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 6, 2025 is acknowledged. Claims 1-7, 9-11 and 14-15 are canceled. Claim 8 and 12-13 are amended. Claims 16-21 are newly added. Claims 8, 12-13 and new claims 16-21 are pending in this application. Election was made with traverse in the reply filed on June 30, 2025.
3. Claims 8, 12-13 and 16-21 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 6, 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Claim Rejections/Objections Withdrawn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 The objection to claims 8-9 and 12-15 is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 9 and 14-15.
The rejection of claim 14 on the basis that it contains an improper Markush grouping of alternatives is moot because the claim is canceled.
The rejection of claims 14-15 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 9 and 14-15 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, lack of scope of enablement is moot because the claims are canceled.
The rejection of claims 8-9 and 12-15 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 9 and 14-15.
The rejection of claims 8-9 and 12-13 under 35 U.S.C. 102(a)(1) as being anticipated by Mueller et al. (WO2013112922) as evidenced by Takeda et al. (Hypertension Re. 2020; 43:162-167) is withdrawn in response to Applicant’s amendment to the claims and cancelation of claims 9 and 14-15.
Claim Rejections/Objections Maintained
In view of the amendment filed on November 6, 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 8, 12-13 and 16-21 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 increasing the Discrimination Index (DI) values based on novel object recognition memory behavior test in an animal model of type 1 diabetes induced by intraperitoneal injection of streptozotocin (STZ ) or to an animal model of Chronic Cerebral Hypoperfusion Model induced by bilateral Carotid artery Stenosis (BCAS) or improving a decreased number of doublecortin-positive neural progenitor cells in the hippocampal dentate gyrus caused by diabetes in the mice of diabetes by administering a humanized anti-RGMa neutralizing antibody comprising SEQ ID NOs: 5-10 for LCDRs1-3 and HCDRs1-3 as compared to the animal model treated with a control antibody palivizumab, does not reasonably provide enablement for a method of treating including curing dementia including diabetic dementia and vascular dementia using the claimed anti-RGMa neutralizing antibody 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 8, 12-13 and 16-21 that is directed to a method of curing diabetic dementia or vascular dementia.
Claims 8, 12-13 and 16-21 as amended are drawn to a method of treating diabetic dementia or vascular dementia, 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 dementia including diabetic dementia or vascular dementia using the claimed anti-RGMa neutralizing antibody in view of paragraph [0081] of the instant specification filed on 11/06/2025.
Response to Arguments
On p. 8-9 of the response, Applicant argues that the rejection has been overcome in view of amendment to claim 8 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 curing dementia including diabetic dementia or vascular dementia using the claimed anti-RGMa neutralizing antibody in view of paragraph [0078] of the amended specification filed on 11/06/2025.
Based on paragraph [0078] of the amended specification filed on 11/06/2025, the definition of “treat” “treating” or “treatment” encompasses curing dementia including diabetic dementia or vascular dementia because the treatment is defined as “to extinguish, heal…such as disease and symptom”, which is to cure the claimed diseases.
[0078] 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 dementia including diabetic dementia or vascular dementia. Currently there is no cure for diabetic dementia or vascular dementia (see the factsheet of diabetic dementia or vascular dementia retrieved from the Mayo Clinic website and Kciuk et al., Intl. J. Mol. Sci. 2024; 25:11955. Doi.org/10.3390/ijms252211955, cited previously).
ii. The specification only disclosed that administration of the claimed anti-RGMa neutralizing antibody to an animal model of type 1 diabetes induced by intraperitoneal injection of streptozotocin (STZ ) or an animal model of Chronic Cerebral Hypoperfusion Model induced by bilateral Carotid artery Stenosis (BCAS) increased the Discrimination Index (DI) values based on a novel object recognition memory behavior test (Examples 1 and 3, Figures 1 and 3), and improved decreased number of doublecortin-positive neural progenitor cells in the hippocampal dentate gyrus caused by diabetes in the mice of diabetes as compared to the mice treated with a control antibody: palivizumab (Example 2, figure 2).
iii. The specification fails to provide sufficient guidance to enable one of skill in the art to practice the invention as it pertains to a method of curing diabetic dementia or vascular dementia. Thus, it is unpredictable whether the claimed method can treat and cure diabetic dementia or vascular dementia, 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 dementia including diabetic or vascular dementia can be treated and cured by the claimed anti-RGMa neutralizing antibody; 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 diabetic dementia or vascular dementia by administration of the claimed anti-RGMa neutralizing antibody.
Accordingly, the rejection of claims 8, 12-13 and 16-21 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 8, 12-13 and 16-21 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 Takeda et al. (Hypertension Re. 2020; 43:162-167), Shalimova et al. (J. Clin Endocrinol. Metab, 2019; 104:2239-2249) and Cholerton et al. (Spectrum Diabetes Journals, 2016; 29:210-219). The reference is necessitated by Applicant’s arguments. The rejection is maintained for the reasons of record and the reasons set forth below.
Claims 8, 12-13 and 16-21 as amended are drawn to a method of treating dementia that is diabetic dementia or vascular dementia, which comprises administration of an effective dose of an anti-RGMa neutralizing antibody, and wherein the anti-RGMa neutralizing antibody comprises SEQ ID NOs:5-10 for LCDRs1-3 and HCDRs1-3 respectively.
Response to Arguments
On p. 12-13 of the response, Applicant acknowledges that Cholerton and Takeda teach that diabetes is a risk factor for dementia and Hashimoto teaches treatment of diabetes mellites. But Applicant argues that diabetes mellites disclosed by Hashimoto is a metabolic disease and is not the claimed diabetic dementia which is a specific neurological disease, and distinct from Alzheimer’s disease and other forms of dementia; and that Cholerton and Takeda do not teach that diabetes mellites inherently involves diabetic dementia.
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 diabetic dementia or vascular dementia using an anti-RGMa neutralizing antibody comprising recited SEQ ID NOs: 4-10 for HCDRs1-3 and LCDRs1-3 respectively.
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. dementia including mild cognitive impairment (MCI), Alzheimer’s disease (AD), dementia associated with AD, diabetes mellites (i.e. diabetic dementia) and brain infarction, vascular amyloidosis, cerebral hemorrhage associated with amyloidosis (i.e. vascular dementia); see para.[0033]; [0053]-[0054]; [0057]; [0188]-[0189], claims 29-30), which meet the limitations recited in claims8, 12-13 and 16-21.
The patients with brain infarction, vascular amyloidosis, cerebral hemorrhage associated with amyloidosis disclosed by Hashimoto develop vascular dementia recited in claims 8 and 19 as evidenced by Takeda et al. (see p.162, abstract; p. 165) because brain infarction and cerebral hemorrhage damage blood vessels in the brain and block blood flow, which causes vascular dementia; and vascular Aβ accumulation (cerebral amyloid angiopathy, CAA) causes direct cerebrovascular damage and contributes to the pathogenesis of vascular dementia as taught by Takeda (see p.162-163; p. 164, 2nd col.-p. 165.).
The patients with diabetes including type I and type II diabetes mellites disclosed by Hashimoto develop diabetic dementia and vascular dementia recited in claims 8, 16 and 19 as evidenced by Shalimova et al. (see p. 2240-2243), Cholerton et al. (see p. 211-213) and Takeda et al. (see p.162-163; p. 164, 2nd col.-p. 165) because hyperinsulinemia caused by insulin resistance in type II diabetes results in a Aβ accumulation which causes direct cerebrovascular damage and contributes to the pathogenesis of vascular dementia, and hyperglycemia and hypoglycemia in type I diabetes result in memory impairment and cerebrovascular lesions, which contribute to the pathogenesis and progression of vascular dementia as taught by Shalimova et al. (see p. 2240-2243), Cholerton et al. (see p. 211-213), Takeda (see p.162-163; p. 164, 2nd col.-p. 165), which is also evidenced by paragraph [0076] of the instant specification. In addition, the animal model used in the instant specification is a type 1 diabetes animal model induced by intraperitoneal injection of streptozotocin (STZ).
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 claims 11-12, 17 and 20, and also recognizes an amino acid sequence including SEQ ID NO:36 recited in claims 13, 18 and 21. Thus, claims 8, 12-13 and 16-21 are anticipated by Hashimoto as evidenced by Cholerton and Takeda.
Accordingly, the rejection of claims 8, 12-13 and 16-21 under 35 U.S.C. 102(a)(1) & (a)(2) as being anticipated by Hashimoto as evidenced by Cholerton and Takeda is maintained.
Conclusion
8. NO CLAIM IS ALLOWED.
9. 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 dementia including mild cognitive impairment (MCI), Alzheimer’s disease (AD), dementia associated with AD, diabetes mellites (i.e. diabetic dementia) and brain infarction, vascular amyloidosis, cerebral hemorrhage associated with amyloidosis (i.e. vascular dementia), 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 dementia including mild cognitive impairment (MCI), Alzheimer’s disease (AD), dementia associated with AD, diabetes mellites (i.e. diabetic dementia) and brain infarction, vascular amyloidosis, cerebral hemorrhage associated with amyloidosis (i.e. vascular dementia), 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 dementia including mild cognitive impairment (MCI), Alzheimer’s disease (AD), dementia associated with AD, diabetes mellites (i.e. diabetic dementia) and brain infarction, vascular amyloidosis, cerebral hemorrhage associated with amyloidosis (i.e. vascular dementia), 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:36
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
10. 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.
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 on Monday-Thursday, 7:00am-5:30pm 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 on 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 an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see https://ppair-my.uspto.gov/pair/PrivatePair. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
Chang-Yu Wang
January 9, 2026
/CHANG-YU WANG/Primary Examiner, Art Unit 1675