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MAB3802

Sigma-Aldrich

Anti-53BP1 Antibody, clone BP13

clone BP13, Chemicon®, from mouse

Synonym(s):

p53 Binding Protein 1

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

BP13, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

immunofluorescence: suitable
western blot: suitable

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... TP53BP1(7158)

Related Categories

General description

P53-binding protein 1 (53BP1) plays a critical role in tumor suppression and is a putative substrate of ATM kinase. Upon DNA damage, it is phosphorylated and relocalizes to the presumptive sites of damage, specifically, double-strand breaks. This also suggests a role in DNA repair, and maintaining genomic stability. It is sequence specific transcription factor that plays a central role in the the response of mammalian cells to genotoxic stress. Also, 53BP1 localizes to kinetochores in mitotic cells, suggesting a potential function in mitotic checkpoint signaling.

Specificity

53BP1

Immunogen

Recombinant human 53BP1 proteins.

Application

Detect 53BP1 also known as p53 Binding Protein 1 with Anti-53BP1 Antibody, clone BP13 (Mouse Monoclonal Antibody) validated in IF & WB.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Cell Cycle, DNA Replication & Repair
Western blot. Recognizes a protein of >250 kD. Suggested dilution buffer is TBST. Suggested blocking buffer is 5% non-fat dry milk.

Immunoprecipitation. Expected size in immunoblot is >250 kD. Suggested lysis buffer is NETN. Suggested capture agent is Protein A + rabbit anti-mouse linker antibody.

Optimal working dilutions must be determined by the end user.

Physical form

Format: Purified
Purified immunoglobulin. Liquid in PBS, containing sodium azide.

Storage and Stability

Maintain at 2-8°C in undiluted aliquots for up to 12 months from date of receipt.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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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WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Shankar J Chinta et al.
Cell reports, 22(4), 930-940 (2018-02-02)
Exposure to the herbicide paraquat (PQ) is associated with an increased risk of idiopathic Parkinson's disease (PD). Therapies based on PQ's presumed mechanisms of action have not, however, yielded effective disease therapies. Cellular senescence is an anticancer mechanism that arrests
Ankana Tiwari et al.
Nature communications, 9(1), 677-677 (2018-02-16)
Chromosome missegregation acts as one of the driving forces for chromosome instability and cancer development. Here, we find that in human cancer cells, HeLa and U2OS, depletion of 53BP1 (p53-binding protein 1) exacerbates chromosome non-disjunction resulting from a new type
Heather A Galick et al.
Oncotarget, 8(49), 85883-85895 (2017-11-22)
Base excision repair (BER) is a key genome maintenance pathway. The NEIL1 DNA glycosylase recognizes oxidized bases, and likely removes damage in advance of the replication fork. The rs5745906 SNP of the NEIL1 gene is a rare human germline variant
Dominika Kwasna et al.
Molecular cell, 70(1), 150-164 (2018-03-27)
Deubiquitinating enzymes (DUBs) are important regulators of ubiquitin signaling. Here, we report the discovery of deubiquitinating activity in ZUFSP/C6orf113. High-resolution crystal structures of ZUFSP in complex with ubiquitin reveal several distinctive features of ubiquitin recognition and catalysis. Our analyses reveal
Motohiro Yamauchi et al.
DNA repair, 7(3), 405-417 (2008-02-06)
Several DNA damage checkpoint factors form nuclear foci in response to ionizing radiation (IR). Although the number of the initial foci decreases concomitantly with DNA double-strand break repair, some fraction of foci persists. To date, the physiological role of the

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