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AB175800

Anti-p95/NBS1 antibody

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(6 Publications)

Rabbit Polyclonal p95/NBS1 antibody. Suitable for IP, WB, IHC-P, ICC/IF and reacts with Human, Mouse samples. Cited in 6 publications. Immunogen corresponding to Recombinant Fragment Protein within Human NBN aa 250-500.

View Alternative Names

NBS, NBS1, P95, NBN, Nibrin, Cell cycle regulatory protein p95, Nijmegen breakage syndrome protein 1, hNbs1

4 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-p95/NBS1 antibody (AB175800)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-p95/NBS1 antibody (AB175800)

Immunohistochemistry (formalin/PFA-fixed paraffin-embedded) analysis of Human linfoid tissue labelling p95/NBS1 with ab175800 at 1 : 1000. Antigen retrieval was by microwave boiling for 7 minutes in 10mM TrisHCl, pH9. Left - 4X, Right - 20X.

Immunocytochemistry/ Immunofluorescence - Anti-p95/NBS1 antibody (AB175800)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-p95/NBS1 antibody (AB175800)

Immunocytochemistry/Immunofluorescence analysis of U2OS cells labelling p95/NBS1 with ab175800 at 1 : 1000. Cells were fixed with PFA and permeabilized with methanol for 2 minutes. Cells were incubated with the primary anitbody overnight at room temperature. Left - p95/NBS1, Middle - DAPI, Right - Merge.

Immunoprecipitation - Anti-p95/NBS1 antibody (AB175800)
  • IP

Supplier Data

Immunoprecipitation - Anti-p95/NBS1 antibody (AB175800)

Immunoprecipitation analysis of U2OS cells labelling p95/NBS1 with ab175800. Protein A beads were crosslinked to the serum.

All lanes:

Immunoprecipitation - Anti-p95/NBS1 antibody (ab175800)

Predicted band size: 84 kDa

false

Western blot - Anti-p95/NBS1 antibody (AB175800)
  • WB

Supplier Data

Western blot - Anti-p95/NBS1 antibody (AB175800)

All lanes:

Western blot - Anti-p95/NBS1 antibody (ab175800)

Lane 1:

Control si

Lane 2:

Nbs1 si

Lane 3:

NIH 3T3 cell lysate at 40 µg

Predicted band size: 84 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

IP, WB, IHC-P, ICC/IF

applications

Immunogen

Recombinant Fragment Protein within Human NBN aa 250-500. The exact immunogen used to generate this antibody is proprietary information.

O60934

Reactivity data

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Properties and storage information

Form
Liquid
Purity
Tissue culture supernatant
Storage buffer
Constituents: Water
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The target known as p95/NBS1 also referred to as NBN protein is a critical component in the DNA damage response mechanism. The full molecular weight of the NBS1 protein is approximately 95 kDa. This protein is abundantly expressed in various tissues particularly where there is a higher rate of cell division or repair such as in the thymus and testis. It plays an important role in maintaining the stability of the genome through its involvement in the repair of double-strand breaks.
Biological function summary

The NBS1 protein functions as an essential component of the MRN complex which also includes MRE11 and RAD50 proteins. This complex is fundamental in accurately detecting DNA double-strand breaks and initiating repair processes. Through its actions NBS1 facilitates numerous cellular processes that preserve genomic integrity such as homologous recombination and non-homologous end joining. Its influence in controlling the cell cycle further emphasizes its role in maintaining cellular health.

Pathways

The NBS1 protein engages significantly in the DNA damage response and repair pathways notably impacting the ATM signaling pathway. By interacting with proteins such as ATM kinase NBS1 facilitates the phosphorylation and activation of several downstream effectors necessary for DNA repair and cell cycle checkpoints. The MRN complex also links with the RAD50 protein highlighting its involvement in these pathways.

Mutations in the NBS1 gene are linked to Nijmegen breakage syndrome characterized by sensitivity to radiation immune deficiency and increased cancer risk. Additionally NBS1's role in pathways makes it pertinent to certain cancer pathologies where its malfunction can contribute to genomic instability. The NBN protein through its interaction with ATM and RAD50 assists in understanding its connection with predispositions to these diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed : 10888888, PubMed : 15616588, PubMed : 18411307, PubMed : 18583988, PubMed : 18678890, PubMed : 19759395, PubMed : 23115235, PubMed : 28216226, PubMed : 28867292, PubMed : 9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed : 19759395, PubMed : 28867292, PubMed : 9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed : 19759395, PubMed : 9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed : 19759395, PubMed : 28867292, PubMed : 9705271). Within the MRN complex, NBN acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (PubMed : 12419185, PubMed : 15616588, PubMed : 18411307, PubMed : 18582474, PubMed : 18583988, PubMed : 18678890, PubMed : 19759395, PubMed : 19804756, PubMed : 23762398, PubMed : 24534091, PubMed : 27814491, PubMed : 27889449, PubMed : 33836577). Recruits MRE11 and RAD50 components of the MRN complex to DSBs in response to DNA damage (PubMed : 12419185, PubMed : 18411307, PubMed : 18583988, PubMed : 18678890, PubMed : 24534091, PubMed : 26438602). Promotes the recruitment of PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites, activating their functions (PubMed : 15064416, PubMed : 15616588, PubMed : 15790808, PubMed : 16622404, PubMed : 22464731, PubMed : 30952868, PubMed : 35076389). Mediates the recruitment of phosphorylated RBBP8/CtIP to DSBs, leading to cooperation between the MRN complex and RBBP8/CtIP to initiate end resection (PubMed : 19759395, PubMed : 27814491, PubMed : 27889449, PubMed : 33836577). RBBP8/CtIP specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts (PubMed : 27814491, PubMed : 27889449, PubMed : 30787182, PubMed : 33836577). The MRN complex is also required for the processing of R-loops (PubMed : 31537797). NBN also functions in telomere length maintenance via its interaction with TERF2 : interaction with TERF2 during G1 phase preventing recruitment of DCLRE1B/Apollo to telomeres (PubMed : 10888888, PubMed : 28216226). NBN also promotes DNA repair choice at dysfunctional telomeres : NBN phosphorylation by CDK2 promotes non-homologous end joining repair at telomeres, while unphosphorylated NBN promotes microhomology-mediated end-joining (MMEJ) repair (PubMed : 28216226). Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (PubMed : 23762398).
See full target information NBN

Publications (6)

Recent publications for all applications. Explore the full list and refine your search

Biomolecules & therapeutics 33:1015-1023 PubMed41033779

2025

IFI16 Enhances Chemosensitivity of Breast Cancer Cells by Inhibiting DNA Damage Response.

Applications

Unspecified application

Species

Unspecified reactive species

Na-Lee Ka,Ga Young Lim,Seung-Su Kim,Mi-Ock Lee

Nature structural & molecular biology 30:1346-1356 PubMed37653239

2023

DNA-PK and the TRF2 iDDR inhibit MRN-initiated resection at leading-end telomeres.

Applications

Unspecified application

Species

Unspecified reactive species

Logan R Myler,Beatrice Toia,Cara K Vaughan,Kaori Takai,Andreea M Matei,Peng Wu,Tanya T Paull,Titia de Lange,Francisca Lottersberger

Molecular cell 83:167-185.e9 PubMed36577401

2022

Cryo-EM structure of the Mre11-Rad50-Nbs1 complex reveals the molecular mechanism of scaffolding functions.

Applications

Unspecified application

Species

Unspecified reactive species

Matthias Rotheneder,Kristina Stakyte,Erik van de Logt,Joseph D Bartho,Katja Lammens,Yilan Fan,Aaron Alt,Brigitte Kessler,Christophe Jung,Wynand P Roos,Barbara Steigenberger,Karl-Peter Hopfner

Nucleic acids research 48:4915-4927 PubMed32232336

2020

PHF2 regulates homology-directed DNA repair by controlling the resection of DNA double strand breaks.

Applications

WB

Species

Human

Ignacio Alonso-de Vega,Maria Cristina Paz-Cabrera,Magdalena B Rother,Wouter W Wiegant,Cintia Checa-Rodríguez,Juan Ramón Hernández-Fernaud,Pablo Huertas,Raimundo Freire,Haico van Attikum,Veronique A J Smits

EMBO reports 21:e48460 PubMed31782600

2019

PHF6 promotes non-homologous end joining and G2 checkpoint recovery.

Applications

WB

Species

Human

Daniël O Warmerdam,Ignacio Alonso-de Vega,Wouter W Wiegant,Bram van den Broek,Magdalena B Rother,Rob Mf Wolthuis,Raimundo Freire,Haico van Attikum,René H Medema,Veronique Aj Smits

Anticancer research 36:5237-5247 PubMed27798884

2016

High Expression of MRE11-RAD50-NBS1 Is Associated with Poor Prognosis and Chemoresistance in Gastric Cancer.

Applications

IHC-P

Species

Human

Bolag Altan,Takehiko Yokobori,Munenori Ide,Tuya Bai,Toru Yanoma,Akiharu Kimura,Norimichi Kogure,Masaki Suzuki,Pinjie Bao,Erito Mochiki,Kyoichi Ogata,Tadashi Handa,Kyoichi Kaira,Masahiko Nishiyama,Takayuki Asao,Tetsunari Oyama,Hiroyuki Kuwano
View all publications

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