Poly [ADP-ribose] polymerase 11 Recombinant Protein | PARP11 recombinant protein

Recombinant Human Poly [ADP-ribose] polymerase 11

Cat. Num. AAA1265598

• Gene Names: PARP1; PARP; PPOL; ADPRT; ARTD1; ADPRT1; PARP-1; ADPRT 1; pADPRT-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Poly [ADP-ribose] polymerase 11; Recombinant Human Poly [ADP-ribose] polymerase 11; ADP-ribosyltransferase diphtheria toxin-like 1; ARTD1NAD(+) ADP-ribosyltransferase 1; ADPRT 1; Poly[ADP-ribose] synthase 1; PARP11 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-331aa; Partial
• Sequence: AESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRK
• Sequence Length: 1014

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for PARP11 recombinant protein

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. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites.

Product Categories/Family for PARP11 recombinant protein

Epigenetics and Nuclear Signaling

References

Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase.Uchida K., Morita T., Sato T., Ogura T., Yamashita R., Noguchi S., Suzuki H., Nyunoya H., Miwa M., Sugimura T.Biochem. Biophys. Res. Commun. 148:617-622(1987) Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence.Kurosaki T., Ushiro H., Mitsuuchi Y., Suzuki S., Matsuda M., Matsuda Y., Katunuma N., Kangawa K., Matsuo H., Hirose T., Inayama S., Shizuta Y.J. Biol. Chem. 262:15990-15997(1987) cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase.Cherney B.W., McBride O.W., Chen D., Alkhatib H., Bhatia K., Hensley P., Smulson M.E.Proc. Natl. Acad. Sci. U.S.A. 84:8370-8374(1987) Human nuclear NAD+ ADP-ribosyltransferase(polymerizing) organization of the gene.Auer B., Nagl U., Herzog H., Schneider R., Schweiger M.DNA 8:575-580(1989) NIEHS SNPs programThe DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

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
• Molecular Weight: 41 kDa
• 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; ARTD1; ADPRT1; PARP-1; ADPRT 1; pADPRT-1
• NCBI Protein Information: poly [ADP-ribose] polymerase 1
• UniProt Protein Name: Poly [ADP-ribose] polymerase 1
• Protein Family: Poly [ADP-ribose] polymerase
• UniProt Gene Name: PARP1
• UniProt Synonym Gene Names: ADPRT; PPOL; PARP-1; ARTD1; ADPRT 1
• 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, Jul 2008]

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

Chromosomal Location of Human Ortholog: 1q41-q42

Cellular Component: membrane; mitochondrion; nuclear chromosome, telomeric region; nuclear envelope; nucleolus; nucleoplasm; nucleus; protein complex; transcription factor complex

Molecular Function: chromatin binding; DNA binding; DNA ligase (ATP) activity; enzyme binding; histone deacetylase binding; identical protein binding; NAD binding; NAD+ ADP-ribosyltransferase activity; protein binding; protein kinase binding; protein N-terminus binding; transcription factor binding; zinc ion binding

Biological Process: base-excision repair; behavioral response to cocaine; cellular protein metabolic process; cellular response to insulin stimulus; DNA damage response, detection of DNA damage; DNA ligation during DNA repair; DNA repair; double-strand break repair; double-strand break repair via homologous recombination; gene expression; lagging strand elongation; macrophage differentiation; mitochondrial DNA metabolic process; mitochondrial DNA repair; mitochondrion organization and biogenesis; negative regulation of transcription from RNA polymerase II promoter; nucleotide-excision repair; nucleotide-excision repair, DNA damage recognition; nucleotide-excision repair, DNA incision; positive regulation of transcription from RNA polymerase II promoter; post-translational protein modification; protein amino acid ADP-ribosylation; protein autoprocessing; protein sumoylation; regulation of growth rate; response to DNA damage stimulus; telomere maintenance; transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway