Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Poly [ADP-ribose] polymerase 10 (PARP-10) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 10) (ARTD10)

 PAR10_HUMAN             Reviewed;        1025 AA.
Q53GL7; Q8N2I0; Q8WV05; Q96CH7; Q96K72;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
18-JUL-2018, entry version 123.
RecName: Full=Poly [ADP-ribose] polymerase 10;
Short=PARP-10;
EC=2.4.2.30;
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 10;
Short=ARTD10;
Name=PARP10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-630.
TISSUE=Mammary gland, and Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-1025.
TISSUE=Skin, and Uterus;
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).
[4]
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND INTERACTION WITH MYC.
PubMed=15674325; DOI=10.1038/sj.onc.1208410;
Yu M., Schreek S., Cerni C., Schamberger C., Lesniewicz K., Poreba E.,
Vervoorts J., Walsemann G., Groetzinger J., Kremmer E., Mehraein Y.,
Mertsching J., Kraft R., Austen M., Luescher-Firzlaff J., Luescher B.;
"PARP-10, a novel Myc-interacting protein with poly(ADP-ribose)
polymerase activity, inhibits transformation.";
Oncogene 24:1982-1993(2005).
[5]
FUNCTION, AND PHOSPHORYLATION AT THR-101.
PubMed=16455663; DOI=10.1074/jbc.M506745200;
Chou H.Y., Chou H.T., Lee S.C.;
"CDK-dependent activation of poly(ADP-ribose) polymerase member 10
(PARP10).";
J. Biol. Chem. 281:15201-15207(2006).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-916, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND SER-1011, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[9]
INTERACTION WITH PARP14, AND MUTAGENESIS OF GLY-888.
PubMed=23473667; DOI=10.1016/j.str.2012.12.019;
Forst A.H., Karlberg T., Herzog N., Thorsell A.G., Gross A.,
Feijs K.L., Verheugd P., Kursula P., Nijmeijer B., Kremmer E.,
Kleine H., Ladurner A.G., Schuler H., Luscher B.;
"Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8
macrodomains.";
Structure 21:462-475(2013).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-423; SER-431
AND SER-663, 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).
[11]
STRUCTURE BY NMR OF 7-101.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RRM domain in the human poly (ADP-ribose)
polymerase family, member 10 variant.";
Submitted (FEB-2007) to the PDB data bank.
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 809-1017.
Structural genomics consortium (SGC);
"Human poly(ADP-ribose) polymerase 10, catalytic fragment in complex
with an inhibitor 3-aminobenzamide.";
Submitted (JUN-2009) to the PDB data bank.
-!- FUNCTION: May play a role in cell proliferation. May be required
for the maintenance of cell cycle progression.
{ECO:0000269|PubMed:15674325, ECO:0000269|PubMed:16455663}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397}.
-!- SUBUNIT: Interacts with MYC (PubMed:15674325). Interacts with
PARP14 (PubMed:23473667). {ECO:0000269|PubMed:15674325,
ECO:0000269|PubMed:23473667}.
-!- INTERACTION:
Q9Y530:OARD1; NbExp=3; IntAct=EBI-2857573, EBI-8502288;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:15674325}. Cytoplasm
{ECO:0000269|PubMed:15674325}. Note=Shuttles between the nuclear
and cytoplasmic compartment. A subpopulation concentrates in the
nucleolus during late G1/S phase.
-!- TISSUE SPECIFICITY: Highly expressed in spleen and thymus.
Intermediate levels in liver, kidney, pancreas, prostate, testis,
ovary, intestine, and leukocytes. Low expression in heart, brain,
placenta, lung, skeletal muscle, and colon.
{ECO:0000269|PubMed:15674325}.
-!- PTM: Stimulated through its phosphorylation by CDK2. Acquires CDK-
dependent phosphorylation through late-G1 to S phase, and from
prometaphase to cytokinesis in the nucleolar organizing regions.
Phosphorylation is suppressed in growth-arrested cells.
{ECO:0000269|PubMed:16455663}.
-!- SEQUENCE CAUTION:
Sequence=BAC11498.1; Type=Frameshift; Positions=965; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK027370; BAB55067.1; -; mRNA.
EMBL; AK075250; BAC11498.1; ALT_SEQ; mRNA.
EMBL; AK222914; BAD96634.1; -; mRNA.
EMBL; BC014229; AAH14229.2; -; mRNA.
EMBL; BC019030; AAH19030.2; -; mRNA.
CCDS; CCDS34960.1; -.
RefSeq; NP_116178.2; NM_032789.4.
UniGene; Hs.348609; -.
PDB; 2DHX; NMR; -; A=10-100.
PDB; 3HKV; X-ray; 2.10 A; A/B=809-1017.
PDB; 5LX6; X-ray; 1.25 A; A/B=819-1007.
PDBsum; 2DHX; -.
PDBsum; 3HKV; -.
PDBsum; 5LX6; -.
ProteinModelPortal; Q53GL7; -.
SMR; Q53GL7; -.
BioGrid; 124320; 21.
IntAct; Q53GL7; 4.
MINT; Q53GL7; -.
STRING; 9606.ENSP00000325618; -.
BindingDB; Q53GL7; -.
ChEMBL; CHEMBL2429708; -.
iPTMnet; Q53GL7; -.
PhosphoSitePlus; Q53GL7; -.
BioMuta; PARP10; -.
DMDM; 116248563; -.
EPD; Q53GL7; -.
MaxQB; Q53GL7; -.
PaxDb; Q53GL7; -.
PeptideAtlas; Q53GL7; -.
PRIDE; Q53GL7; -.
ProteomicsDB; 62485; -.
Ensembl; ENST00000313028; ENSP00000325618; ENSG00000178685.
GeneID; 84875; -.
KEGG; hsa:84875; -.
UCSC; uc003zal.5; human.
CTD; 84875; -.
EuPathDB; HostDB:ENSG00000178685.13; -.
GeneCards; PARP10; -.
H-InvDB; HIX0201285; -.
HGNC; HGNC:25895; PARP10.
HPA; HPA028122; -.
HPA; HPA052427; -.
MIM; 609564; gene.
neXtProt; NX_Q53GL7; -.
OpenTargets; ENSG00000178685; -.
PharmGKB; PA134892853; -.
eggNOG; ENOG410IH3S; Eukaryota.
eggNOG; ENOG411034Y; LUCA.
GeneTree; ENSGT00760000119084; -.
HOVERGEN; HBG068843; -.
InParanoid; Q53GL7; -.
KO; K15261; -.
PhylomeDB; Q53GL7; -.
TreeFam; TF328965; -.
Reactome; R-HSA-197264; Nicotinamide salvaging.
ChiTaRS; PARP10; human.
EvolutionaryTrace; Q53GL7; -.
GeneWiki; PARP10; -.
GenomeRNAi; 84875; -.
PRO; PR:Q53GL7; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000178685; -.
CleanEx; HS_PARP10; -.
ExpressionAtlas; Q53GL7; baseline and differential.
Genevisible; Q53GL7; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IMP:UniProtKB.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:UniProtKB.
GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:1900045; P:negative regulation of protein K63-linked ubiquitination; IMP:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; IMP:UniProtKB.
GO; GO:0070213; P:protein auto-ADP-ribosylation; IMP:UniProtKB.
GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
GO; GO:0010847; P:regulation of chromatin assembly; IDA:UniProtKB.
CDD; cd12547; RRM1_2_PAR10; 2.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034464; PAR10_RRM1_2.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
Pfam; PF00644; PARP; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Glycosyltransferase; NAD; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 1025 Poly [ADP-ribose] polymerase 10.
/FTId=PRO_0000252435.
DOMAIN 806 1025 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
REGION 700 907 Myc binding.
MOTIF 650 667 Ubiquitin-interacting.
MOTIF 673 690 Ubiquitin-interacting.
COMPBIAS 186 193 Poly-Leu.
COMPBIAS 588 697 Glu-rich.
MOD_RES 101 101 Phosphothreonine.
{ECO:0000269|PubMed:16455663}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 663 663 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 916 916 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1011 1011 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 249 249 I -> V (in dbSNP:rs11136344).
/FTId=VAR_027859.
VARIANT 395 395 L -> P (in dbSNP:rs11136343).
/FTId=VAR_027860.
VARIANT 630 630 V -> A (in dbSNP:rs11544989).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_027861.
MUTAGEN 888 888 G->W: Abolishes catalytic activity;
abolishes interaction with PARP14.
{ECO:0000305|PubMed:23473667}.
CONFLICT 313 313 M -> I (in Ref. 1; BAB55067).
{ECO:0000305}.
CONFLICT 518 518 P -> S (in Ref. 1; BAB55067).
{ECO:0000305}.
CONFLICT 813 813 L -> P (in Ref. 3; AAH14229).
{ECO:0000305}.
CONFLICT 922 922 R -> K (in Ref. 1; BAB55067).
{ECO:0000305}.
CONFLICT 1013 1013 D -> G (in Ref. 2; BAD96634).
{ECO:0000305}.
STRAND 12 17 {ECO:0000244|PDB:2DHX}.
HELIX 24 32 {ECO:0000244|PDB:2DHX}.
TURN 34 37 {ECO:0000244|PDB:2DHX}.
STRAND 43 48 {ECO:0000244|PDB:2DHX}.
STRAND 51 55 {ECO:0000244|PDB:2DHX}.
HELIX 59 66 {ECO:0000244|PDB:2DHX}.
STRAND 72 77 {ECO:0000244|PDB:2DHX}.
STRAND 79 82 {ECO:0000244|PDB:2DHX}.
STRAND 819 822 {ECO:0000244|PDB:5LX6}.
STRAND 825 827 {ECO:0000244|PDB:3HKV}.
HELIX 828 839 {ECO:0000244|PDB:5LX6}.
HELIX 842 844 {ECO:0000244|PDB:5LX6}.
TURN 845 847 {ECO:0000244|PDB:5LX6}.
STRAND 848 856 {ECO:0000244|PDB:5LX6}.
HELIX 859 875 {ECO:0000244|PDB:5LX6}.
STRAND 883 889 {ECO:0000244|PDB:5LX6}.
HELIX 891 893 {ECO:0000244|PDB:5LX6}.
HELIX 894 900 {ECO:0000244|PDB:5LX6}.
HELIX 904 906 {ECO:0000244|PDB:5LX6}.
STRAND 916 923 {ECO:0000244|PDB:5LX6}.
HELIX 924 927 {ECO:0000244|PDB:5LX6}.
TURN 930 932 {ECO:0000244|PDB:5LX6}.
STRAND 941 948 {ECO:0000244|PDB:5LX6}.
STRAND 952 955 {ECO:0000244|PDB:5LX6}.
STRAND 961 963 {ECO:0000244|PDB:3HKV}.
STRAND 971 974 {ECO:0000244|PDB:5LX6}.
STRAND 976 980 {ECO:0000244|PDB:5LX6}.
STRAND 982 984 {ECO:0000244|PDB:5LX6}.
STRAND 987 990 {ECO:0000244|PDB:5LX6}.
STRAND 995 1006 {ECO:0000244|PDB:5LX6}.
SEQUENCE 1025 AA; 109998 MW; AC9CCFCF9B83A989 CRC64;
MVAMAEAEAG VAVEVRGLPP AVPDELLTLY FENRRRSGGG PVLSWQRLGC GGVLTFREPA
DAERVLAQAD HELHGAQLSL RPAPPRAPAR LLLQGLPPGT TPQRLEQHVQ ALLRASGLPV
QPCCALASPR PDRALVQLPK PLSEADVRVL EEQAQNLGLE GTLVSLARVP QARAVRVVGD
GASVDLLLLE LYLENERRSG GGPLEDLQRL PGPLGTVASF QQWQVAERVL QQEHRLQGSE
LSLVPHYDIL EPEELAENTS GGDHPSTQGP RATKHALLRT GGLVTALQGA GTVTMGSGEE
PGQSGASLRT GPMVQGRGIM TTGSGQEPGQ SGTSLRTGPM GSLGQAEQVS SMPMGSLEHE
GLVSLRPVGL QEQEGPMSLG PVGSAGPVET SKGLLGQEGL VEIAMDSPEQ EGLVGPMEIT
MGSLEKAGPV SPGCVKLAGQ EGLVEMVLLM EPGAMRFLQL YHEDLLAGLG DVALLPLEGP
DMTGFRLCGA QASCQAAEEF LRSLLGSISC HVLCLEHPGS ARFLLGPEGQ HLLQGLEAQF
QCVFGTERLA TATLDTGLEE VDPTEALPVL PGNAHTLWTP DSTGGDQEDV SLEEVRELLA
TLEGLDLDGE DWLPRELEEE GPQEQPEEEV TPGHEEEEPV APSTVAPRWL EEEAALQLAL
HRSLEPQGQV AEQEEAAALR QALTLSLLEQ PPLEAEEPPD GGTDGKAQLV VHSAFEQDVE
ELDRALRAAL EVHVQEETVG PWRRTLPAEL RARLERCHGV SVALRGDCTI LRGFGAHPAR
AARHLVALLA GPWDQSLAFP LAASGPTLAG QTLKGPWNNL ERLAENTGEF QEVVRAFYDT
LDAARSSIRV VRVERVSHPL LQQQYELYRE RLLQRCERRP VEQVLYHGTT APAVPDICAH
GFNRSFCGRN ATVYGKGVYF ARRASLSVQD RYSPPNADGH KAVFVARVLT GDYGQGRRGL
RAPPLRGPGH VLLRYDSAVD CICQPSIFVI FHDTQALPTH LITCEHVPRA SPDDPSGLPG
RSPDT


Related products :

Catalog number Product name Quantity
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 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 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
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
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
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
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
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
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
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
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
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
EIAAB29933 Homo sapiens,Human,PARP7,PARP-7,Poly [ADP-ribose] polymerase 7,TCDD-inducible poly [ADP-ribose] polymerase,TIPARP
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
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
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur