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

WASH complex subunit 1 (WAS protein family homolog 1)

 WASH1_MOUSE             Reviewed;         475 AA.
Q8VDD8; Q3U473;
19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
12-SEP-2018, entry version 117.
RecName: Full=WASH complex subunit 1 {ECO:0000312|MGI:MGI:1916017};
AltName: Full=WAS protein family homolog 1;
Name=Washc1 {ECO:0000312|MGI:MGI:1916017};
Synonyms=Orf19, Wash, Wash1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10655549; DOI=10.1093/hmg/9.3.395;
Ciccodicola A., D'Esposito M., Esposito T., Gianfrancesco F.,
Migliaccio C., Miano M.G., Matarazzo M.R., Vacca M., Franze A.,
Cuccurese M., Cocchia M., Curci A., Terracciano A., Torino A.,
Cocchia S., Mercadante G., Pannone E., Archidiacono N., Rocchi M.,
Schlessinger D., D'Urso M.;
"Differentially regulated and evolved genes in the fully sequenced
Xq/Yq pseudoautosomal region.";
Hum. Mol. Genet. 9:395-401(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Cecum, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
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]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
"The Arp2/3 activator WASH controls the fission of endosomes through a
large multiprotein complex.";
Dev. Cell 17:712-723(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19732055; DOI=10.1111/j.1462-5822.2009.01380.x;
Haenisch J., Ehinger J., Ladwein M., Rohde M., Derivery E., Bosse T.,
Steffen A., Bumann D., Misselwitz B., Hardt W.D., Gautreau A.,
Stradal T.E., Rottner K.;
"Molecular dissection of Salmonella-induced membrane ruffling versus
invasion.";
Cell. Microbiol. 12:84-98(2010).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH BLOC1S2 AND TUBULIN GAMMA
CHAIN.
PubMed=20308062; DOI=10.1074/jbc.M109.078501;
Monfregola J., Napolitano G., D'Urso M., Lappalainen P., Ursini M.V.;
"Functional characterization of Wiskott-Aldrich syndrome protein and
scar homolog (WASH), a bi-modular nucleation-promoting factor able to
interact with biogenesis of lysosome-related organelle subunit 2
(BLOS2) and gamma-tubulin.";
J. Biol. Chem. 285:16951-16957(2010).
[8]
FUNCTION.
PubMed=22114305; DOI=10.1242/jcs.080986;
Zech T., Calaminus S.D., Caswell P., Spence H.J., Carnell M.,
Insall R.H., Norman J., Machesky L.M.;
"The Arp2/3 activator WASH regulates alpha5beta1-integrin-mediated
invasive migration.";
J. Cell Sci. 124:3753-3759(2011).
[9]
FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, AND INTERACTION WITH
BECN1.
PubMed=23974797; DOI=10.1038/emboj.2013.189;
Xia P., Wang S., Du Y., Zhao Z., Shi L., Sun L., Huang G., Ye B.,
Li C., Dai Z., Hou N., Cheng X., Sun Q., Li L., Yang X., Fan Z.;
"WASH inhibits autophagy through suppression of Beclin 1
ubiquitination.";
EMBO J. 32:2685-2696(2013).
[10]
FUNCTION.
PubMed=23275443; DOI=10.1128/MCB.01288-12;
Piotrowski J.T., Gomez T.S., Schoon R.A., Mangalam A.K.,
Billadeau D.D.;
"WASH knockout T cells demonstrate defective receptor trafficking,
proliferation, and effector function.";
Mol. Cell. Biol. 33:958-973(2013).
[11]
FUNCTION.
PubMed=24886983; DOI=10.1371/journal.pone.0098606;
Graham D.B., Osborne D.G., Piotrowski J.T., Gomez T.S., Gmyrek G.B.,
Akilesh H.M., Dani A., Billadeau D.D., Swat W.;
"Dendritic cells utilize the evolutionarily conserved WASH and
retromer complexes to promote MHCII recycling and helper T cell
priming.";
PLoS ONE 9:E98606-E98606(2014).
[12]
FUNCTION.
PubMed=24998208; DOI=10.1038/srep05596;
Wang F., Zhang L., Zhang G.L., Wang Z.B., Cui X.S., Kim N.H.,
Sun S.C.;
"WASH complex regulates Arp2/3 complex for actin-based polar body
extrusion in mouse oocytes.";
Sci. Rep. 4:5596-5596(2014).
[13]
INTERACTION WITH TBC1D23.
PubMed=29084197; DOI=10.1038/ncb3627;
Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
"TBC1D23 is a bridging factor for endosomal vesicle capture by golgins
at the trans-Golgi.";
Nat. Cell Biol. 19:1424-1432(2017).
-!- FUNCTION: Acts as a nucleation-promoting factor at the surface of
endosomes, where it recruits and activates the Arp2/3 complex to
induce actin polymerization, playing a key role in the fission of
tubules that serve as transport intermediates during endosome
sorting (PubMed:19922875). Its assembly in the WASH core complex
seems to inhibit its NPF activity and via WASHC2 is required for
its membrane targeting (By similarity). Regulates the trafficking
of endosomal alpha5beta1 integrin to the plasma membrane and
involved in invasive cell migration (PubMed:22114305). In T-cells
involved in endosome-to-membrane recycling of receptors including
T-cell receptor (TCR), CD28 and ITGAL; proposed to be implicated
in T-cell proliferation and effector function (PubMed:23275443).
In dendritic cells involved in endosome-to-membrane recycling of
major histocompatibility complex (MHC) class II probably involving
retromer and subsequently allowing antigen sampling, loading and
presentation during T-cell activation (PubMed:24886983). Involved
in cytokinesis and following polar body extrusion during oocyte
meiotic maturation (PubMed:24998208). Involved in Arp2/3 complex-
dependent actin assembly driving Salmonella typhimurium invasion
independent of ruffling (PubMed:19732055). Involved in the
exocytosis of MMP14 leading to matrix remodeling during invasive
migration and implicating late endosome-to-plasma membrane tubular
connections and cooperation with the exocyst complex (By
similarity). Involved in negative regulation of autophagy
independently from its role in endosomal sorting by inhibiting
BECN1 ubiquitination to inactivate PIK3C3/Vps34 activity
(PubMed:23974797). {ECO:0000250|UniProtKB:A8K0Z3,
ECO:0000250|UniProtKB:C4AMC7, ECO:0000269|PubMed:19732055,
ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:20308062,
ECO:0000269|PubMed:22114305, ECO:0000269|PubMed:23275443,
ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:24886983,
ECO:0000269|PubMed:24998208, ECO:0000305|PubMed:20308062}.
-!- SUBUNIT: Component of the WASH core complex also described as WASH
regulatory complex SHRC composed of WASHC1, WASHC2, WASHC3, WASHC4
and WASHC5. The WASH core complex associates with the F-actin-
capping protein dimer (formed by CAPZA1, CAPZA2 or CAPZA3 and
CAPZB) in a transient or substoichiometric manner which was
initially described as WASH complex. Interacts (via WHD1 region)
with WASHC2; the interaction is direct (By similarity). Interacts
with BECN1; WASHC1 and AMBRA1 can competetively interact with
BECN1 (PubMed:23974797). Interacts with BLOC1S2; may associate
with the BLOC-1 complex. Interacts with tubulin gamma chain (TUBG1
or TUBG2) (PubMed:20308062). Interacts with TBC1D23
(PubMed:29084197). {ECO:0000250|UniProtKB:A8K0Z3,
ECO:0000250|UniProtKB:C4AMC7, ECO:0000269|PubMed:20308062,
ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:29084197}.
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:19922875}. Recycling endosome membrane
{ECO:0000269|PubMed:19922875}. Cytoplasmic vesicle, autophagosome
{ECO:0000269|PubMed:23974797}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000269|PubMed:20308062}. Note=Localization to the endosome
membrane is mediated via its interaction with WASHC2 (By
similarity). Localized to Salmonella typhimurium entry sites
(PubMed:19732055). {ECO:0000250|UniProtKB:A8K0Z3,
ECO:0000269|PubMed:19732055}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:19922875}.
-!- DOMAIN: The VCA (verprolin, cofilin, acidic) domain promotes actin
polymerization by the Arp2/3 complex in vitro.
{ECO:0000250|UniProtKB:C4AMC7}.
-!- PTM: Ubiquitinated at Lys-219 via 'Lys-63'-linked ubiquitin chains
by the TRIM27:MAGEL2 E3 ubiquitin ligase complex, leading to
promote endosomal F-actin assembly.
{ECO:0000250|UniProtKB:A8K0Z3}.
-!- SIMILARITY: Belongs to the WASH1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE32561.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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; AJ304796; CAC83096.1; -; mRNA.
EMBL; AK033616; BAC28393.1; -; mRNA.
EMBL; AK149967; BAE29201.1; -; mRNA.
EMBL; AK154400; BAE32561.1; ALT_INIT; mRNA.
EMBL; AK159820; BAE35400.1; -; mRNA.
EMBL; AK171737; BAE42641.1; -; mRNA.
EMBL; AK172673; BAE43124.1; -; mRNA.
EMBL; BC025839; AAH25839.1; -; mRNA.
CCDS; CCDS28944.1; -.
RefSeq; NP_001032846.1; NM_001037757.1.
RefSeq; NP_081109.1; NM_026833.1.
RefSeq; XP_006524922.1; XM_006524859.1.
RefSeq; XP_006524923.1; XM_006524860.3.
UniGene; Mm.296545; -.
ProteinModelPortal; Q8VDD8; -.
BioGrid; 213039; 25.
ComplexPortal; CPX-1177; WASH complex, variant WASHC1/WASHC2.
IntAct; Q8VDD8; 28.
STRING; 10090.ENSMUSP00000072220; -.
iPTMnet; Q8VDD8; -.
PhosphoSitePlus; Q8VDD8; -.
EPD; Q8VDD8; -.
MaxQB; Q8VDD8; -.
PaxDb; Q8VDD8; -.
PeptideAtlas; Q8VDD8; -.
PRIDE; Q8VDD8; -.
Ensembl; ENSMUST00000072383; ENSMUSP00000072220; ENSMUSG00000024101.
Ensembl; ENSMUST00000116556; ENSMUSP00000112255; ENSMUSG00000024101.
GeneID; 68767; -.
KEGG; mmu:68767; -.
UCSC; uc008dgy.1; mouse.
CTD; 100287171; -.
MGI; MGI:1916017; Washc1.
eggNOG; ENOG410IFZ4; Eukaryota.
eggNOG; ENOG410YN2V; LUCA.
GeneTree; ENSGT00390000016717; -.
HOGENOM; HOG000007381; -.
HOVERGEN; HBG066686; -.
InParanoid; Q8VDD8; -.
KO; K18461; -.
OMA; NLRHEET; -.
OrthoDB; EOG091G0GKX; -.
PhylomeDB; Q8VDD8; -.
TreeFam; TF318222; -.
PRO; PR:Q8VDD8; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024101; Expressed in 259 organ(s), highest expression level in blood.
Genevisible; Q8VDD8; MM.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0071437; C:invadopodium; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0071203; C:WASH complex; IDA:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IMP:UniProtKB.
GO; GO:0002468; P:dendritic cell antigen processing and presentation; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0007032; P:endosome organization; IMP:MGI.
GO; GO:0099638; P:endosome to plasma membrane protein transport; IDA:MGI.
GO; GO:0006887; P:exocytosis; ISO:MGI.
GO; GO:0022617; P:extracellular matrix disassembly; ISO:MGI.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:MGI.
GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:1904109; P:positive regulation of cholesterol import; IMP:MGI.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:MGI.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI.
GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; IMP:UniProtKB.
GO; GO:0090306; P:spindle assembly involved in meiosis; IMP:UniProtKB.
GO; GO:0042098; P:T cell proliferation; IMP:UniProtKB.
InterPro; IPR028290; WASH1.
InterPro; IPR021854; WASH1_WAHD.
InterPro; IPR003124; WH2_dom.
PANTHER; PTHR23331; PTHR23331; 1.
Pfam; PF11945; WASH_WAHD; 1.
PROSITE; PS51082; WH2; 1.
1: Evidence at protein level;
Actin-binding; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endosome; Isopeptide bond; Membrane; Reference proteome;
Transport; Ubl conjugation.
CHAIN 1 475 WASH complex subunit 1.
/FTId=PRO_0000390963.
DOMAIN 369 391 WH2. {ECO:0000255|PROSITE-
ProRule:PRU00406}.
REGION 1 167 WHD1.
REGION 1 54 Required for WASH complex assembly.
{ECO:0000250|UniProtKB:C4AMC7}.
REGION 357 475 VCA. {ECO:0000250|UniProtKB:C4AMC7}.
COMPBIAS 267 331 Pro-rich.
COMPBIAS 346 349 Poly-Ser.
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:A8K0Z3}.
CONFLICT 15 15 Y -> C (in Ref. 2; BAE32561).
{ECO:0000305}.
SEQUENCE 475 AA; 51659 MW; 4198C8AEE499D3C3 CRC64;
MTPVKTQCSL AGQLYAVPLI QPDLRREEAI QQVADALQYL QNISGDIFSR ISRRVELSRR
QLQAISERVS LAQAKIEKIK GSKKAIKVFS SAKYPAPEHL QEYGSIFTGA LDPGLQRRPR
YRIQSKHRPL DERALQEKLK YFPVCVNTKS EPEDEAEEGL GGLPSNISSI SSLLLFNTTE
NLYKKYVFLD PLAGAVTKTH TMLGTEEEKL FDAPLSISKR EQLERQAPEN YFYVPDLGQV
PEIDVPSYLP DLPGVADDLM YSADLGPGIA PSAPGAIPEL PAFHTEVAEP LQPELENEVL
LAAPPPPPPP PPPPPPAPTA LVSTPQPPMF PDMATAAGQV AREEDSSSSM AHTASVQGAP
KEVVDPSSGR ATLLESIRQA GGIGKAKLRS VKERKLEKKK QKEQEQVRAT SQGGDLMSDL
FNKLVMRRKG ISGKGPSTGT SEGPGGAFSR MSDSIPPLPP PQQPAGDEDE EDWES


Related products :

Catalog number Product name Quantity
EIAAB08144 Barren homolog protein 1,BRRN,BRRN1,CAPH,Chromosome-associated protein H,Condensin complex subunit 2,hCAP-H,Homo sapiens,Human,KIAA0074,NCAPH,Non-SMC condensin I complex subunit H,XCAP-H homolog
EIAAB08145 Barren homolog protein 1,Brrn,Brrn1,Caph,Chromosome-associated protein H,Condensin complex subunit 2,mCAP-H,Mouse,Mus musculus,Ncaph,Non-SMC condensin I complex subunit H,XCAP-H homolog
EIAAB11359 CBF5 homolog,DKC1,Dyskerin,H_ACA ribonucleoprotein complex subunit 4,Homo sapiens,Human,NOLA4,Nopp140-associated protein of 57 kDa,Nucleolar protein family A member 4,Nucleolar protein NAP57,snoRNP pr
OBT1775 CSN1 (COP9 Signalosome Complex Subunit 1), COPS1 (COP9 Constitutive Photomorphogenic homolog Subunit 1), GPS1 (G Protein Pathway Surppressor 1), MFH protein Arabidopsis Fus6_Cop11 homolog, Rabbit ant 0.1 mg.
OBT1775 CSN1 (COP9 Signalosome Complex Subunit 1), COPS1 (COP9 Constitutive Photomorphogenic homolog Subunit 1), GPS1 (G Protein Pathway Surppressor 1), MFH protein Arabidopsis Fus6_Cop11 homolog, Rabbit ant 0.1 mg.
EIAAB08496 COG complex subunit 3,COG3,Component of oligomeric Golgi complex 3,Conserved oligomeric Golgi complex subunit 3,Homo sapiens,Human,p94,SEC34,Vesicle-docking protein SEC34 homolog
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.1 mg
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.05 mg
EIAAB06421 ANAPC6,Anaphase-promoting complex subunit 6,APC6,CDC16,CDC16 homolog,CDC16Hs,Cell division cycle protein 16 homolog,Cyclosome subunit 6,Homo sapiens,Human
EIAAB33312 Complex III subunit 8,Complex III subunit VIII,Cytochrome b-c1 complex subunit 8,Low molecular mass ubiquinone-binding protein,Qpc,Rat,Rattus norvegicus,Ubiquinol-cytochrome c reductase complex 9.5 kD
EIAAB33310 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Homo sapiens,Human,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQBP,UQCRB
EIAAB33299 Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Homo sapiens,Human,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,UQCR,UQCR11
EIAAB33298 Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,Uqcr,Uqcr11
EIAAB33300 Bos taurus,Bovine,Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,UQCR,UQCR11
EIAAB33317 Complex III subunit 9,Complex III subunit X,Cytochrome b-c1 complex subunit 9,Cytochrome c1 non-heme 7 kDa protein,Homo sapiens,HSPC119,Human,Ubiquinol-cytochrome c reductase complex 7.2 kDa protein,U
30-178 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
26-111 NCAPH is a member of the barr family and a regulatory subunit of the condensin complex. This complex is required for the conversion of interphase chromatin into condensed chromosomes. The protein is a 0.05 mg
EIAAB33309 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 14 kDa protein,Uqcrb
EIAAB33311 Bos taurus,Bovine,Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQCRB
EIAAB33316 Complex III subunit 9,Complex III subunit X,Cytochrome b-c1 complex subunit 9,Cytochrome c1 non-heme 7 kDa protein,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 7.2 kDa protein,Uqcr10
EIAAB33318 Bos taurus,Bovine,Complex III subunit 9,Complex III subunit X,Cytochrome b-c1 complex subunit 9,Cytochrome c1 non-heme 7 kDa protein,Ubiquinol-cytochrome c reductase complex 7.2 kDa protein,UQCR10
EIAAB06428 ANAPC12,Anaphase-promoting complex subunit 12,Anaphase-promoting complex subunit CDC26,APC12,C9orf17,CDC26,Cell division cycle protein 26 homolog,Homo sapiens,Human
EIAAB10216 Bos taurus,Bovine,Complex III subunit 4,Complex III subunit IV,CYC1,Cytochrome b-c1 complex subunit 4,Cytochrome c-1,Cytochrome c1, heme protein, mitochondrial,Ubiquinol-cytochrome-c reductase complex
18-003-43113 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.1 mg Protein A
18-003-43113 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.05 mg Aff Pur


 

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