anti-PARP antibody (full length)

Details for Product anti-PARP Antibody No. ABIN967515
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Antigen
Synonyms
ADPRT, ADPRT 1, ADPRT1, ARTD1, PARP, PARP-1, PPOL, pADPRT-1, adprt1, padprt-1, parp, ppol, 5830444G22Rik, AI893648, Adprp, Adprt1, C80510, parp-1, sPARP-1, BEST:LD21673, CG17685, CG17696, CG17718, CG4 ... show more
ADPRT, ADPRT 1, ADPRT1, ARTD1, PARP, PARP-1, PPOL, pADPRT-1, adprt1, padprt-1, parp, ppol, 5830444G22Rik, AI893648, Adprp, Adprt1, C80510, parp-1, sPARP-1, BEST:LD21673, CG17685, CG17696, CG17718, CG40411, D.PARP, Dm.pARTa, Dmel\\CG40411, LD21673.3prime, PARP1, dPARP show less
Epitope
full length
(13), (10), (9), (6), (6), (6), (4), (3), (2), (2), (2), (1), (1), (1), (1)
Reactivity
Cow (Bovine)
(80), (25), (10), (3), (1), (1), (1), (1), (1), (1)
Host
Mouse
(55), (37), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
This PARP antibody is un-conjugated
(1)
Application
Immunofluorescence (IF), Western Blotting (WB)
(89), (37), (15), (15), (14), (8), (8), (6), (5), (2), (2), (1), (1), (1)
Pubmed 5 references available
Quantity 0.1 mL
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Immunogen Cow PARP (full-length, thymus derived)
Clone C2-10
Isotype IgG1
Cross-Reactivity Mouse (Murine), Hamster, Human
Characteristics 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.
Purification Ascites
Background 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 nonapoptotic cells following DNA damage, and PARP is thought to play an important role in mediating the normal cellular reponse to DNA damage and is a target of the caspase protease activity associated with apoptosis. During apoptosis, PARP is cleaved from a 113 kDa intact form into 89 kDa and 24 kDa fragments. This process separates the amino-terminal DNA-binding domain of the enzyme from the C-terminal catalytic domain resulting in the loss of normal PARP function. Although the role of PARP in apoptosis remains to be elucidated, PARP cleavage is considered to be a marker of apoptosis. This antibody has been reported to recognize an epitope located within the DNA-binding domain of the enzyme.
Synonyms: Poly (ADP-Ribose) Polymerase
Molecular Weight 113 kDa (full-length), 89 kDa (cleaved)
Research Area Chromatin and Nuclear Signaling, DNA/RNA, Enzymes, Metabolism
Application Notes This antibody is prepared as an ascites solution. For western blot analysis, investigators are highly encouraged to titrate the antibody for optimal performance. A titration range between 1:2000 to 1:4000 is suggested.
Comment

Related Products: ABIN967540, ABIN967299, ABIN967389

Restrictions For Research Use only
Format Liquid
Buffer Aqueous buffered solution.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Supplier Images
anti-PARP (full length) antibody Western blot analysis of PARP cleavage. Jurkat cells (Human T-cell leukemia, ATCC TIB...
anti-PARP (full length) antibody (2) anti-PARP (full length) antibody (Image 2)
Product cited in: 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).

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).

Background publications 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).

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).

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).

Validation Images
Catalog No. ABIN967515
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