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Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit X)

 PSB5_MOUSE              Reviewed;         264 AA.
O55234; Q3UZI1; Q91X53; Q9CWR4; Q9R1P2;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 3.
23-MAY-2018, entry version 157.
RecName: Full=Proteasome subunit beta type-5;
EC=3.4.25.1 {ECO:0000250|UniProtKB:P28074};
AltName: Full=Macropain epsilon chain;
AltName: Full=Multicatalytic endopeptidase complex epsilon chain;
AltName: Full=Proteasome chain 6;
AltName: Full=Proteasome epsilon chain;
AltName: Full=Proteasome subunit X;
Flags: Precursor;
Name=Psmb5;
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 [GENOMIC DNA / MRNA].
STRAIN=129/SvJ, and C57BL/6J;
PubMed=9382924; DOI=10.1007/s002510050329;
Kohda K., Matsuda Y., Ishibashi T., Tanaka K., Kasahara M.;
"Structural analysis and chromosomal localization of the mouse Psmb5
gene coding for the constitutively expressed beta-type proteasome
subunit.";
Immunogenetics 47:77-87(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=B10.A; TISSUE=Macrophage;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic stem cell;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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]
PROTEIN SEQUENCE OF 79-91; 141-150 AND 167-179, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
INDUCTION BY ANTIOXIDANTS.
PubMed=14612418; DOI=10.1128/MCB.23.23.8786-8794.2003;
Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., Kensler T.W.;
"Antioxidants enhance mammalian proteasome expression through the
Keap1-Nrf2 signaling pathway.";
Mol. Cell. Biol. 23:8786-8794(2003).
[7]
INDUCTION BY ANTIOXIDANTS.
PubMed=16723119; DOI=10.1016/j.bbrc.2006.05.043;
Kwak M.K., Kensler T.W.;
"Induction of 26S proteasome subunit PSMB5 by the bifunctional inducer
3-methylcholanthrene through the Nrf2-ARE, but not the AhR/Arnt-XRE,
pathway.";
Biochem. Biophys. Res. Commun. 345:1350-1357(2006).
[8]
TISSUE SPECIFICITY.
PubMed=16434403; DOI=10.1074/jbc.M511512200;
Ma X.H., Hu S.J., Ni H., Zhao Y.C., Tian Z., Liu J.L., Ren G.,
Liang X.H., Yu H., Wan P., Yang Z.M.;
"Serial analysis of gene expression in mouse uterus at the
implantation site.";
J. Biol. Chem. 281:9351-9360(2006).
[9]
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).
[10]
INDUCTION BY DITHIOLETHIONE.
PubMed=17521679; DOI=10.1016/j.lfs.2007.04.014;
Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.;
"Tissue specific increase of the catalytic subunits of the 26S
proteasome by indirect antioxidant dithiolethione in mice: enhanced
activity for degradation of abnormal protein.";
Life Sci. 80:2411-2420(2007).
[11]
INDUCTION BY LITHIUM.
PubMed=18349697; DOI=10.1097/YPG.0b013e3282fb0051;
Chetcuti A., Adams L.J., Mitchell P.B., Schofield P.R.;
"Microarray gene expression profiling of mouse brain mRNA in a model
of lithium treatment.";
Psychiatr. Genet. 18:64-72(2008).
[12]
FUNCTION.
PubMed=19183883; DOI=10.1007/s12272-009-1124-2;
Park H.M., Kim J.A., Kwak M.K.;
"Protection against amyloid beta cytotoxicity by sulforaphane: role of
the proteasome.";
Arch. Pharm. Res. 32:109-115(2009).
[13]
IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
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).
[14]
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).
[15]
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). Within the 20S core complex, PSMB5 displays a
chymotrypsin-like activity. {ECO:0000269|PubMed:16581775,
ECO:0000269|PubMed:19183883, ECO:0000269|PubMed:22341445}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000250|UniProtKB:P28074}.
-!- 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). Directly interacts with POMP (By similarity).
Interacts with ABCB1 and TAP1 (By similarity).
{ECO:0000250|UniProtKB:P28074, ECO:0000269|PubMed:16857966,
ECO:0000269|PubMed:22341445}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28074}.
Nucleus {ECO:0000250|UniProtKB:P28074}.
-!- TISSUE SPECIFICITY: Expressed in uterus at the embryo implantation
site. {ECO:0000269|PubMed:16434403, ECO:0000269|PubMed:22341445}.
-!- INDUCTION: Up-regulated in embryonic fibroblasts and neuroblastoma
cells by antioxidants through the Nrf2-ARE pathway (at protein
level). Up-regulated by the antioxidant dithiolethione (D3T) in
liver, small intestine and brain (at protein level). Down-
regulated under lithium treatment. {ECO:0000269|PubMed:14612418,
ECO:0000269|PubMed:16723119, ECO:0000269|PubMed:17521679,
ECO:0000269|PubMed:18349697}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; AB003304; BAA24916.1; -; mRNA.
EMBL; AB003306; BAA24917.1; -; Genomic_DNA.
EMBL; AF060091; AAD50536.1; -; mRNA.
EMBL; AK010441; BAB26942.1; -; mRNA.
EMBL; AK133839; BAE21876.1; -; mRNA.
EMBL; BC012246; AAH12246.1; -; mRNA.
EMBL; BC106144; AAI06145.1; -; mRNA.
CCDS; CCDS27095.1; -.
RefSeq; NP_035316.1; NM_011186.1.
UniGene; Mm.8911; -.
PDB; 3UNB; X-ray; 2.90 A; 1/K/Y/m=60-264.
PDB; 3UNE; X-ray; 3.20 A; 1/K/Y/m=60-264.
PDBsum; 3UNB; -.
PDBsum; 3UNE; -.
ProteinModelPortal; O55234; -.
SMR; O55234; -.
BioGrid; 202421; 69.
CORUM; O55234; -.
IntAct; O55234; 69.
MINT; O55234; -.
STRING; 10090.ENSMUSP00000022803; -.
ChEMBL; CHEMBL1944494; -.
MEROPS; T01.012; -.
iPTMnet; O55234; -.
PhosphoSitePlus; O55234; -.
SwissPalm; O55234; -.
EPD; O55234; -.
MaxQB; O55234; -.
PaxDb; O55234; -.
PeptideAtlas; O55234; -.
PRIDE; O55234; -.
Ensembl; ENSMUST00000022803; ENSMUSP00000022803; ENSMUSG00000022193.
GeneID; 19173; -.
KEGG; mmu:19173; -.
UCSC; uc007twl.1; mouse.
CTD; 5693; -.
MGI; MGI:1194513; Psmb5.
eggNOG; KOG0175; Eukaryota.
eggNOG; ENOG410XQRP; LUCA.
GeneTree; ENSGT00510000046395; -.
HOGENOM; HOG000091082; -.
HOVERGEN; HBG108297; -.
InParanoid; O55234; -.
KO; K02737; -.
OMA; TMCAGVT; -.
OrthoDB; EOG091G0BPS; -.
PhylomeDB; O55234; -.
TreeFam; TF106223; -.
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-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-9020702; Interleukin-1 signaling.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:O55234; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022193; -.
ExpressionAtlas; O55234; baseline and differential.
Genevisible; O55234; MM.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; 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:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR037558; Proteasome_beta_5.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF51; PTHR11599:SF51; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
Threonine protease; Zymogen.
PROPEP 1 59 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000026591.
CHAIN 60 264 Proteasome subunit beta type-5.
/FTId=PRO_0000026592.
ACT_SITE 60 60 Nucleophile.
{ECO:0000250|UniProtKB:P28074}.
BINDING 108 108 Bortezomib; via amide nitrogen.
{ECO:0000250}.
CONFLICT 110 110 D -> N (in Ref. 3; BAB26942).
{ECO:0000305}.
CONFLICT 248 248 S -> N (in Ref. 4; AAH12246).
{ECO:0000305}.
STRAND 61 67 {ECO:0000244|PDB:3UNB}.
STRAND 70 75 {ECO:0000244|PDB:3UNB}.
STRAND 79 81 {ECO:0000244|PDB:3UNB}.
STRAND 84 88 {ECO:0000244|PDB:3UNB}.
STRAND 93 97 {ECO:0000244|PDB:3UNB}.
STRAND 100 103 {ECO:0000244|PDB:3UNB}.
HELIX 108 129 {ECO:0000244|PDB:3UNB}.
HELIX 135 147 {ECO:0000244|PDB:3UNB}.
TURN 148 153 {ECO:0000244|PDB:3UNB}.
STRAND 156 164 {ECO:0000244|PDB:3UNB}.
STRAND 167 174 {ECO:0000244|PDB:3UNB}.
STRAND 179 181 {ECO:0000244|PDB:3UNB}.
STRAND 183 188 {ECO:0000244|PDB:3UNB}.
HELIX 191 200 {ECO:0000244|PDB:3UNB}.
HELIX 208 225 {ECO:0000244|PDB:3UNB}.
STRAND 226 228 {ECO:0000244|PDB:3UNE}.
STRAND 231 239 {ECO:0000244|PDB:3UNB}.
STRAND 242 250 {ECO:0000244|PDB:3UNB}.
HELIX 251 258 {ECO:0000244|PDB:3UNB}.
SEQUENCE 264 AA; 28532 MW; FCCD619734EF3C57 CRC64;
MALASVLQRP MPVNQHGFFG LGGGADLLDL GPGSPGDGLS LAAPSWGVPE EPRIEMLHGT
TTLAFKFLHG VIVAADSRAT AGAYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR
QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI
SGTAFSVGSG SVYAYGVMDR GYSYDLKVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE
DGWIRVSSDN VADLHDKYSS VSVP


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E1177h ELISA kit Homo sapiens,Human,LMP2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta 96T
E1177h ELISA Homo sapiens,Human,LMP2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,P 96T
U1177r CLIA Lmp2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,Psmb9,Rat,Rattus norv 96T
U1177h CLIA Homo sapiens,Human,LMP2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,PS 96T
E1177r ELISA kit Lmp2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,Psmb9,Rat,Rattu 96T
E1177r ELISA Lmp2,Low molecular mass protein 2,Macropain chain 7,Multicatalytic endopeptidase complex chain 7,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit beta-1i,Psmb9,Rat,Rattus nor 96T
EIAAB32753 Lmp3,Low molecular mass protein 3,Macropain beta chain,Mouse,Multicatalytic endopeptidase complex beta chain,Mus musculus,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,Psmb4
15-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 Polyclonal 0.1 mg
EIAAB32757 Macropain beta chain,Multicatalytic endopeptidase complex beta chain,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,Psmb4,Rat,Rattus norvegicus,RN3
15-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 Polyclonal 0.05 mg
10-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 0.1 mg
EIAAB32755 Macropain beta chain,Multicatalytic endopeptidase complex beta chain,Pig,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,PSMB4,Sus scrofa
10-288-22554F Proteasome subunit beta type 4 - EC 3.4.25.1; Proteasome beta chain; Macropain beta chain; Multicatalytic endopeptidase complex beta chain; Proteasome chain 3; HSN3; HsBPROS26 0.05 mg
EIAAB32760 Chicken,Gallus gallus,Macropain chain 1,Multicatalytic endopeptidase complex chain 1,Proteasome chain 1,Proteasome subunit beta type-5,Proteasome subunit C1,PSMB5
EIAAB32765 Lmp19,Low molecular mass protein 19,Macropain delta chain,Mouse,Multicatalytic endopeptidase complex delta chain,Mus musculus,Proteasome delta chain,Proteasome subunit beta type-6,Proteasome subunit Y
EIAAB32764 Homo sapiens,Human,LMPY,Macropain delta chain,Multicatalytic endopeptidase complex delta chain,Proteasome delta chain,Proteasome subunit beta type-6,Proteasome subunit Y,PSMB6,Y
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


 

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