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Human Polyclonal FAM175A Primary Antibody for IHC, ELISA - ABIN1002067
Kim, Huang, Chen: CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response. in Nature structural & molecular biology 2007
Show all 3 Pubmed References
Our data also suggest how ataxia telangiectasia mutated (ATM (show ATM Antibodies))-dependent BRCA1 dimerization may stabilize self-association of the entire BRCA1-A complex.
Results identified 16 novel rare variants in FAM175A but no significant difference in allele frequencies between cases and controls was observed which suggest no evidence that rare variants in ABRAXAS are associated with increased breast cancer risk in the population studied.
Demonstrate a mechanism involving IR-induced phosphorylation and dimerization of the BRCT/Abraxas complex for regulating Abraxas-mediated recruitment of BRCA1 in response to IR.
Abraxas and RAP80 (show UIMC1 Antibodies) were required for DNA damage resistance, G(2)-M checkpoint control, and DNA repair.
CCDC98 is a BRCA1 binding partner that mediates BRCA1 function in response to DNA damage.
CCDC98 is a mediator of BRCA1 function involved in the mammalian DNA damage response.
the human Ubc13 (show UBE2N Antibodies)/Rnf8 (show RNF8 Antibodies) ubiquitin ligases control foci formation of the Rap80 (show UIMC1 Antibodies)/Abraxas/Brca1/Brcc36 (show BRCC3 Antibodies) complex in response to DNA damage
Mutational analysis in 168 multiple-case breast/ovarian cancer families, negative for mutations in BRCA1 or BRCA2 (show BRCA2 Antibodies), suggests that CCDC98 does not play an important role as a high penetrance breast cancer susceptibility gene.
it seems unlikely that moderate to highly penetrant alleles of either RAP80 (show UIMC1 Antibodies) or Abraxas, confer a significantly high relative risk of breast cancer.
examined RAP80 (show UIMC1 Antibodies) and Abraxas expression and their effect on treatment outcome in non-small-cell lung cancer
Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the brca1-bard1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as a central scaffold protein that assembles the various components of the BRCA1-A complex and mediates the recruitment of brca1 (By similarity).
coiled-coil domain containing 98
, BRCA1-A complex subunit Abraxas
, Protein FAM175A
, abraxas protein
, coiled-coil domain-containing protein 98