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
In response to the previous Office action, a non-Final rejection (mailed on 10/21/2025), Applicants filed a response and amendment received on 01/21/2026. Said amendment canceled Claims 9, 11 and 16-49, amended Claims 1, and added claims 50-56. Thus, Claims 1-8, 10, 12-15 and 50-56 are at issue and present for examination.
Objections to the Specification - WITHDRAWN
The previous objection of the specification for containing an embedded hyperlink and/or other form of browser-executable code [1] “http://” on pages 133, 167, 188, 229, 246 and 296; and [2] “https://” on pages 156, 180, 243, 302 and 303, is withdrawn by virtue of Applicants’ amendment.
Claim Rejections - 35 U.S.C. § 112 - MAINTAINED
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.
Claims 1-8, 10, 12-15 and 50-56 are rejected under 35 U.S.C. 112, first paragraph, because the specification, while being enabling for an engineered or non-naturally occurring composition comprising: [I]. a fusion protein comprising a Cas polypeptide, a reverse transcriptase (RT) polypeptide and a Rad52 polypeptide, wherein the fusion protein comprises an amino acid sequence having at least 90% sequence identity to SEQ ID NO: 5 or SEQ ID NO: 6; and [II]. a guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR- Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide, does not reasonably provide enablement for
any engineered or non-naturally occurring composition comprising: a. any Type II or any Type V Cas polypeptide; b. any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. any guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR-Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands (858 F.2d 731, 737, 8 USPQ2nd 1400 (Fed. Cir. 1988)) as follows: 1) quantity of experimentation necessary, 2) the amount of direction or guidance presented, 3) the presence and absence of working examples, 4) the nature of the invention, 5) the state of prior art, 6) the relative skill of those in the art, 7) the predictability or unpredictability of the art, and 8) the breath of the claims. The factors which have lead the Examiner to conclude that the specification fails to teach how to make and/or use the claimed invention without undue experimentation, are addressed in detail below.
The breath of the claims. Claims 1-8, 10, 12-15 and 50-56 are so broad as to encompass any engineered or non-naturally occurring composition comprising: a. any Type II or any Type V Cas polypeptide; b. any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. any guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR- Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide, optionally further comprising any adaptor protein including any DNA exonuclease, optionally T5, Fen1, Rad27, RnhA; or any recombinase optionally ΦC31 integrase, Bxb1, ΦBT1 integrase, A118, TP901-1 or R4; or alternatively any adaptor protein, optionally GAM, Rad52, RecT, RecO, DrdGB, UvsY, gp32, p22 ERF, or any functional fragments or variants thereof (italicized for added emphasis, see claims 8 and 13). The enablement provided is not commensurate in scope with the claim due to the extremely large number of different combinations of enzymes, DNA exonucleases, recombinases, and/or adaptor proteins including any functional fragments or variants thereof of unknown structure encompassed by the claims. It is noted by the Examiner that the phrase “any functional fragments or variants thereof” is not defined in the specification. In the instant case, the specification enables a single species, i.e., a fusion protein comprising a Cas polypeptide, a reverse transcriptase (RT) polypeptide and a Rad52 polypeptide, wherein the fusion protein comprises an amino acid sequence having at least 90% sequence identity to SEQ ID NO: 5 or SEQ ID NO: 6.
The amount of direction or guidance presented and the existence of working examples. The specification discloses a fusion protein comprising a Cas polypeptide, a reverse transcriptase (RT) polypeptide and a Rad52 polypeptide, wherein the fusion protein comprises an amino acid sequence having at least 90% sequence identity to SEQ ID NO: 5 or SEQ ID NO: 6 as a working example. However, the specification fails to provide any clue as to the structural elements required in any engineered or non-naturally occurring composition comprising: a. any Type II or any Type V Cas polypeptide; b. any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. any guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR-Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide, optionally further comprising any adaptor protein including any DNA exonuclease, optionally T5, Fen1, Rad27, RnhA; or any recombinase optionally ΦC31 integrase, Bxb1, ΦBT1 integrase, A118, TP901-1 or R4; or alternatively any adaptor protein, optionally GAM, Rad52, RecT, RecO, DrdGB, UvsY, gp32, p22 ERF, or any functional fragments or variants thereof (italicized for added emphasis). There is no information or guidance as to which amino acid residues in the adaptor proteins, DNA exonucleases or recombinases recited in the claims can be modified or deleted in order to make any functional fragments or variants of the T5, Fen1, Rad27, RnhA, GAM, Rad52, RecT, RecO, DrdGB, UvsY, gp32, p22 ERF, and determine which of these if any would be capable of binding or forming complex with a composition comprising any Type II or any Type V Cas polypeptide; b. any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT.
The state of prior art, the relative skill of those in the art, and the predictability or unpredictability of the art. The amino acid sequence of a polypeptide determines its structural and functional properties. While the art discloses many structurally/functionally different Type II and Type V Cas polypeptides, Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, gRNAs, DNA exonucleases, recombinases, adaptor proteins, neither the specification nor the art provide a correlation between structure of these enzymes/adaptor proteins and gRNA that allows one of skill in the art can envision which structure among any Type II and Type V Cas polypeptides, in a specific combination with Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, or Moloney murine leukemia virus (M-MLV) RT, any gRNA and any adaptor proteins, including any of the listed DNA exonucleases, recombinases or any functional fragments or variants thereof in order to make a functional CRISPR-Cas complex with a desire activity. Regarding the phrase “functional fragments or variants thereof” as recited in claims 8 and 13, the art clearly teaches that modification or deletion of a protein’s amino acid sequence to obtain any functional fragments or variants thereof with the desired activity without any guidance/knowledge as to which amino acids in a protein are tolerant of modification and which ones are conserved is highly unpredictable. Therefore, at the time of the invention there was a high level of unpredictability associated with altering or deleting a polypeptide sequence with an expectation that the polypeptide will maintain the desired activity.
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification. While methods of generating or isolating fragments and/or variants of a polypeptide were known in the art at the time of the invention, it was not routine in the art to screen by a trial and error process any engineered or non-naturally occurring composition comprising: a. any Type II or any Type V Cas polypeptide; b. any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. any guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR- Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide, optionally further comprising any adaptor protein including any DNA exonuclease, optionally T5, Fen1, Rad27, RnhA; or any recombinase optionally ΦC31 integrase, Bxb1, ΦBT1 integrase, A118, TP901-1 or R4; or alternatively any adaptor protein, optionally GAM, Rad52, RecT, RecO, DrdGB, UvsY, gp32, p22 ERF, or any functional fragments or variants thereof (italicized for added emphasis) to determine which ones would be capable of use together in a CRISPR/Cas complex for a desired activity. In the absence of a rational and predictable scheme, one of skill in the art would have to test an essentially infinite number of different structure of any Type II or any Type V Cas polypeptide, any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide, any gRNA and any adaptor protein including any DNA exonuclease, optionally T5, Fen1, Rad27, RnhA; or any recombinase optionally ΦC31 integrase, Bxb1, ΦBT1 integrase, A118, TP901-1 or R4; or alternatively any adaptor protein, optionally GAM, Rad52, RecT, RecO, DrdGB, UvsY, gp32, p22 ERF, or any functional fragments or variants thereof to determine which ones can be used in the same CRISPR-Cas complex for a desired activity.
Therefore, taking into consideration the extremely broad scope of the claim, the lack of guidance, the amount of information provided, the lack of knowledge about a correlation between structure and the desired function, and the high degree of unpredictability of the prior art in regard to structural changes and their effect on function, one of ordinary skill in the art would have to go through the burden of undue experimentation in order to practice the claimed invention.
It is noted by the Examiner that none of the dependent claims remedy the deficiency noted under the instant ‘scope of enablement’ rejection as discussed above.
Thus, Applicant has not provided sufficient guidance to enable one of ordinary skill in the art to make and use the invention in a manner reasonably correlated with the scope of the claims.
Applicants’ Arguments:
Applicant has amended Claim 1 to specify that the Cas polypeptide is a Type II or Type V Cas polypeptide and that the reverse transcriptase polypeptide is selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT. These amendments render moot the Examiner's concerns regarding both the quantity of experimentation and predictability. The specified Cas protein types and the enumerated reverse transcriptase species are disclosed in the specification as functional components of the claimed invention, with clear direction how to make and use these embodiments in combination. Withdrawal of the rejection is respectfully requested.
Examiner’s Explanation:
Applicants’ arguments have been fully considered but are not deemed persuasive for the following reasons. Contrary to Applicants’ allegation, it is well-known in the relevant field of art at the time the invention is made that Type V Cas polypeptides have markedly different structures and functions to Type II Cas polypeptides, i.e., different PAM requirements, cleavage patterns, and no natural nickase variants (as required in newly added claim 51), which is a clear indication that it would require an undue experimentation with extensive trial-and-error protein engineering, guide RNA designing/redesigning, and cell-based testing in order to enable one of ordinary skill in the art to make and use the invention in a manner reasonably correlated with the full scope of the claims which encompasses any engineered or non-naturally occurring composition comprising: a. any Type II or any Type V Cas polypeptide; b. any reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. any guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR- Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide, optionally further comprising any adaptor protein including any DNA exonuclease, optionally T5, Fen1, Rad27, RnhA; or any recombinase optionally ΦC31 integrase, Bxb1, ΦBT1 integrase, A118, TP901-1 or R4; or alternatively any adaptor protein, optionally GAM, Rad52, RecT, RecO, DrdGB, UvsY, gp32, p22 ERF, or any functional fragments or variants thereof (italicized for added emphasis). Thus, as explained above, Applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the invention in a manner reasonably correlated with the scope of the claims, and none of the dependent claims or newly added claims remedy the deficiencies noted above.
Claim Rejections - 35 U.S.C. § 102 - WITHDRAWN
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.
The previous rejection of Claims 1-4, 7, 10 and 12-15 under 35 U.S.C. 102(a)(1)/102(a)(2) as being anticipated by Mohr et al. (A Reverse Transcriptase-Cas1 Fusion Protein Contains a Cas6 Domain Required for Both CRISPR RNA Biogenesis and RNA Spacer Acquisition, Molecular Cell, Volume 72, Issue 4, 15 November 2018, Pages 700-714) is withdrawn in favor of a new rejection shown below in order to better address Applicants’ amendment to claims.
It is noted by the Examiner that any arguments provided by Applicants are moot because the rejection using Mohr et al. reference has been withdrawn.
Claim Rejections - 35 U.S.C. § 102 – NECESSITATED BY APPLICANTS’ AMENDMENT TO CLAIMS
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 1-4, 50, 51 and 56 are rejected under 35 U.S.C. 102(a) as being anticipated by Anzalone et al. (Search-and-replace genome editing without double-strand breaks or donor DNA, Nature, Vol 576, pages 149-157 published on 10/21/2019, see IDS).
The instant claims are drawn to an engineered or non-naturally occurring composition comprising: a. a Type II or Type V Cas polypeptide; b. a reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. a guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR-Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide.
Anzalone et al. teach an engineered composition comprising a Type II Cas polypeptide, S. pyogenes Cas9 nickase (H840A variant) fused to M-MLV RT, prime editing guide RNA (pegRNA) comprising a hairpin structure at the 3' end of the guide molecule as well as stem loop 2, which is capable of directing site-specific binding of the CRISPR-Cas complex to a target sequence of a target polynucleotide; a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide (see Abstract, Figure 1, and its related discussions on page 150), thereby anticipating claims 1-4, 50, 51 and 56. Therefore, teachings of Anzalone et al. anticipate the invention as claimed.
Claim Rejections - 35 USC § 103 – NECESSITATED BY APPLICANTS’ AMENDMENT TO CLAIMS
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.
Claims 1-8, 10, 12-15 and 50-56 are rejected under 35 U.S.C. 103 as being unpatentable over Anzalone et al. (Search-and-replace genome editing without double-strand breaks or donor DNA, Nature, Vol 576, pages 149-157 published on 10/21/2019, see IDS) in view of Konermann et al. (Genome-scale transcriptional activation by an engineered CRISPR-Cas9 complex, Nature. 2015 January 29; 517(7536): 583–588, see IDS), Tran et al. (Enhancement of Precise Gene Editing by the Association of Cas9 With Homologous Recombination Factors, Front Genet., published on 04/30/2019; Vol. 10, Article 365), and Park et al. (Targeted gene knock-in by CRISPR/ Cas ribonucleoproteins in porcine zygotes, Scientific Reports, 7:42458, published 02/14/2017).
The instant claims are drawn to an engineered or non-naturally occurring composition comprising: a. a Type II or Type V Cas polypeptide; b. a reverse transcriptase (RT) polypeptide selected from the group consisting of Human immunodeficiency virus (HIV) RT, Avian myoblastosis virus (AMV) RT, and Moloney murine leukemia virus (M-MLV) RT, wherein the RT polypeptide is connected to or otherwise capable of forming a complex with the Cas polypeptide; and c. a guide molecule capable of forming a CRISPR-Cas complex with the Cas polypeptide and comprising: i. a guide sequence capable of directing site-specific binding of the CRISPR-Cas complex to a target sequence of a target polynucleotide; ii. a 3' binding site region capable of binding to a cleaved upstream strand of the target polynucleotide; and iii. a RT template sequence encoding an extended sequence, wherein the extended sequence comprises a variant region and a 3' homologous sequence capable of hybridization to the downstream cleaved strand of the target polynucleotide.
Teachings of Anzalone et al. are as described above.
Anzalone et al. further teach that Fen1 can excise 5’ DNA flap (see page 151, left column 1st para; and Fig. 1c). Anzalone et al. further teach that prime editing method is shown to install short recombinase sites with high efficiency including an extended Cre recombinase loxP site (44 bp with 23% efficiency, see page 156, right column 1st para).
Anzalone et al. do not teach the use of MS2 loop for recruiting an adaptor protein such as Fen1, Rad52 or a recombinase phiC31 integrase.
Konermann et al. teach inserting an aptamer sequence into a guide RNA, i.e., MS2 loop, as the hairpin structure for binding or recruitment of adaptor protein (see Figure 1 a-d on page 30).
Tran et al. demonstrates that a single strand annealing protein Rad52 enhances Cas9-MS2-CtIP gene editing system via homology directed repair (HDR) (see abstract and Figure 4c).
Park et al. teach installing attP sites using CRISPR/Cas9 at safe-harbor locus (COL1A) followed by phiC31 integrase to mediate targeted knock-in of large transgenes in pigs (see abstract). Park et al. also use knocking-in loxP site to demonstrate this concept (see Figure 1).
It would have been obvious to a person of ordinary skill in the art (POSITA) prior to the effective filing date of the instant application to make and use the composition taught by Anzalone et al. and insert an aptamer sequence into the guide RNA, i.e., MS2 loop, as the hairpin structure for binding or recruitment of adaptor protein such as Fen1, Rad52 or phiC31 integrase as taught by Konermann et al., Tran et al. and Park et al. A POSITA would have been motivated to make and use such composition because [1] Fen1 can excise 5’ DNA flap (see page 151, left column 1st para; and Fig. 1c); [2] Rad52 was shown to enhance Cas9 gene editing via HDR as taught by Tran et al. (see abstract and Figure 4c), and [3] installing attP sites using prime editing, similar to how Anzalone et al. installed loxP sites, allows the use of a recombinase phiC31 integrase to insert a long transgene as taught by Park et al. (see page 2, last para). A POSITA would have had a reasonable expectation of success to make and use such composition because all of the required biochemical reagents and techniques were readily available and rampantly used as evidenced by Anzalone et al, Konermann et al., Tran et al. and Park et al. prior to the filing of the instant application. For the reasons provided herein, the invention as claimed is prima facie obvious over the combined teachings of the prior art.
Conclusion
Claims 1-8, 10, 12-15 and 50-56 are rejected for the reasons as stated above. Applicants must respond to the objections/rejections in this Office action to be fully responsive in prosecution.
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JAE W LEE whose telephone number is (571)272-9949. The examiner can normally be reached on M-F between 9:00-6:00.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Manjunath 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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/JAE W LEE/
Examiner, Art Unit 1656
/MANJUNATH N RAO/Supervisory Patent Examiner, Art Unit 1656