Human PARP2 protein (Recombinant) (N-His) (STJP006709)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human PARP2-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | PARP2 |
| Gene ID | 10038 |
| Uniprot ID | PARP2_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Ser223-Trp583 |
Additional Info
| Post Translational Modifications | Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP2-HPF1 complex from chromatin. Poly-ADP-ribosylated by PARP1. Acetylation reduces DNA binding and enzymatic activity. Proteolytically cleaved by caspase-8 (CASP8) in response to apoptosis, leading to its inactivation. |
| 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. HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains. Specifically mediates formation of branched poly-ADP-ribosylation. Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF. In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex. |
| Protein Name | Poly Adp-Ribose Polymerase 2Parp-2Hparp-2Adp-Ribosyltransferase Diphtheria Toxin-Like 2Artd2Dna Adp-Ribosyltransferase Parp2Nad(+ Adp-Ribosyltransferase 2Adprt-2PolyAdp-Ribose Synthase 2Padprt-2Protein Poly-Adp-Ribosyltransferase Parp2 |
| Database Links | Reactome: R-HSA-110362Reactome: R-HSA-5685939Reactome: R-HSA-5696394Reactome: R-HSA-5696395Reactome: R-HSA-5696400 |
| Cellular Localisation | NucleusChromosomeRecruited To Dna Damage Sites In A Parp1-Dependent Process: Recognizes And Binds Poly-Adp-Ribose Chains Produced By Parp1 At Dna Damage Sites Via Its N-TerminusLeading To Its Recruitment |
| Alternative Protein Names | Poly Adp-Ribose Polymerase 2 proteinParp-2 proteinHparp-2 proteinAdp-Ribosyltransferase Diphtheria Toxin-Like 2 proteinArtd2 proteinDna Adp-Ribosyltransferase Parp2 proteinNad(+ Adp-Ribosyltransferase 2 proteinAdprt-2 proteinPolyAdp-Ribose Synthase 2 proteinPadprt-2 proteinProtein Poly-Adp-Ribosyltransferase Parp2 proteinPARP2 proteinADPRT2 proteinADPRTL2 protein |
Information sourced from Uniprot.org