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

Proteasome subunit alpha type-3 (EC 3.4.25.1) (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K)

 PSA3_MOUSE              Reviewed;         255 AA.
O70435;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 156.
RecName: Full=Proteasome subunit alpha type-3;
EC=3.4.25.1 {ECO:0000250|UniProtKB:P25788};
AltName: Full=Macropain subunit C8;
AltName: Full=Multicatalytic endopeptidase complex subunit C8;
AltName: Full=Proteasome component C8;
AltName: Full=Proteasome subunit K;
Name=Psma3;
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].
Gao Y., Simons M.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=10436176; DOI=10.1007/s002510050562;
Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
"The complete primary structure of mouse 20S proteasomes.";
Immunogenetics 49:835-842(1999).
[3]
PROTEIN SEQUENCE OF 73-86.
TISSUE=Brain;
Lubec G., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[4]
IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, AND ACETYLATION AT
SER-2.
PubMed=16857966; DOI=10.1161/01.RES.0000237386.98506.f7;
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F.,
Ping P.;
"Mapping the murine cardiac 26S proteasome complexes.";
Circ. Res. 99:362-371(2006).
[5]
FUNCTION.
PubMed=16581775; DOI=10.1128/MCB.26.8.2999-3007.2006;
Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
Sleckman B.P.;
"Proteasome activator PA200 is required for normal spermatogenesis.";
Mol. Cell. Biol. 26:2999-3007(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME,
SUBUNIT, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J.,
Groettrup M., Groll M.;
"Immuno- and constitutive proteasome crystal structures reveal
differences in substrate and inhibitor specificity.";
Cell 148:727-738(2012).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby
mediates its degradation. Negatively regulates the membrane
trafficking of the cell-surface thromboxane A2 receptor (TBXA2R)
isoform 2. {ECO:0000269|PubMed:16581775,
ECO:0000269|PubMed:22341445}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000255|PROSITE-ProRule:PRU00808}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966,
PubMed:22341445). Interacts with AURKB. Interacts with CDKN1A.
Interacts with MDM2 and RB1. Interacts with the C-terminus of
TBXA2R isoform 2. Interacts with DNAJB2.
{ECO:0000250|UniProtKB:P25788, ECO:0000269|PubMed:16857966,
ECO:0000269|PubMed:22341445}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25788}.
Nucleus {ECO:0000250|UniProtKB:P25788}.
-!- TISSUE SPECIFICITY: Detected in liver (at protein level).
{ECO:0000269|PubMed:22341445}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF055983; AAC12943.1; -; mRNA.
EMBL; AF060089; AAD50534.1; -; mRNA.
CCDS; CCDS25961.1; -.
RefSeq; NP_035314.3; NM_011184.5.
RefSeq; XP_017170485.1; XM_017314996.1.
UniGene; Mm.296338; -.
PDB; 3UNB; X-ray; 2.90 A; F/T/h/v=1-255.
PDB; 3UNE; X-ray; 3.20 A; F/T/h/v=1-255.
PDB; 3UNF; X-ray; 2.90 A; F/T=1-255.
PDB; 3UNH; X-ray; 3.20 A; F/T=1-255.
PDBsum; 3UNB; -.
PDBsum; 3UNE; -.
PDBsum; 3UNF; -.
PDBsum; 3UNH; -.
ProteinModelPortal; O70435; -.
SMR; O70435; -.
BioGrid; 202417; 1.
CORUM; O70435; -.
IntAct; O70435; 9.
STRING; 10090.ENSMUSP00000125548; -.
iPTMnet; O70435; -.
PhosphoSitePlus; O70435; -.
SwissPalm; O70435; -.
EPD; O70435; -.
PaxDb; O70435; -.
PeptideAtlas; O70435; -.
PRIDE; O70435; -.
Ensembl; ENSMUST00000160027; ENSMUSP00000125548; ENSMUSG00000060073.
GeneID; 19167; -.
KEGG; mmu:19167; -.
UCSC; uc007ntz.2; mouse.
CTD; 5684; -.
MGI; MGI:104883; Psma3.
eggNOG; KOG0184; Eukaryota.
eggNOG; ENOG410XP01; LUCA.
GeneTree; ENSGT00550000074912; -.
HOVERGEN; HBG105566; -.
InParanoid; O70435; -.
KO; K02727; -.
OMA; FELEMTW; -.
OrthoDB; EOG091G0GQL; -.
PhylomeDB; O70435; -.
TreeFam; TF106208; -.
Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-MMU-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
Reactome; R-MMU-446652; Interleukin-1 family signaling.
Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
Reactome; R-MMU-4641257; Degradation of AXIN.
Reactome; R-MMU-4641258; Degradation of DVL.
Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-MMU-5632684; Hedgehog 'on' state.
Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
Reactome; R-MMU-5689603; UCH proteinases.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-MMU-68949; Orc1 removal from chromatin.
Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-MMU-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-MMU-69481; G2/M Checkpoints.
Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:O70435; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000060073; -.
ExpressionAtlas; O70435; baseline and differential.
Genevisible; O70435; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0000502; C:proteasome complex; ISO:MGI.
GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
Pfam; PF00227; Proteasome; 1.
Pfam; PF10584; Proteasome_A_N; 1.
SMART; SM00948; Proteasome_A_N; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein;
Protease; Proteasome; Reference proteome; Threonine protease.
INIT_MET 1 1 Removed. {ECO:0000305|PubMed:16857966}.
CHAIN 2 255 Proteasome subunit alpha type-3.
/FTId=PRO_0000124092.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:16857966}.
MOD_RES 57 57 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 206 206 N6-acetyllysine.
{ECO:0000250|UniProtKB:P25788}.
MOD_RES 230 230 N6-acetyllysine.
{ECO:0000250|UniProtKB:P25788}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000250|UniProtKB:P25788}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
STRAND 5 10 {ECO:0000244|PDB:3UNB}.
HELIX 22 32 {ECO:0000244|PDB:3UNB}.
STRAND 37 42 {ECO:0000244|PDB:3UNB}.
STRAND 45 53 {ECO:0000244|PDB:3UNB}.
STRAND 67 71 {ECO:0000244|PDB:3UNB}.
STRAND 74 80 {ECO:0000244|PDB:3UNB}.
HELIX 82 103 {ECO:0000244|PDB:3UNB}.
HELIX 109 122 {ECO:0000244|PDB:3UNB}.
STRAND 125 129 {ECO:0000244|PDB:3UNB}.
STRAND 134 140 {ECO:0000244|PDB:3UNB}.
TURN 143 145 {ECO:0000244|PDB:3UNB}.
STRAND 148 152 {ECO:0000244|PDB:3UNB}.
STRAND 158 167 {ECO:0000244|PDB:3UNB}.
HELIX 170 177 {ECO:0000244|PDB:3UNB}.
TURN 182 184 {ECO:0000244|PDB:3UNF}.
HELIX 187 201 {ECO:0000244|PDB:3UNB}.
TURN 204 206 {ECO:0000244|PDB:3UNB}.
STRAND 210 218 {ECO:0000244|PDB:3UNB}.
TURN 219 223 {ECO:0000244|PDB:3UNB}.
HELIX 230 242 {ECO:0000244|PDB:3UNB}.
SEQUENCE 255 AA; 28405 MW; CFB4405E143CEB23 CRC64;
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV
HAYTLYSAVR PFGCSFMLGS YSANDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL
QMKEMTCRDV VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TKGRHEIVPK DIREEAEKYA
KESLKEEDES DDDNM


Related products :

Catalog number Product name Quantity
EIAAB32718 HC9,Homo sapiens,Human,Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,PSC9,PSMA4
EIAAB32711 Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3,Rat,Rattus norvegicus
EIAAB32714 Macropain subunit C8,Mouse,Multicatalytic endopeptidase complex subunit C8,Mus musculus,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3
EIAAB32715 Macropain subunit C9,Mouse,Multicatalytic endopeptidase complex subunit C9,Mus musculus,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4
EIAAB32716 Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4,Rat,Rattus norvegicus
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.05 mg
EIAAB32704 Macropain subunit C2,Mouse,Multicatalytic endopeptidase complex subunit C2,Mus musculus,Proteasome component C2,Proteasome nu chain,Proteasome subunit alpha type-1,Psma1
15-288-22044A Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg
18-003-44182 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.1 mg Protein A
15-288-22044A Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg
18-003-44181 Proteasome subunit alpha type-1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 Pol 0.05 mg Aff Pur
EIAAB32706 Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,Proteasome component C2,Proteasome nu chain,Proteasome subunit alpha type-1,Psma1,Rat,Rattus norvegicus
10-288-22044F Proteasome subunit alpha type 1 - EC 3.4.25.1; Proteasome component C2; Macropain subunit C2; Multicatalytic endopeptidase complex subunit C2; Proteasome nu chain; 30 kDa prosomal protein; PROS-30 0.1 mg
EIAAB32776 Homo sapiens,Human,LMP7,Low molecular mass protein 7,Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit b
EIAAB32735 Macropain subunit C5,Multicatalytic endopeptidase complex subunit C5,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,Psmb1,Rat,Rattus norvegicus
EIAAB32737 Macropain subunit C5,Mouse,Multicatalytic endopeptidase complex subunit C5,Mus musculus,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,Psmb1
EIAAB32738 Homo sapiens,Human,Macropain subunit C5,Multicatalytic endopeptidase complex subunit C5,Proteasome component C5,Proteasome gamma chain,Proteasome subunit beta type-1,PSC5,PSMB1
EIAAB32772 Lmp7,Low molecular mass protein 7,Macropain subunit C13,Mc13,Mouse,Multicatalytic endopeptidase complex subunit C13,Mus musculus,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subu
EIAAB32710 Macropain subunit C3,Multicatalytic endopeptidase complex subunit C3,Proteasome component C3,Proteasome subunit alpha type-2,Psma2,Rat,Rattus norvegicus
EIAAB32707 Lmpc3,Macropain subunit C3,Mouse,Multicatalytic endopeptidase complex subunit C3,Mus musculus,Proteasome component C3,Proteasome subunit alpha type-2,Psma2
EIAAB32708 HC3,Homo sapiens,Human,Macropain subunit C3,Multicatalytic endopeptidase complex subunit C3,Proteasome component C3,Proteasome subunit alpha type-2,PSC3,PSMA2
EIAAB32712 HC8,Homo sapiens,Human,Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,PSC8,PSMA3
EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,Rat,Rattus norvegicus
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa
EIAAB32703 30 kDa prosomal protein,HC2,Homo sapiens,Human,Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,NU,PROS30,PROS-30,Proteasome component C2,Proteasome nu chain,Proteasome subunit alp


 

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