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

Thioredoxin domain-containing protein 5 (Endoplasmic reticulum resident protein 46) (ER protein 46) (ERp46) (Thioredoxin-like protein p46)

 TXND5_HUMAN             Reviewed;         432 AA.
Q8NBS9; B2RDM2; Q5TCQ0; Q8ND33; Q8TCT2; Q9BVH9;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
11-APR-2003, sequence version 2.
12-SEP-2018, entry version 168.
RecName: Full=Thioredoxin domain-containing protein 5;
AltName: Full=Endoplasmic reticulum resident protein 46;
Short=ER protein 46;
Short=ERp46;
AltName: Full=Thioredoxin-like protein p46;
Flags: Precursor;
Name=TXNDC5; Synonyms=TLP46; ORFNames=UNQ364/PRO700;
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] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung;
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).
[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 GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 70-432 (ISOFORM 1).
TISSUE=Liver;
Lo S.L., Nissom P.M., Ong S.E., Choong M.L., Ng S.S., Lim J.W.E.,
Liang R.C.M.Y., Ou K., Seow T.K., Chung M.C.M.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-432 (ISOFORM 1).
TISSUE=Eye;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-432 (ISOFORMS 1/2).
TISSUE=Lymph node;
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
STRUCTURE BY NMR OF 322-432.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the third thioredoxin domain of human
thioredoxin domain-containing protein 5.";
Submitted (SEP-2006) to the PDB data bank.
-!- FUNCTION: Possesses thioredoxin activity. Has been shown to reduce
insulin disulfide bonds. Also complements protein disulfide-
isomerase deficiency in yeast (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q13162:PRDX4; NbExp=2; IntAct=EBI-2510815, EBI-2211957;
O08807:Prdx4 (xeno); NbExp=2; IntAct=EBI-16091651, EBI-494652;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8NBS9-1; Sequence=Displayed;
Name=2;
IsoId=Q8NBS9-2; Sequence=VSP_045181;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH01199.1; Type=Erroneous initiation; 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; AY358646; AAQ89009.1; -; mRNA.
EMBL; AK075291; BAC11526.1; -; mRNA.
EMBL; AK315598; BAG37969.1; -; mRNA.
EMBL; AL023694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL096800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471087; EAW55221.1; -; Genomic_DNA.
EMBL; AJ440721; CAD29430.1; -; mRNA.
EMBL; BC001199; AAH01199.1; ALT_INIT; mRNA.
EMBL; AL834423; CAD39084.1; -; mRNA.
CCDS; CCDS4505.1; -. [Q8NBS9-1]
CCDS; CCDS47369.1; -. [Q8NBS9-2]
RefSeq; NP_001139021.1; NM_001145549.3. [Q8NBS9-2]
RefSeq; NP_110437.2; NM_030810.4. [Q8NBS9-1]
UniGene; Hs.150837; -.
UniGene; Hs.635352; -.
PDB; 2DIZ; NMR; -; A=323-432.
PDB; 3UJ1; X-ray; 2.65 A; A=323-432.
PDB; 3UVT; X-ray; 2.00 A; A/B/C/D/E=323-428.
PDB; 3WGD; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I=62-170.
PDB; 3WGE; X-ray; 0.95 A; A=190-298.
PDB; 3WGX; X-ray; 0.92 A; A/B=190-298.
PDBsum; 2DIZ; -.
PDBsum; 3UJ1; -.
PDBsum; 3UVT; -.
PDBsum; 3WGD; -.
PDBsum; 3WGE; -.
PDBsum; 3WGX; -.
ProteinModelPortal; Q8NBS9; -.
SMR; Q8NBS9; -.
BioGrid; 123529; 80.
DIP; DIP-53700N; -.
IntAct; Q8NBS9; 22.
MINT; Q8NBS9; -.
STRING; 9606.ENSP00000369081; -.
iPTMnet; Q8NBS9; -.
PhosphoSitePlus; Q8NBS9; -.
SwissPalm; Q8NBS9; -.
BioMuta; TXNDC5; -.
DMDM; 29839560; -.
EPD; Q8NBS9; -.
MaxQB; Q8NBS9; -.
PaxDb; Q8NBS9; -.
PeptideAtlas; Q8NBS9; -.
PRIDE; Q8NBS9; -.
ProteomicsDB; 72817; -.
Ensembl; ENST00000379757; ENSP00000369081; ENSG00000239264. [Q8NBS9-1]
Ensembl; ENST00000473453; ENSP00000420784; ENSG00000239264. [Q8NBS9-2]
GeneID; 81567; -.
KEGG; hsa:81567; -.
UCSC; uc003mxv.4; human. [Q8NBS9-1]
CTD; 81567; -.
DisGeNET; 81567; -.
EuPathDB; HostDB:ENSG00000239264.8; -.
GeneCards; TXNDC5; -.
HGNC; HGNC:21073; TXNDC5.
HPA; HPA034677; -.
HPA; HPA034678; -.
MIM; 616412; gene.
neXtProt; NX_Q8NBS9; -.
OpenTargets; ENSG00000239264; -.
PharmGKB; PA134992492; -.
eggNOG; KOG0191; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133723; -.
HOGENOM; HOG000007899; -.
HOVERGEN; HBG058611; -.
InParanoid; Q8NBS9; -.
KO; K13984; -.
OMA; HVSSGNH; -.
OrthoDB; EOG091G08PT; -.
PhylomeDB; Q8NBS9; -.
TreeFam; TF106379; -.
BRENDA; 5.3.4.1; 2681.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; TXNDC5; human.
EvolutionaryTrace; Q8NBS9; -.
GeneWiki; TXNDC5; -.
GenomeRNAi; 81567; -.
PRO; PR:Q8NBS9; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000239264; Expressed in 93 organ(s), highest expression level in lymph node.
CleanEx; HS_TXNDC5; -.
ExpressionAtlas; Q8NBS9; baseline and differential.
Genevisible; Q8NBS9; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
GO; GO:0043277; P:apoptotic cell clearance; IBA:GO_Central.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 3.
SUPFAM; SSF52833; SSF52833; 3.
TIGRFAMs; TIGR01126; pdi_dom; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 3.
PROSITE; PS51352; THIOREDOXIN_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Redox-active center; Reference proteome;
Repeat; Signal.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 432 Thioredoxin domain-containing protein 5.
/FTId=PRO_0000034183.
DOMAIN 36 169 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 170 295 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 304 429 Thioredoxin 3. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 429 432 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
DISULFID 89 92 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 217 220 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DISULFID 350 353 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 1 108 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045181.
CONFLICT 354 354 K -> R (in Ref. 2; BAC11526).
{ECO:0000305}.
HELIX 68 77 {ECO:0000244|PDB:3WGD}.
STRAND 78 85 {ECO:0000244|PDB:3WGD}.
HELIX 90 106 {ECO:0000244|PDB:3WGD}.
STRAND 113 120 {ECO:0000244|PDB:3WGD}.
TURN 121 123 {ECO:0000244|PDB:3WGD}.
HELIX 125 130 {ECO:0000244|PDB:3WGD}.
STRAND 135 142 {ECO:0000244|PDB:3WGD}.
STRAND 149 151 {ECO:0000244|PDB:3WGD}.
HELIX 157 168 {ECO:0000244|PDB:3WGD}.
STRAND 191 194 {ECO:0000244|PDB:3WGX}.
TURN 196 198 {ECO:0000244|PDB:3WGX}.
HELIX 199 203 {ECO:0000244|PDB:3WGX}.
STRAND 204 213 {ECO:0000244|PDB:3WGX}.
HELIX 218 233 {ECO:0000244|PDB:3WGX}.
TURN 234 236 {ECO:0000244|PDB:3WGX}.
STRAND 238 246 {ECO:0000244|PDB:3WGX}.
TURN 247 249 {ECO:0000244|PDB:3WGX}.
HELIX 251 256 {ECO:0000244|PDB:3WGX}.
STRAND 261 269 {ECO:0000244|PDB:3WGX}.
STRAND 272 276 {ECO:0000244|PDB:3WGX}.
HELIX 283 294 {ECO:0000244|PDB:3WGX}.
STRAND 324 326 {ECO:0000244|PDB:3UVT}.
TURN 329 331 {ECO:0000244|PDB:3UVT}.
HELIX 332 336 {ECO:0000244|PDB:3UVT}.
STRAND 337 346 {ECO:0000244|PDB:3UVT}.
HELIX 351 364 {ECO:0000244|PDB:3UVT}.
STRAND 374 380 {ECO:0000244|PDB:3UVT}.
TURN 381 383 {ECO:0000244|PDB:3UVT}.
HELIX 385 390 {ECO:0000244|PDB:3UVT}.
STRAND 395 403 {ECO:0000244|PDB:3UVT}.
STRAND 406 411 {ECO:0000244|PDB:3UVT}.
HELIX 417 427 {ECO:0000244|PDB:3UVT}.
SEQUENCE 432 AA; 47629 MW; 85E398008D6DB98C CRC64;
MPARPGRLLP LLARPAALTA LLLLLLGHGG GGRWGARAQE AAAAAADGPP AADGEDGQDP
HSKHLYTADM FTHGIQSAAH FVMFFAPWCG HCQRLQPTWN DLGDKYNSME DAKVYVAKVD
CTAHSDVCSA QGVRGYPTLK LFKPGQEAVK YQGPRDFQTL ENWMLQTLNE EPVTPEPEVE
PPSAPELKQG LYELSASNFE LHVAQGDHFI KFFAPWCGHC KALAPTWEQL ALGLEHSETV
KIGKVDCTQH YELCSGNQVR GYPTLLWFRD GKKVDQYKGK RDLESLREYV ESQLQRTETG
ATETVTPSEA PVLAAEPEAD KGTVLALTEN NFDDTIAEGI TFIKFYAPWC GHCKTLAPTW
EELSKKEFPG LAGVKIAEVD CTAERNICSK YSVRGYPTLL LFRGGKKVSE HSGGRDLDSL
HRFVLSQAKD EL


Related products :

Catalog number Product name Quantity
EIAAB44637 Endoplasmic reticulum resident protein 46,ER protein 46,ERp46,Mouse,Mus musculus,PC-TRP,Plasma cell-specific thioredoxin-related protein,Thioredoxin domain-containing protein 5,Thioredoxin-like protei
EIAAB44636 Endoplasmic reticulum resident protein 46,ER protein 46,ERp46,Homo sapiens,Human,Thioredoxin domain-containing protein 5,Thioredoxin-like protein p46,TLP46,TXNDC5,UNQ364_PRO700
EIAAB44606 Endoplasmic reticulum resident protein 18,Endoplasmic reticulum resident protein 19,ER protein 18,ER protein 19,ERp18,ERp19,Homo sapiens,hTLP19,Human,Thioredoxin domain-containing protein 12,Thioredox
EIAAB44604 Endoplasmic reticulum resident protein 19,ER protein 19,ERp19,Mouse,Mus musculus,Thioredoxin domain-containing protein 12,Thioredoxin-like protein p19,Tlp19,Txndc12
EIAAB13278 Endoplasmic reticulum resident protein 44,ER protein 44,ERp44,Erp44,Kiaa0573,Mouse,Mus musculus,Thioredoxin domain-containing protein 4,Txndc4
EIAAB13277 Endoplasmic reticulum resident protein 44,ER protein 44,ERp44,ERP44,Homo sapiens,Human,KIAA0573,Thioredoxin domain-containing protein 4,TXNDC4,UNQ532_PRO1075
EIAAB13279 Bos taurus,Bovine,Endoplasmic reticulum resident protein 44,ER protein 44,ERp44,ERP44,Thioredoxin domain-containing protein 4,TXNDC4
E1497h ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
E1497r ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
U1497r CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
U1497h CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
U1497m CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 6 96T
E1497m ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER protein 96T
E1497b ELISA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER prot 96T
U1497b CLIA 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER prote 96T
E1497b ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Bos taurus,Bovine,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER 96T
E1497h ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
E1497m ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
E1497r ELISA kit 58 kDa glucose-regulated protein,58 kDa microsomal protein,Disulfide isomerase ER-60,Endoplasmic reticulum resident protein 57,Endoplasmic reticulum resident protein 60,ER protein 57,ER pro 96T
EIAAB13274 C12orf8,Endoplasmic reticulum resident protein 28,Endoplasmic reticulum resident protein 29,Endoplasmic reticulum resident protein 31,ERp28,ERP28,ERp29,ERP29,ERp31,Homo sapiens,Human
EIAAB30362 CaBP2,Cabp2,Calcium-binding protein 2,Endoplasmic reticulum resident protein 70,Endoplasmic reticulum resident protein 72,ER protein 70,ER protein 72,ERp70,Erp70,ERp72,ERp-72,Pdia4,Protein disulfide-i
EIAAB30361 Endoplasmic reticulum resident protein 70,Endoplasmic reticulum resident protein 72,ER protein 70,ER protein 72,ERp70,ERP70,ERp72,ERP72,ERp-72,Homo sapiens,Human,PDIA4,Protein disulfide-isomerase A4
EIAAB44613 14 kDa thioredoxin-related protein,Homo sapiens,Human,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,TXNDC17,TXNL5
EIAAB44614 14 kDa thioredoxin-related protein,Mouse,Mus musculus,Protein 42-9-9,Thioredoxin domain-containing protein 17,Thioredoxin-like protein 5,TRP14,Txndc17,Txnl5
EIAAB30369 Endoplasmic reticulum protein 5,ER protein 5,ERp5,ERP5,Homo sapiens,Human,P5,PDIA6,Protein disulfide isomerase P5,Protein disulfide-isomerase A6,Thioredoxin domain-containing protein 7,TXNDC7


 

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