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05-725

Sigma-Aldrich

Anti-53BP1 Antibody, clone BP18

ascites fluid, clone BP18, Upstate®

Synonym(s):

Anti-Anti-53BP1, Anti-Anti-TDRD30, Anti-Anti-p202, Anti-Anti-p53BP1

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About This Item

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

biological source

mouse

Quality Level

antibody form

ascites fluid

antibody product type

primary antibodies

clone

BP18, monoclonal

species reactivity

mouse, human

manufacturer/tradename

Upstate®

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgM

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... TP53BP1(7158)
mouse ... Trp53Bp1(27223)

Specificity

53BP1

Immunogen

Mix of three GST fusion proteins corresponding to residues 1-337, 338-671, and 1331-1664, respectively, of human 53BP1

Application

Detect 53BP1 with Anti-53BP1 Antibody, clone BP18 (Mouse Monoclonal Antibody), that has been shown to work in IP & WB.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Transcription Factors

Quality

routinely evaluated by immunoblot on whole cell lysates from HeLa cells

Target description

~250kDa

Physical form

Ascites
mouse ascites IgM containing 0.05% sodium azide and 30% glycerol

Storage and Stability

2 years at -20°C

Legal Information

UPSTATE 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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Irene M Ward et al.
Molecular and cellular biology, 23(7), 2556-2563 (2003-03-18)
53BP1 is a p53 binding protein of unknown function that binds to the central DNA-binding domain of p53. It relocates to the sites of DNA strand breaks in response to DNA damage and is a putative substrate of the ataxia
Maria Pinkerneil et al.
Molecular cancer therapeutics, 15(2), 299-312 (2016-01-17)
Class I histone deacetylases HDAC1 and HDAC2 contribute to cell proliferation and are commonly upregulated in urothelial carcinoma. To evaluate whether specific inhibition of these enzymes might serve as an appropriate therapy for urothelial carcinoma, siRNA-mediated knockdown and specific pharmacologic
Maria Pinkerneil et al.
Targeted oncology, 11(6), 783-798 (2016-06-03)
Targeting of class I histone deacetylases (HDACs) exerts antineoplastic actions in various cancer types by modulation of transcription, upregulation of tumor suppressors, induction of cell cycle arrest, replication stress and promotion of apoptosis. Class I HDACs are often deregulated in
I Rappold et al.
The Journal of cell biology, 153(3), 613-620 (2001-05-02)
The tumor suppressor p53 binding protein 1 (53BP1) binds to the DNA-binding domain of p53 and enhances p53-mediated transcriptional activation. 53BP1 contains two breast cancer susceptibility gene 1 COOH terminus (BRCT) motifs, which are present in several proteins involved in
Francesca Cipressa et al.
Nature communications, 7, 10405-10405 (2016-01-19)
Drosophila telomeres are elongated by transposition of specialized retroelements rather than telomerase activity and are assembled independently of the sequence. Fly telomeres are protected by the terminin complex that localizes and functions exclusively at telomeres and by non-terminin proteins that

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