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Phospho-53BP1 (Ser1778) Antibody
synthetic phosphopeptide corresponding to residues surrounding Ser1778 of human 53BP1
W, IF-IC, F
Rabbit
CST
详见MSDS文件
详见说明书
大量
H,Mk
2
-20°c
100 ul (10 western blots)/carrier free & custom formulation / quantity
规格: | 产品价格: | ¥请询价 | |
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规格: | 100 ul (10 western blots) | 产品价格: | ¥请询价 |
规格: | carrier free & custom formulation / quantity | 产品价格: | ¥请询价 |
pathway more info application references datasheet PDF MSDS PDF protocols
Applications Key: W=Western Blotting IF-IC=Immunofluorescence (Immunocytochemistry) F=Flow Cytometry
Reactivity Key: H=Human Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Applications | Reactivity | Sensitivity | MW (kDa) | Source |
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W IF-IC F | H Mk | Endogenous | 450 | Rabbit |
Protocols |
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Specificity / Sensitivity | Phospho-53BP1 (Ser1778) Antibody detects endogenous levels of 53BP1 only when phosphorylated at serine 1778. |
Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser1778 of human 53BP1. Antibodies are purified by protein A and peptide affinity chromatography. Western BlottingWestern blot analysis of extracts from 293 cells, untreated or UV-treated (50 mJ for 2 hours), using Phospho-53BP1 (Ser1778) Antibody (upper) or 53BP1 Antibody #4937 (lower). Flow CytometryFlow cytometric analysis of HeLa cells, untreated (blue) or UV-treated (green), using Phospho-53BP1 (Ser1778) Antibody compared with a nonspecific negative control antibody (red). IF-ICConfocal immunofluorescent analysis of HeLa cells, untreated (left) or UV-treated (right), using Phospho-53BP1 (Ser1778) Antibody (green). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red). |
Background | p53-binding protein 1 (53BP1) was originally identified as a p53 binding partner that could enhance the transcriptional activity of p53 (1,2). 53BP1 consists of two BRCA1 carboxy terminal (BRCT) domains that allow for binding to p53 and a separate domain responsible for binding to phosphorylated histone H2A.X (3). 53BP1 rapidly translocates to nuclear foci following treatment of cells with ionizing radiation (IR) or radiomimetic agents that cause DNA double strand breaks (DSBs) (4,5). Because of this localization to DSBs and homology to the yeast protein Rad9, a role for 53BP1 in DSB repair has been proposed. Recruitment of 53BP1 to sites of DNA damage has been demonstrated to be independent of ATM, NBS1, and DNA-PK (4) and retention of 53BP1 at DNA breaks requires phosphorylated H2A.X (6). In cells lacking 53BP1, phosphorylation of ATM substrates is reduced, suggesting that 53BP1 is upstream of ATM (7). In response to IR, phosphorylation of 53BP1 at serines 6, 25, 29, and 784 by ATM has been demonstrated, but phosphorylation at these sites is not required for localization of 53BP1 to sites of DSBs (6). Within the first BRCT domain (amino acids 1714-1850), there exists a consensus ATM/ATR phosphorylation site, Ser1778. It is conceivable that phosphorylation of Ser1778 could therefore serve to regulate 53BP1-p53 binding.
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Application References |
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Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |
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