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|Tested species reactivity||Bovine, Human, Mouse, Rat|
|Published species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic Peptide: S(509) K G P V K E E G T N K S E K R(524)|
|Storage buffer||whole serum|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay dependent|
|Western Blot (WB)||1:500|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
By Western blot, this antibody detects a 116 kDa protein representing PARP and the 85 kDa apoptosis-induced cleavage product of protease resembling ICE (prICE) and CPP32 from GH4C1 cell extract.
Poly(ADP-ribose) polymerase (PARP) is a eukaryotic nuclear protein involved in differentiation, DNA repair, and chromatin structure formation. During the process of programmed cell death, or apoptosis, the cell undergoes distinct morphological changes which include shrinkage, membrane blebbing, and nuclear reorganization. Several members of the interleukin 1-beta-converting enzyme (ICE)/ced-3 family of proteases, or caspases, are activated in a cascade of cleavage events which leads to the degradation of critical cellular substrates. PARP contains a conserved protease recognition site, DEVD (single letter code for amino acids), which is known to be a target for several caspases including prICE (protease resembling ICE) and CPP32/YAMA. Other nuclear events that are concurrent with PARP cleavage during apoptosis are activation of the domain nuclease and fragmentation nuclease which cleave DNA into >50 kb and nucleosome-sized fragments, respectively.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
A systematic analysis of the PARP protein family identifies new functions critical for cell physiology.
PA3-951 was used in western blot to systematically study the cell physiological roles of PARP family members
|Vyas S,Chesarone-Cataldo M,Todorova T,Huang YH,Chang P||Nature communications (4:null)||2013|
ADP-ribosyltransferase (NAD+; ADP-ribosyltransferase (NAD+) poly (ADP-ribose) polymerase); ADP-ribosyltransferase (NAD+, poly (ADP-ribose) polymerase) 1; ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase); ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase) 1; ADP-ribosyltransferase 1; ADP-ribosyltransferase diphtheria toxin-like 1; ADP-ribosyltransferase NAD(+); ADPRT 1; msPARP; NAD(+) ADP-ribosyltransferase 1; PARP-1; poly (ADP-ribose) polymerase 1; poly (ADP-ribose) polymerase family, member 1; poly (ADP-ribose) polymerase); poly [ADP-ribose] polymerase 1; poly(ADP-ribose) polymerase; poly(ADP-ribose) polymerase PARP-1; poly(ADP-ribose) synthetase; poly(ADP-ribosyl)transferase; poly[ADP-ribose] synthase 1; poly[ADP-ribose] synthetase 1
5830444G22Rik; Adprp; ADPRT; ADPRT 1; ADPRT1; AI893648; ARTD1; BOS_15645; C80510; pADPRT-1; PARP; PARP-1; PARP1; PPOL; sPARP-1