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Poly [ADP-ribose] polymerase 3 (PARP-3) (hPARP-3) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 3) (ARTD3) (IRT1) (NAD( ) ADP-ribosyltransferase 3) (ADPRT-3) (Poly[ADP-ribose] synthase 3) (pADPRT-3)

 PARP3_HUMAN             Reviewed;         533 AA.
Q9Y6F1; Q8NER9; Q96CG2; Q9UG81;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
27-SEP-2017, sequence version 4.
20-JUN-2018, entry version 176.
RecName: Full=Poly [ADP-ribose] polymerase 3;
Short=PARP-3;
Short=hPARP-3;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 3;
Short=ARTD3;
AltName: Full=IRT1;
AltName: Full=NAD(+) ADP-ribosyltransferase 3;
Short=ADPRT-3;
AltName: Full=Poly[ADP-ribose] synthase 3;
Short=pADPRT-3;
Name=PARP3; Synonyms=ADPRT3, ADPRTL3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Koch-Nolte F.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=10329013; DOI=10.1006/geno.1999.5799;
Johansson M.;
"A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA
cloning of two novel poly(ADP-ribose) polymerase homologues.";
Genomics 57:442-445(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
TISSUE=Frontal cortex;
PubMed=12640039; DOI=10.1242/jcs.00341;
Augustin A., Spenlehauer C., Dumond H., Menissier-de Murcia J.,
Piel M., Schmit A.-C., Apiou F., Vonesch J.-L., Kock M., Bornens M.,
de Murcia G.M.;
"PARP-3 localizes preferentially to the daughter centriole and
interferes with the G1/S cell cycle progression.";
J. Cell Sci. 116:1551-1562(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-533 (ISOFORM 1).
TISSUE=Kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; PARP1;
EZH2; HDAC1; HDAC2; SUZ12; YY1; LRIG3 AND LIG4.
PubMed=16924674; DOI=10.1002/jcb.21051;
Rouleau M., McDonald D., Gagne P., Ouellet M.E., Droit A.,
Hunter J.M., Dutertre S., Prigent C., Hendzel M.J., Poirier G.G.;
"PARP-3 associates with polycomb group bodies and with components of
the DNA damage repair machinery.";
J. Cell. Biochem. 100:385-401(2007).
[8]
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).
[9]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-532 IN COMPLEX WITH THE
INHIBITOR 3-AMINOBENZOIC ACID.
Structural genomics consortium (SGC);
"Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex
with an inhibitor 3-aminobenzoic acid.";
Submitted (APR-2007) to the PDB data bank.
[10]
STRUCTURE BY NMR OF 41-157.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the WGR domain from human poly [ADP-ribose]
polymerase-3.";
Submitted (APR-2008) to the PDB data bank.
-!- FUNCTION: 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. May link the DNA damage
surveillance network to the mitotic fidelity checkpoint.
Negatively influences the G1/S cell cycle progression without
interfering with centrosome duplication. Binds DNA. May be
involved in the regulation of PRC2 and PRC3 complex-dependent gene
silencing. {ECO:0000269|PubMed:16924674}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397}.
-!- SUBUNIT: Interacts with PRKDC and PARP1. Interacts with XRCC5; the
interaction is dependent on nucleic acids. Interacts with XRCC6;
the interaction is dependent on nucleic acids. Interacts with
EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4.
{ECO:0000269|PubMed:16924674, ECO:0000269|Ref.9}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome,
centriole. Note=Core component of the centrosome. Preferentially
localized to the daughter centriole throughout the cell cycle.
According to PubMed:16924674, it is almost exclusively localized
in the nucleus and appears in numerous small foci and a small
number of larger foci whereas a centrosomal location has not been
detected.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Short;
IsoId=Q9Y6F1-1; Sequence=Displayed;
Note=More abundant isoform. {ECO:0000269|PubMed:16924674};
Name=2; Synonyms=Long;
IsoId=Q9Y6F1-2; Sequence=VSP_007863;
-!- TISSUE SPECIFICITY: Widely expressed; the highest levels are in
the kidney, skeletal muscle, liver, heart and spleen; also
detected in pancreas, lung, placenta, brain, leukocytes, colon,
small intestine, ovary, testis, prostate and thymus.
-!- DOMAIN: According to PubMed:10329013, the N-terminal domain (54
amino acids) of isoform 2 is responsible for its centrosomal
localization. The C-terminal region contains the catalytic domain.
-!- PTM: Auto-poly(ADP)-ribosylation.
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EMBL; Y16836; CAC79988.1; -; mRNA.
EMBL; AF083068; AAD29855.1; -; mRNA.
EMBL; AY126341; AAM95460.1; -; mRNA.
EMBL; AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014260; AAH14260.1; -; mRNA.
EMBL; AL050034; CAB43246.1; -; mRNA.
CCDS; CCDS43097.1; -. [Q9Y6F1-1]
CCDS; CCDS46839.1; -. [Q9Y6F1-2]
PIR; T08713; T08713.
RefSeq; NP_001003931.3; NM_001003931.3. [Q9Y6F1-2]
RefSeq; NP_005476.4; NM_005485.5. [Q9Y6F1-1]
RefSeq; XP_005264836.2; XM_005264779.4. [Q9Y6F1-1]
RefSeq; XP_016860979.1; XM_017005490.1. [Q9Y6F1-1]
UniGene; Hs.271742; -.
PDB; 2EOC; NMR; -; A=41-157.
PDB; 3C49; X-ray; 2.80 A; A=178-532.
PDB; 3C4H; X-ray; 2.10 A; A=178-532.
PDB; 3CE0; X-ray; 2.80 A; A=178-532.
PDB; 3FHB; X-ray; 2.30 A; A=178-532.
PDB; 4GV0; X-ray; 1.90 A; A=178-532.
PDB; 4GV2; X-ray; 1.80 A; A=178-532.
PDB; 4GV4; X-ray; 1.80 A; A=178-532.
PDB; 4L6Z; X-ray; 2.00 A; A=178-532.
PDB; 4L70; X-ray; 2.00 A; A=178-532.
PDB; 4L7L; X-ray; 2.10 A; A=178-532.
PDB; 4L7N; X-ray; 1.80 A; A=178-532.
PDB; 4L7O; X-ray; 2.00 A; A=178-532.
PDB; 4L7P; X-ray; 2.30 A; A=178-532.
PDB; 4L7R; X-ray; 2.20 A; A=178-532.
PDB; 4L7U; X-ray; 2.80 A; A=178-532.
PDBsum; 2EOC; -.
PDBsum; 3C49; -.
PDBsum; 3C4H; -.
PDBsum; 3CE0; -.
PDBsum; 3FHB; -.
PDBsum; 4GV0; -.
PDBsum; 4GV2; -.
PDBsum; 4GV4; -.
PDBsum; 4L6Z; -.
PDBsum; 4L70; -.
PDBsum; 4L7L; -.
PDBsum; 4L7N; -.
PDBsum; 4L7O; -.
PDBsum; 4L7P; -.
PDBsum; 4L7R; -.
PDBsum; 4L7U; -.
ProteinModelPortal; Q9Y6F1; -.
SMR; Q9Y6F1; -.
BioGrid; 115351; 13.
IntAct; Q9Y6F1; 1.
STRING; 9606.ENSP00000381740; -.
ChEMBL; CHEMBL5083; -.
DrugBank; DB09074; Olaparib.
DrugBank; DB12332; Rucaparib.
GuidetoPHARMACOLOGY; 2864; -.
iPTMnet; Q9Y6F1; -.
PhosphoSitePlus; Q9Y6F1; -.
BioMuta; PARP3; -.
DMDM; 224471880; -.
PaxDb; Q9Y6F1; -.
PeptideAtlas; Q9Y6F1; -.
PRIDE; Q9Y6F1; -.
ProteomicsDB; 86661; -.
ProteomicsDB; 86662; -. [Q9Y6F1-2]
DNASU; 10039; -.
Ensembl; ENST00000398755; ENSP00000381740; ENSG00000041880. [Q9Y6F1-2]
Ensembl; ENST00000417220; ENSP00000395951; ENSG00000041880. [Q9Y6F1-1]
Ensembl; ENST00000431474; ENSP00000401511; ENSG00000041880. [Q9Y6F1-1]
GeneID; 10039; -.
KEGG; hsa:10039; -.
UCSC; uc003dbz.4; human. [Q9Y6F1-1]
CTD; 10039; -.
DisGeNET; 10039; -.
EuPathDB; HostDB:ENSG00000041880.14; -.
GeneCards; PARP3; -.
HGNC; HGNC:273; PARP3.
HPA; HPA067657; -.
MIM; 607726; gene.
neXtProt; NX_Q9Y6F1; -.
OpenTargets; ENSG00000041880; -.
PharmGKB; PA24593; -.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00390000017341; -.
HOGENOM; HOG000173055; -.
HOVERGEN; HBG053514; -.
InParanoid; Q9Y6F1; -.
KO; K10798; -.
OMA; LIYQESQ; -.
OrthoDB; EOG091G06SC; -.
PhylomeDB; Q9Y6F1; -.
TreeFam; TF315407; -.
BRENDA; 2.4.2.30; 2681.
SignaLink; Q9Y6F1; -.
EvolutionaryTrace; Q9Y6F1; -.
GeneWiki; PARP3; -.
GenomeRNAi; 10039; -.
PRO; PR:Q9Y6F1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000041880; -.
CleanEx; HS_PARP3; -.
ExpressionAtlas; Q9Y6F1; baseline and differential.
Genevisible; Q9Y6F1; HS.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0035861; C:site of double-strand break; IDA:MGI.
GO; GO:0003824; F:catalytic activity; TAS:ProtInc.
GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:MGI.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006302; P:double-strand break repair; IDA:MGI.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:1905662; P:negative regulation of telomerase RNA reverse transcriptase activity; IMP:BHF-UCL.
GO; GO:0051106; P:positive regulation of DNA ligation; IGI:MGI.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:MGI.
GO; GO:1990166; P:protein localization to site of double-strand break; IMP:MGI.
GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:MGI.
GO; GO:0000723; P:telomere maintenance; IMP:MGI.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
InterPro; IPR031275; PARP3.
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; IPR036930; WGR_dom_sf.
InterPro; IPR008893; WGR_domain.
PANTHER; PTHR10459:SF66; PTHR10459:SF66; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF05406; WGR; 1.
SMART; SM00773; WGR; 1.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Cytoskeleton; Glycosyltransferase; NAD; Nucleus; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 533 Poly [ADP-ribose] polymerase 3.
/FTId=PRO_0000211329.
DOMAIN 182 300 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 313 533 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
MOTIF 14 20 Nuclear localization signal.
{ECO:0000255}.
VAR_SEQ 1 1 M -> MSLLFLAM (in isoform 2).
{ECO:0000303|PubMed:12640039,
ECO:0000303|Ref.1}.
/FTId=VSP_007863.
VARIANT 91 91 S -> N (in dbSNP:rs34224216).
/FTId=VAR_056643.
VARIANT 100 100 R -> H (in dbSNP:rs28547534).
/FTId=VAR_054622.
VARIANT 269 269 Q -> R (in dbSNP:rs323870).
/FTId=VAR_056644.
CONFLICT 80 80 N -> K (in Ref. 2; AAD29855).
{ECO:0000305}.
CONFLICT 171 171 G -> A (in Ref. 2; AAD29855).
{ECO:0000305}.
CONFLICT 411 411 K -> E (in Ref. 6; CAB43246).
{ECO:0000305}.
STRAND 50 53 {ECO:0000244|PDB:2EOC}.
TURN 54 56 {ECO:0000244|PDB:2EOC}.
STRAND 61 74 {ECO:0000244|PDB:2EOC}.
TURN 75 78 {ECO:0000244|PDB:2EOC}.
STRAND 79 89 {ECO:0000244|PDB:2EOC}.
STRAND 95 100 {ECO:0000244|PDB:2EOC}.
STRAND 111 117 {ECO:0000244|PDB:2EOC}.
HELIX 118 133 {ECO:0000244|PDB:2EOC}.
HELIX 140 142 {ECO:0000244|PDB:2EOC}.
STRAND 147 149 {ECO:0000244|PDB:2EOC}.
STRAND 151 153 {ECO:0000244|PDB:2EOC}.
HELIX 187 196 {ECO:0000244|PDB:4GV2}.
HELIX 199 208 {ECO:0000244|PDB:4GV2}.
TURN 213 215 {ECO:0000244|PDB:4GV2}.
TURN 218 220 {ECO:0000244|PDB:4GV2}.
HELIX 223 240 {ECO:0000244|PDB:4GV2}.
STRAND 246 248 {ECO:0000244|PDB:3C49}.
HELIX 250 260 {ECO:0000244|PDB:4GV2}.
STRAND 265 268 {ECO:0000244|PDB:3C49}.
HELIX 276 298 {ECO:0000244|PDB:4GV2}.
HELIX 303 307 {ECO:0000244|PDB:4GV2}.
STRAND 309 311 {ECO:0000244|PDB:4GV2}.
HELIX 314 321 {ECO:0000244|PDB:4GV2}.
STRAND 325 328 {ECO:0000244|PDB:4GV2}.
HELIX 336 346 {ECO:0000244|PDB:4GV2}.
STRAND 349 351 {ECO:0000244|PDB:4GV2}.
STRAND 354 362 {ECO:0000244|PDB:4GV2}.
TURN 364 366 {ECO:0000244|PDB:3C49}.
HELIX 367 371 {ECO:0000244|PDB:4GV2}.
TURN 372 375 {ECO:0000244|PDB:4GV2}.
STRAND 379 385 {ECO:0000244|PDB:4GV2}.
HELIX 388 390 {ECO:0000244|PDB:4GV2}.
HELIX 391 397 {ECO:0000244|PDB:4GV2}.
STRAND 411 418 {ECO:0000244|PDB:4GV2}.
HELIX 419 423 {ECO:0000244|PDB:4GV2}.
STRAND 429 431 {ECO:0000244|PDB:4GV2}.
STRAND 434 445 {ECO:0000244|PDB:4GV2}.
STRAND 448 454 {ECO:0000244|PDB:4GV2}.
STRAND 467 471 {ECO:0000244|PDB:4GV2}.
STRAND 473 477 {ECO:0000244|PDB:4GV2}.
HELIX 479 481 {ECO:0000244|PDB:4GV2}.
STRAND 483 487 {ECO:0000244|PDB:4GV2}.
STRAND 490 494 {ECO:0000244|PDB:4GV2}.
STRAND 499 501 {ECO:0000244|PDB:4GV2}.
HELIX 503 505 {ECO:0000244|PDB:4GV2}.
STRAND 509 512 {ECO:0000244|PDB:4GV2}.
STRAND 514 519 {ECO:0000244|PDB:4GV2}.
HELIX 520 522 {ECO:0000244|PDB:4GV2}.
STRAND 523 532 {ECO:0000244|PDB:4GV2}.
SEQUENCE 533 AA; 60089 MW; 6296A0E439CC7767 CRC64;
MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP TCPLSSNPGT
QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNR WGRVGEVGQS KINHFTRLED
AKKDFEKKFR EKTKNNWAER DHFVSHPGKY TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV
QPCSLDPATQ KLITNIFSKE MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL
KGPTDGGQSL EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA
VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH RCPTLQHIWK
VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR IMPHSGGRVG KGIYFASENS
KSAGYVIGMK CGAHHVGYMF LGEVALGREH HINTDNPSLK SPPPGFDSVI ARGHTEPDPT
QDTELELDGQ QVVVPQGQPV PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL


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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
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
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 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
17-001-30065 Poly [ADP- - EC 2.4.2.30; PARP-2; NAD(+) ADP-ribosyltransferase 2; Poly[ADP-ribose] synthetase 2; pADPRT-2; hPARP-2 Serum 0.1 mg
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
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
20-272-190972 cleaved PARP - Mouse monoclonal [194C1439] to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Monoclonal 0.05 mg
18-272-197067 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg
18-272-197065 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg
18-272-197066 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg


 

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