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Poly [ADP-ribose] polymerase 4 (PARP-4) (EC 2.4.2.30) (193 kDa vault protein) (ADP-ribosyltransferase diphtheria toxin-like 4) (ARTD4) (PARP-related/IalphaI-related H5/proline-rich) (PH5P) (Vault poly(ADP-ribose) polymerase) (VPARP)

 PARP4_HUMAN             Reviewed;        1724 AA.
Q9UKK3; O75903; Q14682; Q5QNZ9; Q9H1M6;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
12-SEP-2018, entry version 179.
RecName: Full=Poly [ADP-ribose] polymerase 4;
Short=PARP-4;
EC=2.4.2.30;
AltName: Full=193 kDa vault protein;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 4;
Short=ARTD4;
AltName: Full=PARP-related/IalphaI-related H5/proline-rich;
Short=PH5P;
AltName: Full=Vault poly(ADP-ribose) polymerase;
Short=VPARP;
Name=PARP4; Synonyms=ADPRTL1, KIAA0177, PARPL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 306-319, AND VARIANT
THR-899.
PubMed=10477748; DOI=10.1083/jcb.146.5.917;
Kickhoefer V.A., Siva A.C., Kedersha N.L., Inman E.M., Ruland C.,
Streuli M., Rome L.H.;
"The 193 kDa vault protein, VPARP, is a novel poly(ADP-ribose)
polymerase.";
J. Cell Biol. 146:917-928(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-873; ALA-1265 AND
ARG-1280.
TISSUE=Thymus;
PubMed=10644454; DOI=10.1006/geno.1999.6024;
Still I.H., Vince P., Cowell J.K.;
"Identification of a novel gene (ADPRTL1) encoding a potential
poly(ADP-ribosyl)transferase protein.";
Genomics 62:533-536(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-873; ALA-1265
AND ARG-1280.
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. V.
The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 3:17-24(1996).
[4]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[6]
DISCUSSION OF SEQUENCE.
PubMed=10100603; DOI=10.1016/S0014-5793(99)00173-8;
Jean L., Risler J.-L., Nagase T., Coulouarn C., Nomura N.,
Salier J.-P.;
"The nuclear protein PH5P of the inter-alpha-inhibitor superfamily: a
missing link between poly(ADP-ribose)polymerase and the inter-alpha-
inhibitor family and a novel actor of DNA repair?";
FEBS Lett. 446:6-8(1999).
[7]
ASSOCIATION WITH TEP1.
PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O.,
Rome L.H.;
"Vaults and telomerase share a common subunit, TEP1.";
J. Biol. Chem. 274:32712-32717(1999).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-1236; SER-1335
AND SER-1504, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1335, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; SER-1236 AND
SER-1335, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1476, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397}.
-!- SUBUNIT: Component of the vault ribonucleoprotein particle, at
least composed of MVP, PARP4 and one or more vault RNAs (vRNAs).
Binds to MVP. Associates with TEP1.
-!- INTERACTION:
Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-2623021, EBI-6248094;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
spindle. Note=Also found in the nucleus, associated with mitotic
spindles.
-!- TISSUE SPECIFICITY: Widely expressed; the highest levels are in
the kidney; also detected in heart, placenta, lung, liver,
skeletal muscle, spleen, leukocytes and pancreas.
-!- SEQUENCE CAUTION:
Sequence=BAA11494.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF158255; AAD47250.1; -; mRNA.
EMBL; AF057160; AAC62491.1; -; mRNA.
EMBL; D79999; BAA11494.2; ALT_INIT; mRNA.
EMBL; AL359763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS9307.1; -.
RefSeq; NP_006428.2; NM_006437.3.
RefSeq; XP_011533234.1; XM_011534932.2.
UniGene; Hs.744855; -.
ProteinModelPortal; Q9UKK3; -.
BioGrid; 106653; 11.
IntAct; Q9UKK3; 18.
MINT; Q9UKK3; -.
STRING; 9606.ENSP00000371419; -.
BindingDB; Q9UKK3; -.
ChEMBL; CHEMBL6142; -.
CarbonylDB; Q9UKK3; -.
iPTMnet; Q9UKK3; -.
PhosphoSitePlus; Q9UKK3; -.
BioMuta; PARP4; -.
DMDM; 308153574; -.
EPD; Q9UKK3; -.
MaxQB; Q9UKK3; -.
PaxDb; Q9UKK3; -.
PeptideAtlas; Q9UKK3; -.
PRIDE; Q9UKK3; -.
ProteomicsDB; 84811; -.
DNASU; 143; -.
Ensembl; ENST00000381989; ENSP00000371419; ENSG00000102699.
GeneID; 143; -.
KEGG; hsa:143; -.
UCSC; uc001upl.4; human.
CTD; 143; -.
DisGeNET; 143; -.
EuPathDB; HostDB:ENSG00000102699.5; -.
GeneCards; PARP4; -.
H-InvDB; HIX0019099; -.
HGNC; HGNC:271; PARP4.
HPA; HPA011739; -.
MIM; 607519; gene.
neXtProt; NX_Q9UKK3; -.
OpenTargets; ENSG00000102699; -.
PharmGKB; PA24591; -.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00530000063006; -.
HOGENOM; HOG000139369; -.
HOVERGEN; HBG053515; -.
InParanoid; Q9UKK3; -.
KO; K10798; -.
OMA; PGDQIKD; -.
OrthoDB; EOG091G03L8; -.
PhylomeDB; Q9UKK3; -.
TreeFam; TF329720; -.
BRENDA; 2.4.2.30; 2681.
Reactome; R-HSA-197264; Nicotinamide salvaging.
SignaLink; Q9UKK3; -.
ChiTaRS; PARP4; human.
GeneWiki; PARP4; -.
GenomeRNAi; 143; -.
PRO; PR:Q9UKK3; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102699; Expressed in 96 organ(s), highest expression level in intestine.
CleanEx; HS_PARP4; -.
Genevisible; Q9UKK3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; NAS:UniProtKB.
GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IDA:MGI.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; NAS:UniProtKB.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
GO; GO:0051972; P:regulation of telomerase activity; IDA:BHF-UCL.
GO; GO:0042493; P:response to drug; NAS:UniProtKB.
CDD; cd00027; BRCT; 1.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 3.40.50.10190; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR031273; PARP4.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
InterPro; IPR013694; VIT.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10338:SF127; PTHR10338:SF127; 1.
Pfam; PF00533; BRCT; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF08487; VIT; 1.
Pfam; PF00092; VWA; 1.
SMART; SM00292; BRCT; 1.
SMART; SM00609; VIT; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF52113; SSF52113; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS51468; VIT; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Glycosyltransferase; Methylation; NAD; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ribonucleoprotein; Transferase.
CHAIN 1 1724 Poly [ADP-ribose] polymerase 4.
/FTId=PRO_0000211330.
DOMAIN 1 94 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 242 370 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 369 573 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DOMAIN 607 735 VIT. {ECO:0000255|PROSITE-
ProRule:PRU00801}.
DOMAIN 876 1046 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 1562 1724 Interaction with the major vault protein.
MOTIF 19 25 Nuclear localization signal.
{ECO:0000255}.
MOTIF 1237 1249 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1236 1236 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1335 1335 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1476 1476 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1504 1504 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 81 81 I -> V (in dbSNP:rs35200240).
/FTId=VAR_056645.
VARIANT 122 122 S -> N (in dbSNP:rs9578751).
/FTId=VAR_056646.
VARIANT 215 215 F -> Y (in dbSNP:rs9318600).
/FTId=VAR_056647.
VARIANT 792 792 P -> L (in dbSNP:rs4986818).
/FTId=VAR_056648.
VARIANT 873 873 S -> N (in dbSNP:rs7140044).
{ECO:0000269|PubMed:10644454,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_056649.
VARIANT 899 899 A -> T (in dbSNP:rs2275660).
{ECO:0000269|PubMed:10477748}.
/FTId=VAR_056650.
VARIANT 991 991 K -> R (in dbSNP:rs34689435).
/FTId=VAR_056651.
VARIANT 1012 1012 V -> I (in dbSNP:rs9581043).
/FTId=VAR_056652.
VARIANT 1253 1253 S -> T (in dbSNP:rs4986822).
/FTId=VAR_056653.
VARIANT 1265 1265 G -> A (in dbSNP:rs1050110).
{ECO:0000269|PubMed:10644454,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_016090.
VARIANT 1280 1280 G -> R (in dbSNP:rs13428).
{ECO:0000269|PubMed:10644454,
ECO:0000269|PubMed:8724849}.
/FTId=VAR_016091.
CONFLICT 519 519 S -> P (in Ref. 1; AAD47250).
{ECO:0000305}.
CONFLICT 897 897 Q -> E (in Ref. 2; AAC62491 and 3;
BAA11494). {ECO:0000305}.
CONFLICT 936 936 M -> A (in Ref. 2; AAC62491 and 3;
BAA11494). {ECO:0000305}.
CONFLICT 936 936 M -> T (in Ref. 1; AAD47250).
{ECO:0000305}.
CONFLICT 1065 1065 V -> A (in Ref. 1; AAD47250 and 2;
AAC62491). {ECO:0000305}.
CONFLICT 1080 1080 L -> R (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1108 1108 R -> C (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1328 1328 P -> T (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1331 1331 A -> T (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1394 1394 S -> A (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1459 1459 S -> Y (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1550 1550 L -> P (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1555 1555 V -> L (in Ref. 1; AAD47250).
{ECO:0000305}.
CONFLICT 1564 1564 I -> T (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
CONFLICT 1656 1656 A -> P (in Ref. 1; AAD47250, 2; AAC62491
and 3; BAA11494). {ECO:0000305}.
SEQUENCE 1724 AA; 192595 MW; DCA1DD4C001EA22F CRC64;
MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL DNADVLSQYQ
LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI TPPPDQKASS SEVKTEGLCP
DSATEEEDTV ELTEFGMQNV EIPHLPQDFE VAKYNTLEKV GMEGGQEAVV VELQCSRDSR
DCPFLISSHF LLDDGMETRR QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL
ASEQLQALLL EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI
LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC QLIRDMVNVC
ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL QNHHSKSPVD VLQIFRVGRV
NETTEFLSKL GNVRPLLHGS PVQNIVGILC RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD
SLSTSIKYSH PGETDGTRLL LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT
TDFEDDEFVV YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL
PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH VPIEAKYIFP
LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG HGAYLMSQDA PDVFTVSVGN
LPPKAKVLIK ITYITELSIL GTVGVFFMPA TVAPWQQDKA LNENLQDTVE KICIKEIGTK
QSFSLTMSIE MPYVIEFIFS DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL
PRMWVEKHPE KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL
HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN TDFWKTLRYL
SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF ACGIGSTANR HVLRILSQCG
AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL
NDRLLVYGFI PHCTQATLCA LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI
LHENETSHEM KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK
EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM ELSQPEVSED
FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP LFKKVSPWET STSSFFPILA
PAVGSYLPPT ARAHSPASLS FASYRQVASF GSAAPPRQFD ASQFSQGPVP GTCADWIPQS
ASCPTGPPQN PPSSPYCGIV FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS
LPTDPDPIRG FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL
LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL CFLEVKEEDE
IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT NGLHSFLKQK GIQSLGVKGR
ECLLDLIATM LVLQFIRTRL EKEGIVFKSL MKMDDASISR NIPWAFEAIK QASEWVRRTE
GQYPSICPRL ELGNDWDSAT KQLLGLQPIS TVSPLHRVLH YSQG


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EIAAB29926 193 kDa vault protein,ADPRTL1,Homo sapiens,Human,KIAA0177,PARP4,PARP-4,PARPL,PARP-related_IalphaI-related H5_proline-rich,PH5P,Poly [ADP-ribose] polymerase 4,Vault poly(ADP-ribose) polymerase,VPARP
18-003-42430 Poly [ADP-ribose] polymerase 2 - EC 2.4.2.30; PARP-2; NAD(+) ADP-ribosyltransferase 2; Poly[ADP-ribose] synthetase 2; pADPRT-2; hPARP-2 Polyclonal 0.05 mg Aff Pur
18-003-42429 Poly [ADP-ribose] polymerase 1 - EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.1 mg Protein A
EIAAB29923 Adprt2,ADPRT-2,Adprtl2,Aspartl2,Mouse,mPARP-2,Mus musculus,NAD(+) ADP-ribosyltransferase 2,pADPRT-2,Parp2,PARP-2,Poly [ADP-ribose] polymerase 2,Poly[ADP-ribose] synthase 2
EIAAB29924 ADPRT2,ADPRT-2,ADPRTL2,Homo sapiens,hPARP-2,Human,NAD(+) ADP-ribosyltransferase 2,pADPRT-2,PARP2,PARP-2,Poly [ADP-ribose] polymerase 2,Poly[ADP-ribose] synthase 2
EIAAB29925 ADPRT3,ADPRT-3,ADPRTL3,Homo sapiens,hPARP-3,Human,IRT1,NAD(+) ADP-ribosyltransferase 3,pADPRT-3,PARP3,PARP-3,Poly [ADP-ribose] polymerase 3,Poly[ADP-ribose] synthase 3
E0947h ELISA kit ADPRT,ADPRT 1,Homo sapiens,Human,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,PPOL 96T
U0947h CLIA ADPRT,ADPRT 1,Homo sapiens,Human,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,PPOL 96T
E0947h ELISA ADPRT,ADPRT 1,Homo sapiens,Human,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,PPOL 96T
U0947m CLIA Adprp,Adprt,ADPRT 1,Adprt1,Mouse,msPARP,Mus musculus,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947m ELISA kit Adprp,Adprt,ADPRT 1,Adprt1,Mouse,msPARP,Mus musculus,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947m ELISA Adprp,Adprt,ADPRT 1,Adprt1,Mouse,msPARP,Mus musculus,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
U0947r CLIA Adprt,ADPRT 1,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,Rat,Rattus norvegicus 96T
E0947r ELISA Adprt,ADPRT 1,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,Rat,Rattus norvegicus 96T
E0947r ELISA kit Adprt,ADPRT 1,NAD(+) ADP-ribosyltransferase 1,Parp1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1,Rat,Rattus norvegicus 96T
E0947b ELISA kit ADPRT,ADPRT 1,Bos taurus,Bovine,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
U0947b CLIA ADPRT,ADPRT 1,Bos taurus,Bovine,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947b ELISA ADPRT,ADPRT 1,Bos taurus,Bovine,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
EIAAB29933 Homo sapiens,Human,PARP7,PARP-7,Poly [ADP-ribose] polymerase 7,TCDD-inducible poly [ADP-ribose] polymerase,TIPARP
U0947c CLIA ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947c ELISA ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
E0947c ELISA kit ADPRT,ADPRT 1,Chicken,Gallus gallus,NAD(+) ADP-ribosyltransferase 1,PARP1,PARP-1,Poly [ADP-ribose] polymerase 1,Poly[ADP-ribose] synthase 1 96T
AS10 675 Antibody: PARP | Poly [ADP-ribose] polymerase , Immunogen: KLH-conjugated synthetic peptide derived from Arabidopsis thaliana PARP-1 (AT4G02390) and PARP-2 (AT2G31320) and PARP from other plant specie 200
DL-PARP-Hu Human Poly ADP Ribose Polymerase (PARP) ELISA Kit 96T
20312390-1 PARP-2 | Poly [ADP-ribose] polymerase 2 200 uL


 

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