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PARP-1 (Cleaved p85)

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  • 公司名稱 上海希美化學(xué)有限公司
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  • 更新時(shí)間 2017/7/13 22:18:23
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PARP-1 (Cleaved p85)

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PARP-1 (Cleaved p85) Antibody
Rabbit Monoclonal Antibody
 
Cat.#  1074-1

Description

Poly (ADP-ribose) polymerase (PARP) is zinc-dependent DNA binding protein that recognizes DNA strand breaks and is presumed to play a role in DNA repair (1). As a marker for apoptosis, PARP is cleaved in vitro by many caspases, and in vivo by Caspase-3 (2,3). Existing as a 116 kDa nuclear protein, PARP is cleaved between amino acids Asp214 and Gly215 to yield two fragments of 29 kDa (C-terminal catalytic domain) and 85 kDa (N-terminal DNA-binding domain) (2,4).


Recommended Applications

WB, ICC, IP, FC

 
Applications and Recommended Dilution Factors
 
WB IHC ICC FC IP

1:1,000   1:50 1:50 1:50

Species Reactivity*
 
Human Mouse Rat

Positive Negative Positive *Cross reactivity determined by western blot only.

 
Product Data
A. Western blot analysis on (1) Jurkat and (2) Jurkat + Camptothecin using anti-PARP-1 RabMAb (catalog #1074-1), 1:1,000 dilution. B. Flow cytometric analysis of apoptotic and non-apoptotic Jurkat cells using anti-cleaved PARP-1 RabMAb (catalog #1074-1). Jurkat cells were either left untreated (A) or treated with camptothecin (4 uM, 5 hr) to induce apoptosis (B). Cells were fixed and permeabilized, and then stained with anti-cleaved PARP-1. The results indicate that 43% of cells were positive for cleaved PARP (B, M2) after treatment, compared to 9% positive without treatment (A, M2).

Specificity

A synthetic peptide corresponding to residues following the cleavage site of human PARP-1 was used as immunogen. The antibody only recognize p85 cleaved-form of PARP-1.


Storage Buffer & Conditions

50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.


Alternative Names

PARP1, ADPRT, PPOL, Poly [ADP-ribose] polymerase 1, ADPRT;NAD(+) ADP-ribosyltransferase 1;Poly[ADP-ribose] synthetase 1


Description References

1. Ikejima, M, et al. The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA. J.Biol.Chem. 265: 21907
2. Lazebnik, Y.A., et al. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371: 346
3. Tewari, M, et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801
4. Kaufmann, S.H., et al. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53: 2976
 


Product References

1. Yoon S, Molloy MJ, Wu MP, et al, C6ORF32 is upregulated during muscle cell differentiation and induces the formation of cellular filopodia ,Developmental Biology 301 (2007) 70-81
[Application: ICC ]
2. Shangary S, Ding K, Qiu S, et al, Reactivation of p53 by a specific MDM2 antagonist (MI-43) leads to p21-mediated cell cycle arrest and selective cell death in colon cancer ,Mol. Cancer Ther. 7 (2008) 1533 - 1542
[Application: WB ]
 



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