax (571)-273-8137
/IQBAL H CHOWDHURY/
Primary Examiner, Art Unit 1656