BRCA1 Interacting Protein C-terminal Helicase 1 (BRIP1) (C-Term) antibody

Antigen: BRCA1 Interacting Protein C-terminal Helicase 1 (BRIP1)

Synonyms: OF, BACH1, FANCJ, FLJ90232, MGC126521, MGC126523, Bach1, 3110009N10Rik, 8030460J03Rik, MGC68622, BRIP1, fancj, si:ch211-158l18.1

Binding Site: C-Term

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human

Conjugate: Un-conjugated

Application: Immunohistochemistry (IHC)

Catalog no.: ABIN965699

Additional Information

Alternative name: BRIP1

Immunogen: Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human BRIP1(ATP-dependent RNA helicase)

Description: BRIP1(ATP-dependent RNA helicase Is a DNA-dependent ATPase and 5' to 3' DNA helicase which is required for the maintenance of chromosomal stability. BRIP1 acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. BRIP1 is involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1. BRIP1 binds directly to the BRCT domains of BRCA1. BRIP1 is ubiquitously expressed, with highest levels in testis. Defects in BRIP1 are a cause of susceptibility to breast cancer (BC). BC is an extremely common malignancy, affecting one in eight women during their lifetime. A positive family history has been identified as major contributor to risk of development of the disease, and this link is striking for early-onset breast cancer. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage), and defective DNA repair.
Synonyms: FACJ (Fanconi anemia group J protein), BRCA1(interacting protein C-terminal helicase 1)

Application Details

Restrictions: For Research Use only

Publications

Product: Cantor, Bell, Ganesan et al.: "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function." in: Cell, Vol. 105, Issue 1, pp. 149-60, 2001 (PubMed).

Yu, Chini, He et al.: "The BRCT domain is a phospho-protein binding domain." in: Science (New York, N.Y.), Vol. 302, Issue 5645, pp. 639-42, 2003 (PubMed).

Cantor, Drapkin, Zhang et al.: "The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 8, pp. 2357-62, 2004 (PubMed).

Beausoleil, Jedrychowski, Schwartz et al.: "Large-scale characterization of HeLa cell nuclear phosphoproteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 33, pp. 12130-5, 2004 (PubMed).