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N3037

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 95 kDa

species reactivity

human

technique(s)

immunoprecipitation (IP): 2-4 μg using HeLa cell lysates
indirect immunofluorescence: 5-10 μg/mL
microarray: suitable
western blot: 0.25-0.5 μg/mL using extracts of 293T cells transfected with recombinant NBS1
western blot: 0.5-1 μg/mL using MCF7 nuclear extracts

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... NBN(4683)
mouse ... Nbn(27354)
rat ... Nbn(85482)

General description

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).

Immunogen

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Nijmegen breakage syndrome gene (NBS1) is not the tumor suppressor gene at 8q21. 3 involved in colorectal carcinoma
Varon R, et al.
Oncology Reports, 9(4), 709-711 (2002)
Domenica Cilli et al.
PloS one, 9(12), e114651-e114651 (2014-12-09)
Nibrin (also named NBN or NBS1) is a component of the MRE11/RAD50/NBN complex, which is involved in early steps of DNA double strand breaks sensing and repair. Mutations within the NBN gene are responsible for the Nijmegen breakage syndrome (NBS).
ATM phosphorylates p95/nbs1 in an S-phase checkpoint pathway
Lim DS, et al.
Nature, 404(6778), 613-613 (2000)
Wenxiang Fang et al.
Mutation research, 770, 61-68 (2015-03-17)
NBS1 plays pivotal roles in maintaining genomic stability and cancer development. The exon variant rs1805794G>C (p.Glu185Gln) of NBS1 has been frequently studied in several association studies. However, the results were conflicting. Also, the function of this variant has never been
Michal Goldberg et al.
Nature, 421(6926), 952-956 (2003-02-28)
MRE11, RAD50 and NBS1 form a highly conserved protein complex (the MRE11 complex) that is involved in the detection, signalling and repair of DNA damage. We identify MDC1 (KIAA0170/NFBD1), a protein that contains a forkhead-associated (FHA) domain and two BRCA1

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