PARP (cleaved) antibody
Alternatives Western Blotting (WB), Intracellular Flow Cytometry (ICFC), Immunoprecipitation (IP)
|6 references available|
|Quantity||50 µg (0.5 mg/ml) (Variants)|
|Price||Product not available in this region.|
1) 51-9000017: Purified Mouse Anti-Cleaved PARP (Asp214).
Quantity: 50 µg (1 ea).
Concentration: 0.5 mg/ml.
Immunogen: Human cleaved PARP.
Isotype: Mouse IgG1, kappa.
Storage Buffer: Aqueous buffered solution containing Less or equal than 0.09% sodium azide.
2) 51-16606N: Camptothecin Treated: Jurkat Lysate.
Quantity: 50 µg (1 ea).
Storage Buffer: SDS-PAGE buffer (62mM Tris pH 6.8, 2% SDS, 0.9% b-mercaptoethanol, 0.003% bromophenol blue, 5% glycerol).
PARP (Poly [ADP-Ribose] Polymerase) is a 113-kDa nuclear chromatin-associated enzyme that catalyzes the transfer of ADP-ribose units from NAD+ to a variety of nuclear proteins including topoisomerases, histones, and PARP itself. The catalytic activity of PARP is increased in cells following DNA damage, and PARP is thought to play an important role in mediating the normal cellular response to DNA damage. Additionally, PARP is a target of the caspase protease activity associated with apoptosis. The PARP protein consists of an N-terminal DNA-binding domain (DBD) and a C-terminal catalytic domain separated by a central automodification domain. During apoptosis, Caspase-3 cleaves PARP at a recognition site (Asp Glu Val Asp Gly) in the DBD to form 24- and 89-kDa fragments. This process separates the DBD (which is mostly in the 24-kDa fragment) from the catalytic domain (in the 89-kDa fragment) of the enzyme, resulting in the loss of normal PARP function. It has been proposed that inactivation of PARP directs DNA-damaged cells to undergo apoptosis rather than necrotic degradation, and the presence of the 89-kDa PARP cleavage fraction is considered to be a marker of apoptosis.
A peptide corresponding to the N-terminus of the cleavage site (Asp 214) of human PARP was used as the immunogen. The F21-852 monoclonal antibody reacts only with the 89-kDa fragment of human PARP-1 that is downstream of the Caspase-3 cleavage site (Asp214) and contains the automodification and catalytic domains. It does not react with intact human PARP-1. Cross-reactivity with other members of the PARP superfamily is unknown. It may also recognize cleaved PARP in a number of other species due to the conserved nature of the molecule, although this has not been tested.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Related Products: ABIN967299
|Application Notes||Camptothecin treated Jurkat lysate [50 µg (1 µg/µl)] is provided as a positive control (store lysate at -20°C). Additional Jurkat lysate is available untreated (ABIN968537) or as a set containing both untreated and camptothecin treated lysates (ABIN967299) as ready-to-use western blot controls. Additional applications not routinely tested include immunoprecipitation (2 µg/200 µg of lysates) and flow cytometry. The directly conjugated formats are recommended for flow cytometry.|
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution.|
|Preservative||0.09% Sodium azide.|
|Storage||Store purified antibody at 4°C. Store lysate at -20°C|
|Research Area||Chromatin and Nuclear Signaling, DNA/RNA, Enzymes, Metabolism|
|Restrictions||For Research Use only|
Lamarre, Talbot, Leduc et al.: "Production and characterization of monoclonal antibodies specific for the functional domains of poly(ADP-ribose) polymerase." in: Biochemistry and cell biology = Biochimie et biologie cellulaire, Vol. 64, Issue 4, pp. 368-76, 1986 (PubMed).
Lamarre, Talbot, de Murcia et al.: "Structural and functional analysis of poly(ADP ribose) polymerase: an immunological study." in: Biochimica et biophysica acta, Vol. 950, Issue 2, pp. 147-60, 1988 (PubMed).
Tewari, Quan, ORourke 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." in: Cell, Vol. 81, Issue 5, pp. 801-9, 1995 (PubMed).
Kaufmann, Desnoyers, Ottaviano et al.: "Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis." in: Cancer research, Vol. 53, Issue 17, pp. 3976-85, 1993 (PubMed).
Patel, Gores, Kaufmann: "The role of proteases during apoptosis." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 10, Issue 5, pp. 587-97, 1996 (PubMed).
DAmours, Desnoyers, DSilva et al.: "Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions." in: The Biochemical journal, Vol. 342 ( Pt 2), Issue 5691, pp. 249-68, 1999 (PubMed).
|Hosts||Rabbit (32), Mouse (3)|
|Reactivities||Human (33), Mouse (Murine) (26), Rat (Rattus) (25), Cow (Bovine) (5), Dog (Canine) (5)|
|Applications||Immunofluorescence (IF) (21), Western Blotting (WB) (15), ELISA (9), Immunohistochemistry (IHC) (5), Immunohistochemistry (Formalin-fixed Sections) (IHC (f)) (3), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)) (3), Flow Cytometry (FACS) (2), Immunoprecipitation (IP) (2), Immunocytochemistry (ICC) (1), Immunoelectron Microscopy (IEM) (1)|
|Conjugates||Alexa Fluor 350 (2), Alexa Fluor 488 (2), Alexa Fluor 555 (2), Alexa Fluor 647 (2), PE,Cy5.5 (2), Biotin (1), Cy3 (1), Cy5 (1), Cy5.5 (1), Cy7 (1), FITC (1), Gold (1), HRP (1), PE (1), PE,Cy3 (1), PE,Cy5 (1), PE,Cy7 (1)|
|Epitopes||N-Term (4), cleaved (3), Cleavage Site (1), Cleaved-Asp214 (1), Cleaved-Gly215 (1)|