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
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on May 8, 2026 has been entered.
RESPONSE TO AMENDMENT
Status of Application/Amendments/claims
3. Applicant’s amendment filed May 8, 2026 is acknowledged. Claims 1-10, 12-13 and 16-17 are canceled. Claim 11 is amended. Claims 24-25 are newly added. Claims 11, 14-15, 18-23 and new claims 24-25 are pending in this application. Applicant timely traversed the restriction (election) requirement in the reply filed on June 23, 2025.
4. Claims 11, 14-15 and 18-25 are under examination with respect to SEQ ID NO:36 for epitope and SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 in this office action.
5. Applicant’s arguments filed on May 8, 2026 have been fully considered but they are not deemed to be persuasive for the reasons set forth below.
Claim Rejections/Objections Withdrawn
6. The rejection of claims 11, 14-15 and 18-23 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, lack of scope of enablement is withdrawn in response to Applicant’s amendment to the claims.
Claim Rejections/Objections Maintained
In view of the amendment filed on May 8, 2026 the following rejections are maintained.
Claim Rejections - 35 USC § 102
7. 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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 11, 14-15 and 18-25 are rejected under 35 U.S.C. 102(a)(1) & (a)(2) as being anticipated by Hashimoto et al. (WO2016175236; also published as US2018/0100012; and issued as US10287346; the citations are based on US2018/0100012) as evidenced by Wingerchuk et al. (Lacet Neruol.2007;6:805-815) and Aube et al. (J. Immunol. 2014; 193:2438-2454) or Asgari et al. (Neurol. Neuroimmunol. Neuroinflamm. 2017; 4:e343; doi:10.1212/NXI.0000000000000343). The reference of Aube or Asgari is necessitated by Applicant’s amendment to the claims. The rejection is maintained for the reasons of record and the reasons set forth below.
Claims 11, 14-15 and 18-25 as amended are drawn to a method of treating acute phase neuromyelitis optica accompanied by disruption of the blood-spinal cord barrier, or pain symptoms in acute phase neuromyelitis optica, which comprises administration of an effective dose of an anti-RGMa neutralizing antibody to a mammal in need of treatment, wherein the anti-RGMa neutralizing antibody comprises SEQ ID NOs:5-10 for LCDRs1-3 and HCDRs1-3 respectively.
Briefly, Hashimoto et al. teach a method of treating acute phase neuromyelitis optica (NMO), or pain symptoms in acute phase NMO (see para.[0033]; [00532]-[0054]; [0057]; [0188]-[0189], claims 29-30), comprising administering to a mammal in need thereof an effective dose of a humanized anti-RGMa neutralizing antibody or an antigen-binding fragment thereof as in claims 11 and 14-15 (see paragraphs [0033]-[0046]; [0053]-[0057]; [0188]-[0189]; claims 17-31), and wherein the anti-RGMa neutralizing antibody binds to the amino acid sequence of SEQ ID NO:26, which is 100% identical to instant SEQ ID NO: 16 as in claim 15; and the anti-RGMa neutralizing antibody comprises VL of SEQ ID NO: 42, which comprises the amino acid sequences of instant SEQ ID NOs: 5-7 for LCDRs1-3 and VH of SEQ ID NO:41, which comprises instant SEQ ID NOs: 8-10 for HCDRs1-3 respectively recited in claim 11 (see the sequence alignments below; paragraphs [0033]-[0046]; [0053]-[0057]; [0188]-[0189]; claims 17-31). The patients with NMO in the Hashimoto’s method show optic neuritis and acute transverse myelitis and ocular pain, which is acute phase NMO, or pain symptoms in NMO as evidenced by Wingerchuk et al.(see p.806). In addition, the blood-brain barrier (BBB) disruption and blood-spinal cord barrier (BSCB) disruption are the hallmarks of NMO including acute NMO as evidenced by Aube (see p. 2438, abstract; p. 2449, 1st col., 2nd para.; p. 2452) or Asgari (see p.1, abstract; p.3-7). The treatment with the anti-RGMa neutralizing antibody disclosed by Hashimoto is performed after onset of acute phase NMO, which will promote recovery of neurological symptoms and suppress infiltration of granulocytes in the spinal cord recited in claims 24-25 because the method of Hashimoto uses the same material and the same active step in the same patient population. Thus, claims 11, 14-15 and 18-25 are anticipated by Hashimoto as evidenced by Wingerchuk and Aube or Asgari.
Response to Arguments
On p. 7 of the response, Applicant acknowledges that Hashimoto teaches a therapeutical agent for neurological diseases including neuromyelitis optica (NMO) and Wingerchuk is a review article focusing on differentiation between NMO and MS. But Applicant argues that i) Hashimoto does not anticipate instant claims because Hashimoto does not teach treatment of acute phase NMO; ii) Wingerchuk does not demonstrate that Hashimoto inherently discloses acute phase NMO or lacks teaching or suggestion regarding the use of anti-RGMa antibody for treatment of acute phase MO, repair of Blood-spinal cord barrier disruption.
Applicant's arguments have been fully considered but they are not found persuasive. Contrary to Applicant's arguments, the examiner asserts that based on MPEP §2131-2131.01, Hashimoto et al. (US2018/0100012 or WO2016175236 or US10287346) does teach the claimed method because:
i. Hashimoto teaches a therapeutical agent for neurological diseases including neuromyelitis optica (NMO). NMO is listed as one of limited numbers of neurological diseases and has been claimed for the use of treatment of immunological and neurological diseases including NMO (see claims 12-13 in corresponding issued patent US10287346).
ii. The method disclosed by Hashimoto uses the same material (i.e. an anti-RGMa neutralizing antibody including humanized anti-RGMa antibody comprising the claimed SEQ ID NOs: for LCDRs1-3 and HCDRs1-3; see the sequence alignment; para. [0019]; [0058]) and the same active step (i.e. administering to a mammal in need thereof; see para. [0195]-[0202]) in the same patient population (i.e. NMO, pain symptoms in NMO or acute phase NMO; see para.[0033]; [00532]-[0054]; [0057]; [0188]-[0189], claims 29-30). The treatment with the anti-RGMa neutralizing antibody disclosed by Hashimoto is performed after onset of acute phase NMO, which will promote recovery of neurological symptoms and suppress infiltration of granulocytes in the spinal cord recited in claims 24-25 because the method of Hashimoto uses the same material and the same active step in the same patient population.
The patients with NMO in the Hashimoto’s method show optic neuritis and acute transverse myelitis and ocular pain, which is acute phase NMO, or pain symptoms in NMO as evidenced by Wingerchuk et al.(see p.806). In addition, the blood-brain barrier (BBB) disruption and blood-spinal cord barrier (BSCB) disruption are the hallmarks of NMO including acute NMO as evidenced by Aube (see p. 2438, abstract; p. 2449, 1st col., 2nd para.; p. 2452) or Asgari (see p.1, abstract; p.3-7).
The anti-RGMa neutralizing antibody including humanized anti-RGMa antibody disclosed by Hashimoto comprises the claimed SEQ ID NOs: for LCDRs1-3 and HCDRs1-3 recited in claim 11, and also recognizes an amino acid sequence including SEQ ID NO:36 recited in claims 15, 20 and 21. Thus, claims11, 14-15 and 18-25 are anticipated by Hashimoto as evidenced by Wingerchuk and Aube or Asgari.
Accordingly, the rejection of claims 11, 14-15 and 18-25 under 35 U.S.C. 102(a)(1) & (a)(2) as being anticipated by Hashimoto as evidenced by Wingerchuk and Aube or Asgari is maintained.
Claim Rejections - 35 USC § 102
8. Claims 11, 14-15,18-23 and 25 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Harada et al. (Sci. Rept, 2018, Jan 8; 8:34. DOI:10.1038/s41598-017-18362-2, as in IDS) as evidenced by Hashimoto et al. (US10287346) and Aube et al. (2014) or Asgari et al. (2017). The reference of Aube or Asgari is necessitated by Applicant’s amendment to the claims. The rejection is maintained for the reasons of record and the reasons set forth below.
Briefly, Harada teaches a method of treating acute phase neuromyelitis optica (NMO) accompanied by disruption of blood-spinal cord barrier (BSCB), or pain symptoms in acute phase NMO (see p.1, abstract), comprising administering to a mammal in need thereof an effective dose of a humanized anti-RGMa neutralizing antibody; wherein the humanized anti-RGMa neutralizing antibody binds to an amino acid sequence of SEQ ID NO: 36, and comprises SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 respectively (see p.1, abstract; p. 2-7) because the humanized anti-RGMa neutralizing antibody is obtained and produced by the Mitsubishi Tanabe Pharmaceutical composition (see p.7) , which recognizes the epitope of SEQ ID NO:36 and comprises SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 respectively as evidenced by US10287346 (see the sequence alignments; col.27-28, claims 1-14). The blood-brain barrier (BBB) disruption and blood-spinal cord barrier (BSCB) disruption are the hallmarks of NMO including acute NMO as evidenced by Aube (see p. 2438, abstract; p. 2449, 1st col., 2nd para.; p. 2452) or Asgari (see p.1, abstract; p.3-7). The treatment with the anti-RGMa neutralizing antibody disclosed by Harada will suppress infiltration of granulocytes in the spinal cord recited in claim 25 because the method of Harada uses the same material and the same active step in the same patient population (see abstract). Thus, claims 11, 14-15,18-23 and 25 are anticipated by Harada as evidenced by Hashimoto and Aube et al. (2014) or Asgari.
Response to Arguments
On p. 8 of the response, Applicant acknowledges that Harada teaches suppression of the onset of NMO in an animal model by administering anti-RGMa antibodies before the NMO onset but argues that i) Harada does not teach the claimed method because the animal model of Harada does not reflect human clinical pathology of acute phase NMO and the treatment artificially bypass the initial key pathological stage of acute NMO, which is the infiltration of the anti-AQP4 antibody into the spinal cord due to the disruption of the BSCB (blood-spinal cord barrier).
Applicant's arguments have been fully considered but they are not found persuasive. Contrary to Applicant's arguments, the examiner asserts that based on MPEP §2131-2131.01, Harada does teach the claimed method because:
i. In response to applicant's argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e. the Harada’s model involves direct injection of NMO-IgG into spinal cord, which artificially bypass the initial key pathological stage of acute phase NMO…) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
ii. As admitted by Applicant on p. 2 [0005] of the instant specification, the onset of NMO is associated with severe pain in both acute phase and chronic phase. Further, the blood-brain barrier (BBB) disruption and blood-spinal cord barrier (BSCB) disruption are the hallmarks of NMO including acute NMO as evidenced by Aube (see p. 2438, abstract; p. 2449, 1st col., 2nd para.; p. 2452) or Asgari (see p.1, abstract; p.3-7).
iii. Instant claims are directed to treatment of acute NMO accompanied to BSCB in a mammal and not limited to humans. The animal model of acute NMO disclosed by Harada is a mammal and Harada teaches a method of treating NMO, acute phase NMO, or pain symptoms in NMO (see p.1, abstract), comprising administering to a mammal in need thereof an effective dose of a humanized anti-RGMa neutralizing antibody (see p.1, abstract; p. 2-7). The humanized anti-RGMa neutralizing antibody disclosed by Harada meets the claimed anti-RGMa neutralizing antibody comprising SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 respectively and binds to an amino acid sequence of SEQ ID NO: 36 because the humanized anti-RGMa neutralizing antibody is obtained and produced by the Mitsubishi Tanabe Pharmaceutical composition (see p.7) , which recognizes the epitope of SEQ ID NO:36 and comprises SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 respectively as evidenced by US10287346 (see the sequence alignments below; col.27-28, claims 1-14). Further, the blood-brain barrier (BBB) disruption and blood-spinal cord barrier (BSCB) disruption are the hallmarks of NMO including acute NMO as evidenced by Aube (see p. 2438, abstract; p. 2449, 1st col., 2nd para.; p. 2452) or Asgari (see p.1, abstract; p.3-7). The treatment with the anti-RGMa neutralizing antibody disclosed by Harada will suppress infiltration of granulocytes in the spinal cord recited in claim 25 because the method of Harada uses the same material and the same active step in the same patient population. Thus, claims 11, 14-15,18-23 and 25 are anticipated by Harada et al. as evidenced by US10287346.
Accordingly, the rejection of claims 11, 14-15,18-23 and 25 under 35 U.S.C. 102(a)(1) as being anticipated by Harada as evidenced by Hashimoto (US10287346) and Aube or Asgari is maintained.
Conclusion
9. NO CLAIM IS ALLOWED.
10. The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
WO201617523 (under the 102 rejection) teaches a method of treating acute phase neuromyelitis optica, or pain symptoms in neuromyelitis optica, which comprises administration of an effective dose of an anti-RGMa neutralizing antibody to a mammal in need of treatment, wherein the anti-RGMa neutralizing antibody comprises SEQ ID NOs:5-10 for LCDRs1-3 and HCDRs1-3 respectively (see the sequence alignment below).
SEQ ID NO:36
BDI27883
(NOTE: this sequence has 6 duplicates in the database searched.
See complete list at the end of this report)
ID BDI27883 standard; peptide; 14 AA.
XX
AC BDI27883;
XX
DT 15-DEC-2016 (first entry)
XX
DE Mouse anti-RGMa binding peptide, SEQ ID 26.
XX
KW RGMa; Repulsive guidance molecule A; antibody production;
KW antibody therapy; immune disorder; immunomodulator; neurological disease;
KW neuroprotective; prophylactic to disease; protein production;
KW protein therapy.
XX
OS Mus musculus.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 3; SEQ ID NO 26; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a mouse anti-RGMa
CC binding peptide, used in the invention for preventing neurological
CC disease.
XX
SQ Sequence 14 AA;
Query Match 100.0%; Score 75; Length 14;
Best Local Similarity 100.0%;
Matches 14; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EEVVNAVEDWDSQG 14
||||||||||||||
Db 1 EEVVNAVEDWDSQG 14
SEQ ID NO:5
BDI27899
(NOTE: this sequence has 2 duplicates in the database searched.
See complete list at the end of this report)
ID BDI27899 standard; protein; 107 AA.
XX
AC BDI27899;
XX
DT 15-DEC-2016 (first entry)
XX
DE Humanized anti-RGMa antibody light chain variable region, SEQ ID 42.
XX
KW RGMa; Repulsive guidance molecule A; antibody production;
KW antibody therapy; humanized antibody; immune disorder; immunomodulator;
KW light chain variable region; neurological disease; neuroprotective;
KW prophylactic to disease; protein production; protein therapy.
XX
OS Homo sapiens.
OS Mus musculus.
OS Chimeric.
OS Synthetic.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
DR N-PSDB; BDI27901.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 18; SEQ ID NO 42; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a humanized anti-
CC RGMa antibody light chain variable region, used in the invention for
CC preventing neurological disease.
XX
SQ Sequence 107 AA;
Query Match 100.0%; Score 53; Length 107;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RASQDISSYLN 11
|||||||||||
Db 24 RASQDISSYLN 34
SEQ ID NO:6
BDI27888
ID BDI27888 standard; peptide; 7 AA.
XX
AC BDI27888;
XX
DT 15-DEC-2016 (first entry)
XX
DE Mouse anti-RGMa antibody light chain variable region CDR2, SEQ ID 31.
XX
KW RGMa; Repulsive guidance molecule A; antibody; antibody production;
KW antibody therapy; immune disorder; immunomodulator;
KW light chain variable region; neurological disease; neuroprotective;
KW prophylactic to disease; protein production; protein therapy.
XX
OS Mus musculus.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 17; SEQ ID NO 31; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a mouse anti-RGMa
CC antibody light chain variable region CDR2, used in the invention for
CC preventing neurological disease.
XX
SQ Sequence 7 AA;
ALIGNMENT:
Query Match 100.0%; Score 37; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 YTSRLHS 7
|||||||
Db 1 YTSRLHS 7
SEQ ID NO:7
BDI27889
(NOTE: this sequence has 5 duplicates in the database searched.
See complete list at the end of this report)
ID BDI27889 standard; peptide; 7 AA.
XX
AC BDI27889;
XX
DT 15-DEC-2016 (first entry)
XX
DE Mouse anti-RGMa antibody light chain variable region CDR3, SEQ ID 32.
XX
KW RGMa; Repulsive guidance molecule A; antibody; antibody production;
KW antibody therapy; immune disorder; immunomodulator;
KW light chain variable region; neurological disease; neuroprotective;
KW prophylactic to disease; protein production; protein therapy.
XX
OS Mus musculus.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 17; SEQ ID NO 32; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a mouse anti-RGMa
CC antibody light chain variable region CDR3, used in the invention for
CC preventing neurological disease.
XX
SQ Sequence 7 AA;
Query Match 100.0%; Score 36; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QQLNTLP 7
|||||||
Db 1 QQLNTLP 7
SEQ ID NO:8
BDI27898
(NOTE: this sequence has 2 duplicates in the database searched.
See complete list at the end of this report)
ID BDI27898 standard; protein; 116 AA.
XX
AC BDI27898;
XX
DT 15-DEC-2016 (first entry)
XX
DE Humanized anti-RGMa antibody heavy chain variable region, SEQ ID 41.
XX
KW RGMa; Repulsive guidance molecule A; antibody production;
KW antibody therapy; heavy chain variable region; humanized antibody;
KW immune disorder; immunomodulator; neurological disease; neuroprotective;
KW prophylactic to disease; protein production; protein therapy.
XX
OS Mus musculus.
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
DR N-PSDB; BDI27900.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 18; SEQ ID NO 41; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a humanized anti-
CC RGMa antibody heavy chain variable region, used in the invention for
CC preventing neurological disease.
XX
SQ Sequence 116 AA;
Query Match 100.0%; Score 32; Length 116;
Best Local Similarity 100.0%;
Matches 5; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DAWMD 5
|||||
Db 31 DAWMD 35
SEQ ID NO:9
BDI27898
(NOTE: this sequence has 2 duplicates in the database searched.
See complete list at the end of this report)
ID BDI27898 standard; protein; 116 AA.
XX
AC BDI27898;
XX
DT 15-DEC-2016 (first entry)
XX
DE Humanized anti-RGMa antibody heavy chain variable region, SEQ ID 41.
XX
KW RGMa; Repulsive guidance molecule A; antibody production;
KW antibody therapy; heavy chain variable region; humanized antibody;
KW immune disorder; immunomodulator; neurological disease; neuroprotective;
KW prophylactic to disease; protein production; protein therapy.
XX
OS Mus musculus.
OS Homo sapiens.
OS Chimeric.
OS Synthetic.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
DR N-PSDB; BDI27900.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 18; SEQ ID NO 41; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a humanized anti-
CC RGMa antibody heavy chain variable region, used in the invention for
CC preventing neurological disease.
XX
SQ Sequence 116 AA;
Query Match 100.0%; Score 98; Length 116;
Best Local Similarity 100.0%;
Matches 19; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EIRSKANNHATYYAESVKG 19
|||||||||||||||||||
Db 50 EIRSKANNHATYYAESVKG 68
SEQ ID NO:10
BDI27892
(NOTE: this sequence has 5 duplicates in the database searched.
See complete list at the end of this report)
ID BDI27892 standard; peptide; 5 AA.
XX
AC BDI27892;
XX
DT 15-DEC-2016 (first entry)
XX
DE Mouse anti-RGMa antibody heavy chain variable region CDR3, SEQ ID 35.
XX
KW RGMa; Repulsive guidance molecule A; antibody; antibody production;
KW antibody therapy; heavy chain variable region; immune disorder;
KW immunomodulator; neurological disease; neuroprotective;
KW prophylactic to disease; protein production; protein therapy.
XX
OS Mus musculus.
XX
CC PN WO2016175236-A1.
XX
CC PD 03-NOV-2016.
XX
CC PF 27-APR-2016; 2016WO-JP063166.
XX
PR 28-APR-2015; 2015JP-00091095.
XX
CC PA (MTSB ) MITSUBISHI TANABE PHARMA CORP.
CC PA (OSAU ) UNIV OSAKA.
CC PA (UYCH-) UNIV CHIBA NAT CORP.
XX
CC PI Hashimoto M, Yamashita T;
XX
DR WPI; 2016-68867X/79.
XX
CC PT New isolated repulsive guidance molecule-A (RGMa) binding protein useful
CC PT in pharmaceutical composition for preventing neurological disease e.g.
CC PT amyloidosis and retina dystrophy, capable of not inhibiting binding of
CC PT RGMa and neogenin.
XX
CC PS Claim 17; SEQ ID NO 35; 74pp; Japanese.
XX
CC The present invention relates to a novel isolated RGMa binding protein
CC useful for preventing neurological disease. The invention further relates
CC to: (1) a nucleic acid molecule encoding protein part of the RGMa binding
CC protein; (2) a recombinant vector comprises the nucleic acid molecule;
CC (3) a host cell comprises the recombinant vector; (4) a method for
CC preparing the RGMa binding protein; (5) an isolated anti-RGMa antibody;
CC (5) an isolated anti-RGMa antibody; (6) a nucleic acid molecule encoding
CC protein part of the anti-RGMa antibody; (7) a recombinant vector
CC comprises the nucleic acid molecule; (8) a host cell comprises the
CC recombinant vector; and (9) a method for preparing the above-mentioned
CC anti-RGMa antibody. The RGMa binding protein of the invention is also
CC used for immunological disease. The present sequence is a mouse anti-RGMa
CC antibody heavy chain variable region CDR3, used in the invention for
CC preventing neurological disease.
XX
SQ Sequence 5 AA;
Query Match 100.0%; Score 28; Length 5;
Best Local Similarity 100.0%;
Matches 5; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RDGAY 5
|||||
Db 1 RDGAY 5
US20180100012 (under the 102 rejection) teaches a method of treating acute phase neuromyelitis optica, or pain symptoms in neuromyelitis optica, which comprises administration of an effective dose of an anti-RGMa neutralizing antibody to a mammal in need of treatment, wherein the anti-RGMa neutralizing antibody comprises SEQ ID NOs:5-10 for LCDRs1-3 and HCDRs1-3 respectively (see the sequence alignment below).
SEQ ID NO:36
US-15-569-382-26
(NOTE: this sequence has 7 duplicates in the database searched.
See complete list at the end of this report)
Sequence 26, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 26
LENGTH: 14
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 75; Length 14;
Best Local Similarity 100.0%;
Matches 14; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EEVVNAVEDWDSQG 14
||||||||||||||
Db 1 EEVVNAVEDWDSQG 14
SEQ ID NO:5
US-15-569-382-42
(NOTE: this sequence has 3 duplicates in the database searched.
See complete list at the end of this report)
Sequence 42, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 42
LENGTH: 107
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody light chain
Query Match 100.0%; Score 53; Length 107;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RASQDISSYLN 11
|||||||||||
Db 24 RASQDISSYLN 34
SEQ ID NO:6
US-15-569-382-31
Filing date in PALM: 2017-10-25
Sequence 31, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 31
LENGTH: 7
TYPE: PRT
ORGANISM: Mus musculus
ALIGNMENT:
Query Match 100.0%; Score 37; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 YTSRLHS 7
|||||||
Db 1 YTSRLHS 7
SEQ ID NO:7
US-15-569-382-32
(NOTE: this sequence has 7 duplicates in the database searched.
See complete list at the end of this report)
Sequence 32, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 32
LENGTH: 7
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 36; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QQLNTLP 7
|||||||
Db 1 QQLNTLP 7
SEQ ID NO:8
US-15-569-382-41
(NOTE: this sequence has 3 duplicates in the database searched.
See complete list at the end of this report)
Sequence 41, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 41
LENGTH: 116
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody heavy chain
Query Match 100.0%; Score 32; Length 116;
Best Local Similarity 100.0%;
Matches 5; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DAWMD 5
|||||
Db 31 DAWMD 35
SEQ ID NO:9
US-15-569-382-41
(NOTE: this sequence has 3 duplicates in the database searched.
See complete list at the end of this report)
Sequence 41, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 41
LENGTH: 116
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody heavy chain
Query Match 100.0%; Score 98; Length 116;
Best Local Similarity 100.0%;
Matches 19; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EIRSKANNHATYYAESVKG 19
|||||||||||||||||||
Db 50 EIRSKANNHATYYAESVKG 68
SEQ ID NO:10
US-15-569-382-41
(NOTE: this sequence has 3 duplicates in the database searched.
See complete list at the end of this report)
Sequence 41, US/15569382
Publication No. US20180100012A1
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 41
LENGTH: 116
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody heavy chain
Query Match 100.0%; Score 28; Length 116;
Best Local Similarity 100.0%;
Matches 5; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RDGAY 5
|||||
Db 101 RDGAY 105
US10287346 (under the 102 rejection) teaches a method of treating acute phase neuromyelitis optica, or pain symptoms in neuromyelitis optica, which comprises administration of an effective dose of an anti-RGMa neutralizing antibody to a mammal in need of treatment, wherein the anti-RGMa neutralizing antibody comprises SEQ ID NOs:5-10 for LCDRs1-3 and HCDRs1-3 respectively, which recognizes an amino acid sequence selected from SEQ ID NOs: 36, 37 and 39 (see the sequence alignment below; claims 1-14; col.27-28).
SEQ ID NO:36
US-15-569-382-26
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 26, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 26
LENGTH: 14
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 75; Length 14;
Best Local Similarity 100.0%;
Matches 14; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EEVVNAVEDWDSQG 14
||||||||||||||
Db 1 EEVVNAVEDWDSQG 14
SEQ ID NO:5
US-15-569-382-42
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 42, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 42
LENGTH: 107
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody light chain
Query Match 100.0%; Score 53; Length 107;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RASQDISSYLN 11
|||||||||||
Db 24 RASQDISSYLN 34
SEQ ID NO:6
US-15-569-382-42
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 42, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 42
LENGTH: 107
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody light chain
Query Match 100.0%; Score 37; Length 107;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 YTSRLHS 7
|||||||
Db 50 YTSRLHS 56
SEQ ID NO:7
US-15-569-382-32
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 32, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 32
LENGTH: 7
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 36; Length 7;
Best Local Similarity 100.0%;
Matches 7; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QQLNTLP 7
|||||||
Db 1 QQLNTLP 7
SEQ ID NO:8
US-15-569-382-41
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 41, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 41
LENGTH: 116
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody heavy chain
Query Match 100.0%; Score 32; Length 116;
Best Local Similarity 100.0%;
Matches 5; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DAWMD 5
|||||
Db 31 DAWMD 35
SEQ ID NO:9
US-15-569-382-41
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 41, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 41
LENGTH: 116
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody heavy chain
Query Match 100.0%; Score 98; Length 116;
Best Local Similarity 100.0%;
Matches 19; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EIRSKANNHATYYAESVKG 19
|||||||||||||||||||
Db 50 EIRSKANNHATYYAESVKG 68
SEQ ID NO:10
US-15-569-382-41
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 41, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 41
LENGTH: 116
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Synthetic humanized antibody heavy chain
Query Match 100.0%; Score 28; Length 116;
Best Local Similarity 100.0%;
Matches 5; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 RDGAY 5
|||||
Db 101 RDGAY 105
SEQ ID NO:16
US-15-569-382-1
Filing date in PALM: 2017-10-25
Sequence 1, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 1
LENGTH: 450
TYPE: PRT
ORGANISM: Homo sapiens
ALIGNMENT:
Query Match 100.0%; Score 129; Length 450;
Best Local Similarity 100.0%;
Matches 23; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 PCKILKCNSEFWSATSGSHAPAS 23
|||||||||||||||||||||||
Db 47 PCKILKCNSEFWSATSGSHAPAS 69
SEQ ID NO:37
US-15-569-382-27
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 27, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 27
LENGTH: 14
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 75; Length 14;
Best Local Similarity 100.0%;
Matches 14; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 NQQIDFQAFHTNAE 14
||||||||||||||
Db 1 NQQIDFQAFHTNAE 14
SEQ ID NO:38
US-15-569-382-28
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 28, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 28
LENGTH: 11
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 63; Length 11;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 PTAPETFPYET 11
|||||||||||
Db 1 PTAPETFPYET 11
SEQ ID NO:39
US-15-569-382-29
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 29, US/15569382
Patent No. 10287346
GENERAL INFORMATION
APPLICANT: Mitsubishi Tanabe Pharma Corporation
APPLICANT: Osaka University
APPLICANT: National University Corporation Chiba University
TITLE OF INVENTION: RGMa BINDING PROTEIN AND USE THEREOF
FILE REFERENCE: 730591
CURRENT APPLICATION NUMBER: US/15/569,382
CURRENT FILING DATE: 2017-10-25
PRIOR APPLICATION NUMBER: PCT/JP2016/063166
PRIOR FILING DATE: 2016-04-27
PRIOR APPLICATION NUMBER: JP2015-091095
PRIOR FILING DATE: 2015-04-28
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 29
LENGTH: 11
TYPE: PRT
ORGANISM: Mus musculus
Query Match 100.0%; Score 58; Length 11;
Best Local Similarity 100.0%;
Matches 11; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 KLPVEDLYYQA 11
|||||||||||
Db 1 KLPVEDLYYQA 11
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to CHANG-YU WANG whose telephone number is (571)272-4521. The examiner can normally be reached Monday-Thursday, 7:00am-5:00pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
May 30, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675
Prosecution Insights