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This Anti-PARP1 (cleaved form) Antibody is validated for use in WB, IC for the detection of PARP1 (cleaved form).
More>>This Anti-PARP1 (cleaved form) Antibody is validated for use in WB, IC for the detection of PARP1 (cleaved form). Less<<
Anti-PARP1 (cleaved form) Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Poly [ADP-ribose] polymerase 1 (UniProt: P09874; also known as EC: 2.4.2.30, PARP-1, ADP-ribosyltransferase diphtheria toxin-like 1, ARTD1, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1) is encoded by the PARP1 (also known as ADPRT, PPOL) gene (Gene ID: 142) in human. PARP1 is zinc-dependent DNA binding protein that recognizes DNA strand breaks and is presumed to play a role in DNA repair. It is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Its DNA-binding region is localized to amino acids 2-372. PARP1 contains two zinc-finger regions (aa 9-93 and 113-203). PARP is cleaved between amino acids Asp214 and Gly215 to yield two fragments: a 29 kDa (N-terminal) and a 85 kDa (C-terminal DNA-binding domain). The carboxyl-terminally located 54-kDa domain of PARP represents the NAD1-binding domain with the characteristic “PARP signature,” which includes a highly conserved sequence comprising the catalytically crucial amino acid residue Glu-988. Its catalytic activity is stimulated by noncovalent contact of the DNA-binding domain with DNA strand breaks and results in the post-translational modification of various acceptor proteins. In between the DNA binding domain and the NAD1-binding domain, it also contains a 22-kDa automodification domain. (Ref.: Alvarez-Gonzalez, R., et al. (1999). J. Biol. Chem. 274(45); 32122–32126).
References
Product Information
Format
Affinity Purified
Control
Jurkat cell lysate untreated and Camptothecin-treated
Presentation
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
This Anti-PARP1 (cleaved form) Antibody is validated for use in WB, IC for the detection of PARP1 (cleaved form).
Key Applications
Western Blotting
Immunocytochemistry
Application Notes
Immunocytochemistry Analysis: A 1:500 dilution from a representative lot detected cleaved PARP1 in staurosporine-untreated and staurosporine-treated HeLa cells.
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to the DNA binding domain of human PARP1.
Epitope
DNA binding domain
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Rabbit
Specificity
This antibody recognizes cleaved PARP1 at the DNA binding domain.
Species Reactivity
Human
Species Reactivity Note
Demonstrated to react with Human. Other homologies: Rat and Mouse (90% sequence homology).
This gene encodes a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, this enzyme may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes. [provided by RefSeq].
FUNCTION: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150.
SUBUNIT STRUCTURE: Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with PARP3, APTX and SRY. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423 (By similarity). Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. Interacts with RNF4.
SUBCELLULAR LOCATION: Nucleus.
PTM: Phosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR.
Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites.
S-nitrosylated, leading to inhibit transcription regulation activity (By similarity).
MISCELLANEOUS: The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
SEQUENCE SIMILARITIES: Contains 1 BRCT domain.
Contains 1 PARP alpha-helical domain.
Contains 1 PARP catalytic domain.
Contains 2 PARP-type zinc fingers.
Molecular Weight
~89 kDa observed
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in Jurkat cell lysate, untreated and Camptothecin-treated.
Western Blot Analysis: A 1:50,000 dilution of this antibody detected cleaved PARP1 in 10 µg of Jurkat cell lysate, untreated and Camptothecin-treated.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.