Anti-NBS1 (Nibrin), C-terminal antibody produced in rabbit

Nibrin (NBS1) is made up of 754 amino acids.

Nibrin is encoded by the gene mapped to human chromosome 8q21.3. The protein has two domains found in the cell cycle checkpoint proteins, forkhead-associated domain (FHA), and an adjacent breast cancer carboxy-terminal domain (BRCT).

synthetic peptide corresponding to amino acids 735-753 of human NBS1 (nibrin), conjugated to KLH via an N-terminal added cysteine residue. The immunizing peptide differs from the rat and mouse corresponding sequences in two amino acids.

Anti-NBS1 (Nibrin), C-terminal antibody produced in rabbit has been used in:

• immunoblotting
• immunofluorescence
• immunoprecipitation

Nibrin (NBS1) is involved in stabilizing genomes and has a role in development of cancers. It also takes part in the repair mechanism after double strand breaks in the DNA. Mutations in the gene encoding NBS1 have been associated with Nijmegen breakage syndrome (NBS).

Nibrin (NBS1) was first isolated as a protein involved in DNA repair through analysis of mutations in patients with this syndrome. p95/NBS1 (Nibrin) deficiency abrogates the formation of the Meiotic recombination 11 homolog 1 (MRE11)/RAD50 ionizing radiation-induced foci, revealing a molecular link between double-strand break (DSB) repair and cell cycle checkpoint functions. The phenotypic similarities between ataxia-telangiectasia (AT) and Nijmegen breakage syndrome had suggested that ataxia-telangiectasia mutated gene (ATM) and NBS1 functions in a common signaling pathway. This was confirmed by the finding that in response to ionizing radiation, NBS1 is phosphorylated in Ser343 in an ataxia-telangiectasia mutated ATM-dependent manner.

Solution in 0.01 M phosphate buffered saline containing 15 mM sodium azide.

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