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
RESPONSE TO AMENDMENT
Status of Application/Amendments/claims
2. Applicant’s amendment filed November 06, 2025 is acknowledged. Claims 1-10, 12-13 and 16-17 are canceled. Claims 11, and 14-15 are amended. Claims 18-23 are newly added. Claims 11, 14-15 and new claims 18-23 are pending in this application. Election was made with traverse in the reply filed on June 23, 2025.
3. Claims 11, 14-15 and 18-23 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.
4. Applicant’s arguments filed on November 06, 2025 have been fully considered but they are not deemed to be persuasive for the reasons set forth below.
Claim Rejections/Objections Withdrawn
5. The objection to claims 11-12 and 14-17 is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 12 and 16-17.
The rejection of claim 16 on the basis that it contains an improper Markush grouping of alternatives is moot because the claim is canceled.
The rejection of claims 16-17 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite is moot because the claims are canceled.
The rejection of claims 12 and 16-17 under 35 U.S.C. 102(a)(1) & (a)(2) as being anticipated by Hashimoto et al. (WO2016175236; published as US2018/0100012 and issued as US10287346 as evidenced by Wingerchuk et al. (Lacet Neruol.2007;6:805-815) is moot because the claims are canceled
The rejection of claims 12 and 16-17 under 35 U.S.C. 102(a)(1) as being anticipated by Harada et al. (Sci. Rept, 2018, Jan 8; 8:34) as evidenced by Hashimoto et al. (US10287346) is moot because the claims are canceled.
The rejection of claims 11-12 and 14-15 under 35 U.S.C. 102(a)(1) as being anticipated by Mueller et al. (WO2013112922) is withdrawn in response to Applicant’s amendment to the claims and cancelation of claim 12.
Claim Rejections/Objections Maintained
In view of the amendment filed on November 06, 2025, the following rejections are maintained.
Claim Rejections - 35 USC § 112
6. 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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 11, 14-15 and 18-23 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for reducing symptoms of neurological impairment, suppressing intraspinal leakage of rat IgG, increasing recovery from the 50% paw withdrawal threshold decrease and inhibiting granulocyte infiltration in the spinal cord in an animal model of NMO by administering an anti-RGMa neutralizing antibody comprising SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 respectively as compared to NMO rats treated with a control antibody: palivizumab, wherein the NMO animal model is induced by injection with MBP and anti-AQP4 monoclonal antibody E5415A, does not reasonably provide enablement for a method of preventing or treating acute phase neuromyelitis optica or pain symptoms in neuromyelitis optica using the claimed structurally and functionally undefined RGMa inhibiting substance including structurally and functionally undefined anti-RGMa neutralizing antibodies or antigen-binding fragments thereof as broadly claimed. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims. In addition, the specification does not enable the invention of claims 11, 14-15 and 18-23 that is directed to a method of curing.
Claims 11, 14-15 and 18-23 as amended are drawn to a method of treating acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica, comprising administering an effective dose of an anti-RGMa neutralizing antibody to a mammal in need thereof, wherein the anti-RGMa neutralizing antibody comprises a light chain variable region (VL) and a heavy chain variable region (VH), wherein the VL comprises an LCDR1 comprising the amino acid sequence of SEQ ID NO:5, an LCDR2 comprising the amino acid sequence of SEQ ID NO:6, and an LCDR3 comprising the amino acid sequence of SEQ ID NO:7 and the VH comprises an HCDR1 comprising the amino acid sequence of SEQ ID NO:8, an HCDR2 comprising the amino acid sequence of SEQ ID NO:9, and an LCDR3 comprising the amino acid sequence of SEQ ID NO:10.
The claims encompass a method of treating and curing acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica using the claimed anti-RGMa neutralizing antibody in view of paragraphs [0027], [0081] and [0082] of instant specification or paragraphs [0086], and [0171]-[0172] of the published application (US2024/0287167).
Response to Arguments
On p. 8 of the response, Applicant argues that the rejection has been overcome in view of amendment to claim 11 and the specification, which no longer includes “prevention”.
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 §2164, MPEP §§2164.01-2164.06(b) & 2164.08, the specification provides insufficient guidance to enable a skilled artisan to practice the full scope of the claimed invention without undue experimentation because:
i. Claims 11, 14-15 and 18-23 as amended also encompass a method of curing acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica using the claimed anti-RGMa neutralizing antibody in view of paragraph [0081] of the amended specification filed on 11/06/2025.
Based on paragraph [0081] of the amended specification filed on 11/06/2025, the definition of “treat” “treating” or “treatment” encompasses curing acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica because the treatment is defined as “to extinguish, heal…such as disease and symptom”, which is to cure the claimed diseases.
[0081] In this regard, a “treatment” includes any treatment of a disease in a therapeutic objective, preferably a mammal, and especially a human, so as to extinguish, heal, alleviate, or mitigate such a disease and symptom.
However, as previously made of record, neither the specification/prior art provides support that administration of the claimed anti-RGMa neutralizing antibody can cure acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica. Currently there is no cure for acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optic (see the factsheet of acute phase neuromyelitis optica retrieved from the Mayo Clinic website).
ii. The specification only disclosed administration of the claimed anti-RGMa neutralizing antibody to NMO rats reduced symptoms of neurological impairment, suppressed intraspinal leakage of rat IgG, resulted in faster recovery from the 50% paw withdrawal threshold decrease and inhibited granulocyte infiltration in the spinal cord of the NMO rats treated with the claimed anti-RGMa neutralizing antibody compared to the NMO rats treated with a control antibody (i.e. palivizumab) (see Examples 1, and 3-5, figures 1 and 4-6).
iii. The specification fails to provide guidance to enable one of skill in the art to practice the invention as it pertains to a method of curing acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica. Thus, it is unpredictable whether the claimed method can treat and cure acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica, indicating that undue experimentation is required by a skilled artisan to perform while practicing the claimed invention.
Note that the scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without such guidance, it is unpredictable whether AD can be treated by the claimed RdCVF2 polypeptide; and thus the experimentation left to those skilled in the art is extensive and undue. See Ex parte Forman, 230 USPQ 546 (Bd. Pat. App. & Int. 1986). Thus, the skilled artisan cannot readily know how to use the claimed invention as currently claimed without further undue experimentation. In re Marzocchi, 439 F.2d 220, 223-24,
169 USPQ 367, 369-70 (CCPA 1971)” See MPEP § 2164.03.
Therefore, in view of the breadth of the claims, the lack of guidance in the specification, no working examples, the unpredictability of inventions, and the current status of the art, undue experimentation would be required by a skilled artisan to perform in order to practice the claimed invention as it pertains to a method for treating and curing acute phase neuromyelitis optica, or pain symptoms in neuromyeltitis optica by administration of the claimed anti-RGMa neutralizing antibody.
Accordingly, 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 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 18-23 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).. The rejection is maintained for the reasons of record and the reasons set forth below.
Claims 11, 14-15 and 18-23 as amended are drawn to 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.
Response to Arguments
On p. 11-12 of the response, Applicant acknowledges that Hashimoto teaches a therapeutical agent for neurological diseases including neuromyelitis optica (NMO). 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.
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. instant claims are directed to treating acute phase neuromyelitis optica (NMO) or pain symptoms in NMO using an anti-RGMa neutralizing antibody comprising recited SEQ ID NOs: 4-10 for HCDRs1-3 and LCDRs1-3 respectively.
ii. As acknowledged by Applicant on p. 12 of the response, 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).
iii. 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 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).
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 18-23 are anticipated by Hashimoto as evidenced by Wingerchuk.
Accordingly, the rejection of claims 11, 14-15 and 18-23 under 35 U.S.C. 102(a)(1) & (a)(2) as being anticipated by Hashimoto as evidenced by Wingerchuk is maintained.
Claim Rejections - 35 USC § 102
8. Claims 11, 14-15 and 18-23 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).
Response to Arguments
On p. 12-13 of the response, Applicant argues that i) Harada does not teach the claimed method because Harada is directed to the secondary phase of NMO, not acute phase NMO (see p. 5, last paragraph); ii) Harad’s animal model does not reflect acute phase pathology because 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, 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, which is the infiltration of the anti-AQP4 antibody into the spinal cord due to the disruption of the BSCB (blood-spinal cord barrier)) 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.
iii. Instant claims are directed to treating acute phase neuromyelitis optica (NMO) or pain symptoms in NMO using an anti-RGMa neutralizing antibody comprising recited SEQ ID NOs: 4-10 for HCDRs1-3 and LCDRs1-3 respectively.
iv. 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; col.27-28, claims 1-14). Thus, claims 11, 14-15 and 18-23 are anticipated by Harada et al. as evidenced by US10287346.
Accordingly, the rejection of claims 11, 14-15 and 18-23 under 35 U.S.C. 102(a)(1) as being anticipated by Harada as evidenced by Hashimoto (US10287346) 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
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Db 1 KLPVEDLYYQA 11
11. 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 nonprovisional extension fee (37 CFR 1.17(a)) 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.
12. 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 on Monday-Thursday, 7:00am-5:30pm EST.
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Chang-Yu Wang
January 7, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675