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AB3622

Anti-Rad50 抗体

Anti-Rad50 antibody

4

(2 Reviews)

|

(2 Publications)

Rabbit Polyclonal RAD50 antibody. Suitable for IP and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human RAD50.

別名を表示する

DNA repair protein RAD50, hRAD50, RAD50

1 Images
Immunoprecipitation - Anti-Rad50 antibody (AB3622)
  • IP

Unknown

Immunoprecipitation - Anti-Rad50 antibody (AB3622)

Lanes :

1. IP from 1mg extract with 1.25g Rabbit anti-Rad 50 (exon 2-3) (ab3622)

2. IP from 1mg extract with 1.25μg Rabbit anti-Rad 50 (exon 13-14) (ab3623)

Sample : Nuclear extract from Hela cells

for Western blot, affinity purified Rabbit anti-Rad 50 (ab3622) used at 1 : 4000 dilution

All lanes:

Immunoprecipitation - Anti-Rad50 antibody (ab3622)

Predicted band size: 153 kDa

false

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Human

アプリケーション

IP

applications

免疫原

Synthetic Peptide within Human RAD50. The exact immunogen used to generate this antibody is proprietary information.

Q92878

Reactivity data

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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Immunogen
バッファー組成
pH: 7 - 8 Preservative: 0.1% Sodium azide Constituents: PBS, 1.815% Tris, 1.764% Sodium citrate
出荷温度
Blue Ice
短期保存温度
+4°C
長期保存温度
+4°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle

補足情報

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

Rad50 is an important component of the MRN complex with its partners MRE11 and NBS1. This protein plays an important role in DNA double-strand break repair and telomere maintenance. Rad50 also known by its molecular weight of approximately 153 kDa possesses ATPase activity that facilitates the bridging of DNA ends during repair processes. It is expressed in a variety of tissues with higher levels observed in rapidly dividing cells such as those found in testes and lymphoid organs.
Biological function summary

Rad50 contributes to genomic stability by participating in non-homologous end joining (NHEJ) and homologous recombination (HR) both of which are DNA repair mechanisms. It is part of the MRN complex a multi-protein assembly that detects DNA breaks and aids in processing and signaling them for repair. This complex acts at the early stages of DNA damage response assisting in the recruitment of other repair enzymes and proteins to the site of DNA lesions.

Pathways

Rad50 is integral to DNA damage response signaling and repair pathways like Ataxia Telangiectasia Mutated (ATM) signaling. The MRN complex activates ATM a kinase that phosphorylates key substrates involved in controlling cell cycle checkpoints and promoting repair of damaged DNA. This relationship positions Rad50 and its complex members as significant participants in maintaining cellular integrity by preventing the accumulation of genetic mutations.

Rad50 mutations have links to cancer development due to their effect on genomic instability. Deficiencies in Rad50 or the MRN complex can impair DNA repair leading to an increased risk for neoplastic transformations. Additionally Rad50 interactions with proteins such as p53 a tumor suppressor underline its potential role in the mechanisms behind cancers like breast and ovarian cancer. These connections highlight the importance of Rad50 in understanding disease progression and developing therapeutic strategies.

製品プロトコール

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ターゲットの情報

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 : 15064416, PubMed : 21757780, PubMed : 27889449, PubMed : 28134932, PubMed : 28867292, PubMed : 9590181, PubMed : 9651580, 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 : 15064416, PubMed : 21757780, PubMed : 27889449, PubMed : 28867292, PubMed : 9590181, PubMed : 9651580, 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 : 15064416, PubMed : 27889449, PubMed : 28867292, PubMed : 9590181, PubMed : 9651580, 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 : 11741547, PubMed : 9590181, PubMed : 9651580, PubMed : 9705271). Within the complex, RAD50 is both required to bind DNA ends and hold them in close proximity and regulate the activity of MRE11 (PubMed : 11741547, PubMed : 12805565, PubMed : 28134932). RAD50 provides an ATP-dependent control of MRE11 by positioning DNA ends into the MRE11 active site : ATP-binding induces a large structural change from an open form with accessible MRE11 nuclease sites into a closed form (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases : the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed : 15064416, PubMed : 15790808, PubMed : 16622404). The MRN complex is also required for the processing of R-loops (PubMed : 31537797). In telomeres the MRN complex may modulate t-loop formation (PubMed : 10888888).
See full target information RAD50

文献 (2)

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

Proceedings of the National Academy of Sciences of 110:16874-9 PubMed24082117

2013

Nucleolin mediates nucleosome disruption critical for DNA double-strand break repair.

Applications

IP, ChIP

Species

Unspecified reactive species, Unspecified reactive species

Michael Goldstein,Frederick A Derheimer,Jacqueline Tait-Mulder,Michael B Kastan

International journal of cancer 118:2911-6 PubMed16385572

2005

Evaluation of RAD50 in familial breast cancer predisposition.

Applications

Unspecified application

Species

Unspecified reactive species

Johanna Tommiska,Sheila Seal,Anthony Renwick,Rita Barfoot,Linda Baskcomb,Hiran Jayatilake,Jirina Bartkova,Jonna Tallila,Milja Kaare,Anitta Tamminen,Päivi Heikkilä,D Gareth Evans,Diana Eccles,Kristiina Aittomäki,Carl Blomqvist,Jiri Bartek,Michael R Stratton,Heli Nevanlinna,Nazneen Rahman
View all publications

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