Rabbit anti-Human Poly [ADP-ribose] Polymerase-1 Polyclonal Antibody | anti-PARP1 antibody

Poly [ADP-ribose] Polymerase-1 (PARP)

Cat. Num. AAA619868

• Gene Names: PARP1; PARP; PPOL; ADPRT; ADPRT1; PARP-1; ADPRT 1; pADPRT-1
• Reactivity: Human
• Applications: Western Blot, Immunocytochemistry
• Purity: Affinity Purified; Purified by Protein G affinity chromatography.
• Synonyms: Poly [ADP-ribose] Polymerase-1; Polyclonal Antibody; Poly [ADP-ribose] Polymerase-1 (PARP); Anti -Poly [ADP-ribose] Polymerase-1 (PARP); anti-PARP1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Specificity: Recognizes human PARP
• Purity/Purification: Affinity Purified; Purified by Protein G affinity chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.2.

• Applicable Applications for anti-PARP1 antibody: Western Blot (WB), Immunocytochemistry (ICC)
• Application Notes: Suitable for use in Western Blot and Immunocytochemistry.; Dilution: Western Blot: 1:1000; Immunocytochemistry: 1:100
• Immunogen: Synthetic peptide (GVDEVAKKKSKK) corresponding to aa214-225 of human PARP
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Related Product Information for anti-PARP1 antibody

Poly [ADP-ribose] polymerase-1 (PARP) is a nuclear protein that catalyses the poly ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. It is activated by DNA strand breaks and plays a role in DNA-base excision repair, DNA-damage signalling, transcription regulation and proteosomal function. PARP is cleaved by caspases during apoptosis to yield two apoptotic fragments, the amino-terminal DNA binding domain (25 kD) and the carboxy-terminal catalytic domain (85 kD). PARP cleavage facilitates the cellular disassembly and serves as a marker of cell undergoing apoptosis.

Product Categories/Family for anti-PARP1 antibody

Antibodies; Abs to Enzymes; Polymerase

NCBI and Uniprot Product Information

• NCBI GI #: 156523968
• NCBI GeneID: 142
• NCBI Accession #: NP_001609.2
• NCBI GenBank Nucleotide #: NM_001618.3
• UniProt Accession #: P09874; Q8IUZ9; B1ANJ4; Q05D33; Q6PJL0; Q96P95
• Molecular Weight: 113,084 Da
• NCBI Official Full Name: poly
• NCBI Official Synonym Full Names: poly (ADP-ribose) polymerase 1
• NCBI Official Symbol: PARP1
• NCBI Official Synonym Symbols: PARP; PPOL; ADPRT; ADPRT1; PARP-1; ADPRT 1; pADPRT-1
• NCBI Protein Information: poly [ADP-ribose] polymerase 1; poly [ADP-ribose] polymerase 1; OTTHUMP00000035663; poly(ADP-ribose) polymerase; poly(ADP-ribose) synthetase; poly[ADP-ribose] synthase 1; poly(ADP-ribosyl)transferase; ADP-ribosyltransferase NAD(+); NAD(+) ADP-ribosyltransferase 1; poly (ADP-ribose) polymerase family, member 1; ADP-ribosyltransferase (NAD+; poly (ADP-ribose) polymerase)
• UniProt Protein Name: Poly [ADP-ribose] polymerase 1
• Protein Family: Poly [ADP-ribose] polymerase
• UniProt Gene Name: PARP1
• UniProt Synonym Gene Names: ADPRT; PPOL
• UniProt Entry Name: PARP1_HUMAN

NCBI Description

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]

Uniprot Description

PARP1: 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. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. 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. 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 EEF1A1, RNF4 and TXK.

Protein type: Nuclear receptor co-regulator; DNA repair, damage; Nucleolus; EC 2.4.2.30; Transferase; Nuclear envelope

Chromosomal Location of Human Ortholog: 1q41-q42

Cellular Component: nucleoplasm; transcription factor complex; membrane; nucleolus; nuclear envelope; nucleus

Molecular Function: identical protein binding; protein binding; enzyme binding; DNA binding; zinc ion binding; protein N-terminus binding; NAD binding; transcription factor binding; protein kinase binding; NAD+ ADP-ribosyltransferase activity

Biological Process: transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase II promoter; macrophage differentiation; transcription, DNA-dependent; DNA damage response, detection of DNA damage; negative regulation of transcription from RNA polymerase II promoter; DNA repair; protein autoprocessing; protein amino acid ADP-ribosylation; cellular response to insulin stimulus; base-excision repair; double-strand break repair; transforming growth factor beta receptor signaling pathway; gene expression; positive regulation of transcription from RNA polymerase II promoter; regulation of growth rate; telomere maintenance