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The antibody against PARP2 was raised in rabbit using the Recombinant Human Poly [ADP-ribose] polymerase 2 protein (14-149AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB.
The antibody against PARP2 was raised in rabbit using the Recombinant Human Poly [ADP-ribose] polymerase 2 protein (14-149AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB.
$299.00
| Cat.No | ADC-08152A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PARP2 |
| Form | Liquid | Species Reactivity | Human |
| Isotype | IgG | Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 |
| Purification Method | >95%, Protein G purified | Conjugate | Non-conjugated |
| Application | ELISA, WB | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Poly [ADP-ribose] polymerase 2 protein (14-149AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q9UGN5 |
Uniprot Id
Q9UGN5
Target Species
Human
Target Name
PARP2
Target Full Name
Poly [ADP-ribose] polymerase 2
Target Function
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues 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. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site. PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex.
Target Subcellular Location
Nucleus. Chromosome.
Target Tissue Specificity
Widely expressed, mainly in actively dividing tissues. The highest levels are in the brain, heart, pancreas, skeletal muscle and testis; also detected in kidney, liver, lung, placenta, ovary and spleen; levels are low in leukocytes, colon, small intestine
Target Research Area
Epigenetics and Nuclear Signaling
Target Synonyms
ADP ribosyltransferase like 2; ADP-ribosyltransferase diphtheria toxin-like 2; ADPRT 2; ADPRT-2; ADPRT2; ADPRTL 2; ADPRTL 3; ADPRTL2; ADPRTL3; ARTD2; hPARP 2; hPARP-2; hPARP2; NAD(+) ADP ribosyltransferase 2; NAD(+) ADP-ribosyltransferase 2; pADPRT 2; pADPRT-2; pADPRT2; PARP 2; PARP-2; PARP2; PARP2_HUMAN; Poly (ADP ribose) polymerase family member 2; Poly (ADP ribosyl) transferase like 2; poly (ADP-ribose) polymerase 2; Poly [ADP ribose] synthetase 2; Poly [ADP-ribose] polymerase 2; Poly(ADP ribose) synthetase; Poly[ADP-ribose] synthase 2
Target Background
This gene encodes poly(ADP-ribosyl)transferase-like 2 protein, which contains a catalytic domain and is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. The basic residues within the N-terminal region of this protein may bear potential DNA-binding properties, and may be involved in the nuclear and/or nucleolar targeting of the protein. Two alternatively spliced transcript variants encoding distinct isoforms have been found.
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