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

Ubiquitin carboxyl-terminal hydrolase 45 (EC 3.4.19.12) (Deubiquitinating enzyme 45) (Ubiquitin thioesterase 45) (Ubiquitin-specific-processing protease 45)

 UBP45_HUMAN             Reviewed;         814 AA.
Q70EL2; B2RXG0; Q5T062; Q86T44; Q86TC0; Q9BRU1;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
12-SEP-2018, entry version 123.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 45;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 45;
AltName: Full=Ubiquitin thioesterase 45;
AltName: Full=Ubiquitin-specific-processing protease 45;
Name=USP45;
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 1), CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C.,
Cal S., Lopez-Otin C.;
"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
proteases.";
Biochem. Biophys. Res. Commun. 314:54-62(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 248-814 (ISOFORM 1), AND VARIANT
SER-778.
TISSUE=Skeletal muscle;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS GLU-67; THR-521 AND SER-778.
TISSUE=Bone marrow, and Brain cortex;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
{ECO:0000269|PubMed:14715245}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q70EL2-1; Sequence=Displayed;
Name=2;
IsoId=Q70EL2-2; Sequence=VSP_023791, VSP_023792;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q70EL2-3; Sequence=VSP_023789, VSP_023790, VSP_023793;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
ovary, skeletal muscle and spleen. {ECO:0000269|PubMed:14715245}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {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; AJ583819; CAE47746.2; -; mRNA.
EMBL; AL713747; CAD89915.1; -; mRNA.
EMBL; AL832030; CAD91148.1; -; mRNA.
EMBL; AL137784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL513550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005991; AAH05991.1; -; mRNA.
EMBL; BC150648; AAI50649.1; -; mRNA.
EMBL; BC157838; AAI57839.1; -; mRNA.
CCDS; CCDS34501.1; -. [Q70EL2-1]
CCDS; CCDS87419.1; -. [Q70EL2-2]
RefSeq; NP_001073950.1; NM_001080481.1. [Q70EL2-1]
RefSeq; NP_001332950.1; NM_001346021.1. [Q70EL2-1]
RefSeq; NP_001332951.1; NM_001346022.1. [Q70EL2-1]
RefSeq; XP_005267227.1; XM_005267170.4. [Q70EL2-1]
UniGene; Hs.143410; -.
UniGene; Hs.677065; -.
ProteinModelPortal; Q70EL2; -.
SMR; Q70EL2; -.
BioGrid; 124430; 30.
IntAct; Q70EL2; 27.
STRING; 9606.ENSP00000333376; -.
MEROPS; C19.064; -.
iPTMnet; Q70EL2; -.
PhosphoSitePlus; Q70EL2; -.
BioMuta; USP45; -.
DMDM; 296453002; -.
EPD; Q70EL2; -.
MaxQB; Q70EL2; -.
PaxDb; Q70EL2; -.
PeptideAtlas; Q70EL2; -.
PRIDE; Q70EL2; -.
ProteomicsDB; 68545; -.
ProteomicsDB; 68546; -. [Q70EL2-2]
ProteomicsDB; 68547; -. [Q70EL2-3]
DNASU; 85015; -.
Ensembl; ENST00000327681; ENSP00000333376; ENSG00000123552. [Q70EL2-1]
Ensembl; ENST00000500704; ENSP00000424372; ENSG00000123552. [Q70EL2-1]
GeneID; 85015; -.
KEGG; hsa:85015; -.
UCSC; uc003ppx.4; human. [Q70EL2-1]
CTD; 85015; -.
EuPathDB; HostDB:ENSG00000123552.17; -.
GeneCards; USP45; -.
H-InvDB; HIX0006090; -.
HGNC; HGNC:20080; USP45.
HPA; HPA029602; -.
HPA; HPA029604; -.
neXtProt; NX_Q70EL2; -.
OpenTargets; ENSG00000123552; -.
PharmGKB; PA134889604; -.
eggNOG; KOG1873; Eukaryota.
eggNOG; COG5560; LUCA.
GeneTree; ENSGT00860000133682; -.
HOGENOM; HOG000154755; -.
HOVERGEN; HBG062704; -.
InParanoid; Q70EL2; -.
KO; K11844; -.
OMA; QHVSHAI; -.
OrthoDB; EOG091G01WT; -.
PhylomeDB; Q70EL2; -.
TreeFam; TF326075; -.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
ChiTaRS; USP45; human.
GenomeRNAi; 85015; -.
PRO; PR:Q70EL2; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000123552; Expressed in 179 organ(s), highest expression level in corpus callosum.
CleanEx; HS_USP45; -.
ExpressionAtlas; Q70EL2; baseline and differential.
Genevisible; Q70EL2; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006281; P:DNA repair; IMP:MGI.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR001607; Znf_UBP.
Pfam; PF00443; UCH; 1.
Pfam; PF02148; zf-UBP; 1.
SUPFAM; SSF54001; SSF54001; 2.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
PROSITE; PS50271; ZF_UBP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Hydrolase; Metal-binding;
Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 814 Ubiquitin carboxyl-terminal hydrolase 45.
/FTId=PRO_0000280561.
DOMAIN 190 813 USP.
ZN_FING 60 136 UBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00502}.
ACT_SITE 199 199 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 746 746 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K387}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K387}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K387}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K387}.
VAR_SEQ 1 262 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_023789.
VAR_SEQ 263 282 KETEKGPLSPKVLFNQLCQK -> MRSKKVVQNSRFFLPQT
LSW (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_023790.
VAR_SEQ 283 289 APRFKDF -> RVHLHLI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023791.
VAR_SEQ 290 814 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023792.
VAR_SEQ 312 369 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_023793.
VARIANT 67 67 K -> E (in dbSNP:rs7744845).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031167.
VARIANT 521 521 R -> T (in dbSNP:rs41288947).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_060663.
VARIANT 778 778 N -> S (in dbSNP:rs6570065).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_031168.
CONFLICT 603 603 A -> V (in Ref. 2; CAD91148).
{ECO:0000305}.
CONFLICT 691 691 Q -> K (in Ref. 1; CAE47746).
{ECO:0000305}.
CONFLICT 726 726 D -> G (in Ref. 2; CAD89915).
{ECO:0000305}.
SEQUENCE 814 AA; 91733 MW; DE4FCC0AD7AD6499 CRC64;
MRVKDPTKAL PEKAKRSKRP TVPHDEDSSD DIAVGLTCQH VSHAISVNHV KRAIAENLWS
VCSECLKERR FYDGQLVLTS DIWLCLKCGF QGCGKNSESQ HSLKHFKSSR TEPHCIIINL
STWIIWCYEC DEKLSTHCNK KVLAQIVDFL QKHASKTQTS AFSRIMKLCE EKCETDEIQK
GGKCRNLSVR GITNLGNTCF FNAVMQNLAQ TYTLTDLMNE IKESSTKLKI FPSSDSQLDP
LVVELSRPGP LTSALFLFLH SMKETEKGPL SPKVLFNQLC QKAPRFKDFQ QQDSQELLHY
LLDAVRTEET KRIQASILKA FNNPTTKTAD DETRKKVKAY GKEGVKMNFI DRIFIGELTS
TVMCEECANI STVKDPFIDI SLPIIEERVS KPLLWGRMNK YRSLRETDHD RYSGNVTIEN
IHQPRAAKKH SSSKDKSQLI HDRKCIRKLS SGETVTYQKN ENLEMNGDSL MFASLMNSES
RLNESPTDDS EKEASHSESN VDADSEPSES ESASKQTGLF RSSSGSGVQP DGPLYPLSAG
KLLYTKETDS GDKEMAEAIS ELRLSSTVTG DQDFDRENQP LNISNNLCFL EGKHLRSYSP
QNAFQTLSQS YITTSKECSI QSCLYQFTSM ELLMGNNKLL CENCTKNKQK YQEETSFAEK
KVEGVYTNAR KQLLISAVPA VLILHLKRFH QAGLSLRKVN RHVDFPLMLD LAPFCSATCK
NASVGDKVLY GLYGIVEHSG SMREGHYTAY VKVRTPSRKL SEHNTKKKNV PGLKAADNES
AGQWVHVSDT YLQVVPESRA LSAQAYLLFY ERVL


Related products :

Catalog number Product name Quantity
EIAAB45096 Deubiquitinating enzyme 7,HAUSP,Herpesvirus-associated ubiquitin-specific protease,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing pro
EIAAB45055 Deubiquitinating enzyme 4,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 4,Ubiquitin thioesterase 4,Ubiquitin-specific-processing protease 4,Usp4
EIAAB44991 Deubiquitinating enzyme 16,Homo sapiens,Human,MSTP039,Ubiquitin carboxyl-terminal hydrolase 16,Ubiquitin thiolesterase 16,Ubiquitin-processing protease UBP-M,Ubiquitin-specific-processing protease 16,
EIAAB45002 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubiquitin-
EIAAB45093 Chicken,Deubiquitinating enzyme 7,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7,USP7
EIAAB45022 Deubiquitinating enzyme 27,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 22-like,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 2
EIAAB45023 Deubiquitinating enzyme 27,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 27,Usp27,Usp27x,X-linked ubiquitin carboxyl-ter
EIAAB44981 Deubiquitinating enzyme 12,Mouse,Mus musculus,Ubh1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,Usp12
EIAAB45005 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
EIAAB45001 41 kDa ubiquitin-specific protease,Bos taurus,Bovine,Deubiquitinating enzyme 2,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
EIAAB45004 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,MNCb-0190,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubp
EIAAB45076 Deubiquitinating enzyme 48,Rat,Rattus norvegicus,Synaptic ubiquitin-specific protease,synUSP,Ubiquitin carboxyl-terminal hydrolase 48,Ubiquitin thiolesterase 48,Ubiquitin-specific-processing protease
EIAAB45095 Deubiquitinating enzyme 7,Hausp,Herpesvirus-associated ubiquitin-specific protease,mHAUSP,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-process
EIAAB45094 Deubiquitinating enzyme 7,Hausp,Herpesvirus-associated ubiquitin-specific protease,Rat,Rattus norvegicus,rHAUSP,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-proc
EIAAB44983 Deubiquitinating enzyme 12,Homo sapiens,Human,UBH1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,USP12,US
EIAAB45098 Deubiquitinating enzyme 8,Kiaa0055,Mouse,mUBPy,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 8,Ubiquitin isopeptidase Y,Ubiquitin thiolesterase 8,Ubiquitin-specific-processing protease 8,Ubpy,Usp
EIAAB45039 Deubiquitinating enzyme 33,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 33,Ubiquitin thiolesterase 33,Ubiquitin-specific-processing protease 33,Usp33,Vdu1,VHL-interacting deubiquitinating
EIAAB45097 Deubiquitinating enzyme 8,Homo sapiens,hUBPy,Human,KIAA0055,Ubiquitin carboxyl-terminal hydrolase 8,Ubiquitin isopeptidase Y,Ubiquitin thiolesterase 8,Ubiquitin-specific-processing protease 8,UBPY,USP
EIAAB45050 Deubiquitinating enzyme 37,Pig,Sus scrofa,Ubiquitin carboxyl-terminal hydrolase 37,Ubiquitin thiolesterase 37,Ubiquitin-specific-processing protease 37,USP37
EIAAB45067 Inactive deubiquitinating enzyme 44,Inactive ubiquitin carboxyl-terminal hydrolase 44,Inactive ubiquitin thioesterase 44,Inactive ubiquitin-specific-processing protease 44,Mouse,Mus musculus,Usp44
EIAAB45052 Deubiquitinating enzyme 38,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 38,Ubiquitin thiolesterase 38,Ubiquitin-specific-processing protease 38,Usp38
EIAAB45069 Deubiquitinating enzyme 45,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 45,Ubiquitin thiolesterase 45,Ubiquitin-specific-processing protease 45,Usp45
EIAAB45066 Deubiquitinating enzyme 43,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 43,Ubiquitin thiolesterase 43,Ubiquitin-specific-processing protease 43,Usp43
EIAAB45072 Deubiquitinating enzyme 46,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 46,Ubiquitin thiolesterase 46,Ubiquitin-specific-processing protease 46,Usp46
EIAAB45073 Deubiquitinating enzyme 47,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 47,Ubiquitin thiolesterase 47,Ubiquitin-specific-processing protease 47,Usp47


 

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