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ImmunohistochemistryAntibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- ABIN965699 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-BRCA1 Interacting Protein C-terminal Helicase 1 (BRIP1) (C-Term) antibody
- Antibody type
- Polyclonal
- Antigen
- Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human BRIP1(ATP-dependent RNA helicase)
- Reactivity
- Human
- Host
- Rabbit
- Vial size
- 0.1mg
Submitted references The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations.
Large-scale characterization of HeLa cell nuclear phosphoproteins.
The BRCT domain is a phospho-protein binding domain.
BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.
Cantor S, Drapkin R, Zhang F, Lin Y, Han J, Pamidi S, Livingston DM
Proceedings of the National Academy of Sciences of the United States of America 2004 Feb 24;101(8):2357-62
Proceedings of the National Academy of Sciences of the United States of America 2004 Feb 24;101(8):2357-62
Large-scale characterization of HeLa cell nuclear phosphoproteins.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP
Proceedings of the National Academy of Sciences of the United States of America 2004 Aug 17;101(33):12130-5
Proceedings of the National Academy of Sciences of the United States of America 2004 Aug 17;101(33):12130-5
The BRCT domain is a phospho-protein binding domain.
Yu X, Chini CC, He M, Mer G, Chen J
Science (New York, N.Y.) 2003 Oct 24;302(5645):639-42
Science (New York, N.Y.) 2003 Oct 24;302(5645):639-42
BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.
Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, Wahrer DC, Sgroi DC, Lane WS, Haber DA, Livingston DM
Cell 2001 Apr 6;105(1):149-60
Cell 2001 Apr 6;105(1):149-60
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