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

Signal transducer and activator of transcription 5A (Mammary gland factor)

 STA5A_MOUSE             Reviewed;         793 AA.
P42230;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 174.
RecName: Full=Signal transducer and activator of transcription 5A;
AltName: Full=Mammary gland factor;
Name=Stat5a; Synonyms=Mgf, Mpf;
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], FUNCTION, AND PHOSPHORYLATION.
STRAIN=C57BL/6 X A/J; TISSUE=Liver;
PubMed=7720707;
Mui A.L.-F., Wakao H., O'Farrell A.-M., Harada N., Miyajima A.;
"Interleukin-3, granulocyte-macrophage colony stimulating factor and
interleukin-5 transduce signals through two STAT5 homologs.";
EMBO J. 14:1166-1175(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=7568026; DOI=10.1073/pnas.92.19.8831;
Liu X., Robinson G.W., Gouilleux F., Groner B., Hennighausen L.;
"Cloning and expression of Stat5 and an additional homologue (Stat5b)
involved in prolactin signal transduction in mouse mammary tissue.";
Proc. Natl. Acad. Sci. U.S.A. 92:8831-8835(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeN; TISSUE=Mammary gland;
Zhou L.X., Moore R.C., Oka T.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[4]
INTERACTION WITH NR3C1.
PubMed=9528750; DOI=10.1128/MCB.18.4.1783;
Cella N., Groner B., Hynes N.E.;
"Characterization of Stat5a and Stat5b homodimers and heterodimers and
their association with the glucocortiocoid receptor in mammary
cells.";
Mol. Cell. Biol. 18:1783-1792(1998).
[5]
FUNCTION, AND INTERACTION WITH ERBB4.
PubMed=10508857; DOI=10.1083/jcb.147.1.77;
Jones F.E., Welte T., Fu X.Y., Stern D.F.;
"ErbB4 signaling in the mammary gland is required for lobuloalveolar
development and Stat5 activation during lactation.";
J. Cell Biol. 147:77-88(1999).
[6]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=11090077;
Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C.,
Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T.,
Kienast J., Kanakura Y., Berdel W.E., Serve H.;
"Flt3 mutations from patients with acute myeloid leukemia induce
transformation of 32D cells mediated by the Ras and STAT5 pathways.";
Blood 96:3907-3914(2000).
[7]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
ERBB4.
PubMed=16837552; DOI=10.1091/mbc.E06-02-0101;
Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L.,
Feng S.M., Elenius K., Earp H.S. III;
"The intracellular domain of ErbB4 induces differentiation of mammary
epithelial cells.";
Mol. Biol. Cell 17:4118-4129(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
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).
[9]
PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
[10]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=21262971; DOI=10.1074/jbc.M110.205021;
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
Muller J.P.;
"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase
FLT3 signaling.";
J. Biol. Chem. 286:10918-10929(2011).
[11]
ISGYLATION.
PubMed=22022510; DOI=10.1371/journal.pone.0026068;
Maragno A.L., Pironin M., Alcalde H., Cong X., Knobeloch K.P.,
Tangy F., Zhang D.E., Ghysdael J., Quang C.T.;
"ISG15 modulates development of the erythroid lineage.";
PLoS ONE 6:E26068-E26068(2011).
[12]
X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 128-712.
PubMed=16192273; DOI=10.1074/jbc.M507682200;
Neculai D., Neculai A.M., Verrier S., Straub K., Klumpp K.,
Pfitzner E., Becker S.;
"Structure of the unphosphorylated STAT5a dimer.";
J. Biol. Chem. 280:40782-40787(2005).
-!- FUNCTION: Carries out a dual function: signal transduction and
activation of transcription. Mediates cellular responses to the
cytokine KITLG/SCF and other growth factors. May mediate cellular
responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the
GAS element and activates PRL-induced transcription. Regulates the
expression of milk proteins during lactation.
{ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:16837552,
ECO:0000269|PubMed:7720707}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member. Interacts with NCOA1 and SOCS7 (By similarity). Binds
NR3C1. Interacts with ERBB4. {ECO:0000250,
ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:16837552,
ECO:0000269|PubMed:9528750}.
-!- INTERACTION:
Q99490-2:AGAP2 (xeno); NbExp=2; IntAct=EBI-617434, EBI-7737644;
P19941:GHR (xeno); NbExp=3; IntAct=EBI-617434, EBI-7526279;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16837552}.
Nucleus {ECO:0000269|PubMed:16837552}. Note=Translocated into the
nucleus in response to phosphorylation.
-!- TISSUE SPECIFICITY: In the virgin, found in most tissues except
brain and muscle. During lactation, abundantly found in mammary
tissue, as well as in other secretory organs such as salivary
gland and seminal vesicle.
-!- PTM: ISGylated. {ECO:0000269|PubMed:22022510}.
-!- PTM: Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3,
IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (PubMed:16837552).
Activated KIT promotes phosphorylation on tyrosine residues and
subsequent translocation to the nucleus (PubMed:21135090).
Tyrosine phosphorylated in response to constitutively activated
FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Tyrosine
phosphorylation is required for DNA-binding activity and
dimerization (PubMed:7720707). Serine phosphorylation is also
required for maximal transcriptional activity (By similarity).
Tyrosine phosphorylated in response to signaling via activated
FLT3; wild-type FLT3 results in much weaker phosphorylation than
constitutively activated mutant FLT3 (PubMed:11090077,
PubMed:21262971). Alternatively, can be phosphorylated by JAK2 at
Tyr-694 (By similarity). {ECO:0000250|UniProtKB:P40763,
ECO:0000250|UniProtKB:P42229, ECO:0000250|UniProtKB:Q62771,
ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:16837552,
ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21262971,
ECO:0000269|PubMed:7720707}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z48538; CAA88419.1; -; mRNA.
EMBL; U21103; AAA80590.1; -; mRNA.
EMBL; U36502; AAA78945.1; -; mRNA.
CCDS; CCDS25439.1; -.
PIR; S54772; S54772.
RefSeq; NP_035618.1; NM_011488.3.
RefSeq; XP_006532784.1; XM_006532721.1.
RefSeq; XP_006532785.1; XM_006532722.1.
RefSeq; XP_017169891.1; XM_017314402.1.
UniGene; Mm.277403; -.
PDB; 1Y1U; X-ray; 3.21 A; A/B/C=128-712.
PDBsum; 1Y1U; -.
ProteinModelPortal; P42230; -.
SMR; P42230; -.
BioGrid; 203525; 13.
CORUM; P42230; -.
DIP; DIP-897N; -.
IntAct; P42230; 7.
MINT; MINT-2576471; -.
STRING; 10090.ENSMUSP00000102980; -.
ChEMBL; CHEMBL5513; -.
iPTMnet; P42230; -.
PhosphoSitePlus; P42230; -.
EPD; P42230; -.
PaxDb; P42230; -.
PeptideAtlas; P42230; -.
PRIDE; P42230; -.
Ensembl; ENSMUST00000004145; ENSMUSP00000004145; ENSMUSG00000004043.
Ensembl; ENSMUST00000107356; ENSMUSP00000102979; ENSMUSG00000004043.
GeneID; 20850; -.
KEGG; mmu:20850; -.
UCSC; uc007lml.2; mouse.
CTD; 6776; -.
MGI; MGI:103036; Stat5a.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOGENOM; HOG000230988; -.
HOVERGEN; HBG107486; -.
InParanoid; P42230; -.
KO; K11223; -.
TreeFam; TF318648; -.
Reactome; R-MMU-1251985; Nuclear signaling by ERBB4.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-2586552; Signaling by Leptin.
Reactome; R-MMU-451927; Interleukin-2 family signaling.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
EvolutionaryTrace; P42230; -.
PRO; PR:P42230; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000004043; -.
ExpressionAtlas; P42230; baseline and differential.
Genevisible; P42230; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0004871; F:signal transducer activity; IGI:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IMP:BHF-UCL.
GO; GO:0000255; P:allantoin metabolic process; IMP:BHF-UCL.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0006101; P:citrate metabolic process; IMP:BHF-UCL.
GO; GO:0006600; P:creatine metabolic process; IMP:BHF-UCL.
GO; GO:0046449; P:creatinine metabolic process; IMP:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:MGI.
GO; GO:0046544; P:development of secondary male sexual characteristics; IMP:MGI.
GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
GO; GO:0006631; P:fatty acid metabolic process; IMP:BHF-UCL.
GO; GO:0007565; P:female pregnancy; IGI:MGI.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0006549; P:isoleucine metabolic process; IMP:BHF-UCL.
GO; GO:0007259; P:JAK-STAT cascade; IDA:MGI.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; IDA:BHF-UCL.
GO; GO:0007595; P:lactation; IMP:MGI.
GO; GO:0019915; P:lipid storage; IGI:MGI.
GO; GO:0001553; P:luteinization; IGI:MGI.
GO; GO:0030879; P:mammary gland development; IMP:MGI.
GO; GO:0061180; P:mammary gland epithelium development; IMP:MGI.
GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IGI:MGI.
GO; GO:0033026; P:negative regulation of mast cell apoptotic process; IMP:MGI.
GO; GO:0006107; P:oxaloacetate metabolic process; IMP:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0048541; P:Peyer's patch development; IGI:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IGI:MGI.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IGI:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; IGI:MGI.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IGI:MGI.
GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IGI:MGI.
GO; GO:0060376; P:positive regulation of mast cell differentiation; IMP:MGI.
GO; GO:0070668; P:positive regulation of mast cell proliferation; IMP:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IGI:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:MGI.
GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IDA:BHF-UCL.
GO; GO:0019218; P:regulation of steroid metabolic process; IGI:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0043434; P:response to peptide hormone; IDA:MGI.
GO; GO:0006105; P:succinate metabolic process; IMP:BHF-UCL.
GO; GO:0033077; P:T cell differentiation in thymus; IGI:MGI.
GO; GO:0043029; P:T cell homeostasis; IGI:MGI.
GO; GO:0019530; P:taurine metabolic process; IMP:BHF-UCL.
GO; GO:0006573; P:valine metabolic process; IMP:BHF-UCL.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR035858; STAT5a/5b.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_sub.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
PANTHER; PTHR11801:SF47; PTHR11801:SF47; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00252; SH2; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Cytoplasm; DNA-binding;
Lactation; Nucleus; Phosphoprotein; Reference proteome; SH2 domain;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 793 Signal transducer and activator of
transcription 5A.
/FTId=PRO_0000182424.
DOMAIN 589 686 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000250|UniProtKB:P42229}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:P42229}.
MOD_RES 682 682 Phosphotyrosine.
{ECO:0000250|UniProtKB:P42229}.
MOD_RES 694 694 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 779 779 Phosphoserine.
{ECO:0000250|UniProtKB:P42229}.
HELIX 144 181 {ECO:0000244|PDB:1Y1U}.
TURN 182 190 {ECO:0000244|PDB:1Y1U}.
TURN 196 198 {ECO:0000244|PDB:1Y1U}.
HELIX 199 249 {ECO:0000244|PDB:1Y1U}.
HELIX 251 262 {ECO:0000244|PDB:1Y1U}.
TURN 263 265 {ECO:0000244|PDB:1Y1U}.
HELIX 273 300 {ECO:0000244|PDB:1Y1U}.
HELIX 309 330 {ECO:0000244|PDB:1Y1U}.
STRAND 332 336 {ECO:0000244|PDB:1Y1U}.
STRAND 340 345 {ECO:0000244|PDB:1Y1U}.
STRAND 348 355 {ECO:0000244|PDB:1Y1U}.
TURN 356 361 {ECO:0000244|PDB:1Y1U}.
STRAND 368 375 {ECO:0000244|PDB:1Y1U}.
HELIX 376 383 {ECO:0000244|PDB:1Y1U}.
STRAND 404 406 {ECO:0000244|PDB:1Y1U}.
TURN 407 410 {ECO:0000244|PDB:1Y1U}.
STRAND 411 413 {ECO:0000244|PDB:1Y1U}.
STRAND 415 419 {ECO:0000244|PDB:1Y1U}.
HELIX 435 437 {ECO:0000244|PDB:1Y1U}.
STRAND 439 449 {ECO:0000244|PDB:1Y1U}.
STRAND 451 454 {ECO:0000244|PDB:1Y1U}.
STRAND 456 462 {ECO:0000244|PDB:1Y1U}.
STRAND 466 469 {ECO:0000244|PDB:1Y1U}.
HELIX 475 488 {ECO:0000244|PDB:1Y1U}.
STRAND 500 503 {ECO:0000244|PDB:1Y1U}.
HELIX 504 519 {ECO:0000244|PDB:1Y1U}.
HELIX 527 538 {ECO:0000244|PDB:1Y1U}.
HELIX 545 550 {ECO:0000244|PDB:1Y1U}.
STRAND 552 554 {ECO:0000244|PDB:1Y1U}.
HELIX 555 559 {ECO:0000244|PDB:1Y1U}.
STRAND 566 569 {ECO:0000244|PDB:1Y1U}.
HELIX 570 584 {ECO:0000244|PDB:1Y1U}.
HELIX 586 591 {ECO:0000244|PDB:1Y1U}.
HELIX 600 608 {ECO:0000244|PDB:1Y1U}.
STRAND 615 620 {ECO:0000244|PDB:1Y1U}.
STRAND 626 631 {ECO:0000244|PDB:1Y1U}.
STRAND 641 646 {ECO:0000244|PDB:1Y1U}.
HELIX 648 653 {ECO:0000244|PDB:1Y1U}.
HELIX 656 662 {ECO:0000244|PDB:1Y1U}.
HELIX 675 679 {ECO:0000244|PDB:1Y1U}.
TURN 680 682 {ECO:0000244|PDB:1Y1U}.
SEQUENCE 793 AA; 90831 MW; 7C66E435C37624DD CRC64;
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRGQATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
REANNCSSPA GVLVDAMSQK HLQINQRFEE LRLITQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLG QLNPQERMSR ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI
SSNHLEDYNS MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD FSIRSLADRL
GDLNYLIYVF PDRPKDEVFA KYYTPVLAKA VDGYVKPQIK QVVPEFVNAS TDAGASATYM
DQAPSPVVCP QPHYNMYPPN PDPVLDQDGE FDLDESMDVA RHVEELLRRP MDSLDARLSP
PAGLFTSARS SLS


Related products :

Catalog number Product name Quantity
E1738b ELISA kit Bos taurus,Bovine,Mammary gland factor,MGF,Signal transducer and activator of transcription 5A,STAT5A 96T
E1738m ELISA kit Mammary gland factor,Mgf,Mouse,Mpf,Mus musculus,Signal transducer and activator of transcription 5A,Stat5a 96T
U1738m CLIA Mammary gland factor,Mgf,Mouse,Mpf,Mus musculus,Signal transducer and activator of transcription 5A,Stat5a 96T
U1738r CLIA Mammary gland factor,Mgf,Rat,Rattus norvegicus,Signal transducer and activator of transcription 5A,Stat5a 96T
E1738r ELISA Mammary gland factor,Mgf,Rat,Rattus norvegicus,Signal transducer and activator of transcription 5A,Stat5a 96T
E1738m ELISA Mammary gland factor,Mgf,Mouse,Mpf,Mus musculus,Signal transducer and activator of transcription 5A,Stat5a 96T
U1738b CLIA Bos taurus,Bovine,Mammary gland factor,MGF,Signal transducer and activator of transcription 5A,STAT5A 96T
E1738b ELISA Bos taurus,Bovine,Mammary gland factor,MGF,Signal transducer and activator of transcription 5A,STAT5A 96T
E1738r ELISA kit Mammary gland factor,Mgf,Rat,Rattus norvegicus,Signal transducer and activator of transcription 5A,Stat5a 96T
15-288-22780 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
15-288-22780 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg
18-003-43847 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
15-288-22758 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
15-288-22758 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg
18-003-44098 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
18-003-43498 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.05 mg Aff Pur
18-661-15004 Signal transducer and activator of transcription 1-alpha_beta - Transcription factor ISGF-3 components p91_p84 Polyclonal 0.1 mg
E1740h ELISA kit Homo sapiens,Human,Signal transducer and activator of transcription 1-alpha_beta,STAT1,Transcription factor ISGF-3 components p91_p84 96T
U1740h CLIA Homo sapiens,Human,Signal transducer and activator of transcription 1-alpha_beta,STAT1,Transcription factor ISGF-3 components p91_p84 96T
E1740h ELISA Homo sapiens,Human,Signal transducer and activator of transcription 1-alpha_beta,STAT1,Transcription factor ISGF-3 components p91_p84 96T
60044 IgG,signal transducer and activator of transcription 3 (acute_phase response factor) 0.1 mg
10-782-55123 Signal transducer and activator of transcription 3 - Acute-phase response factor N_A 0.2 mg
10-782-55123 Signal transducer and activator of transcription 3 - Acute-phase response factor N_A 0.05 mg
15-288-22759 Signal transducer and activator of transcription 3 - Acute-phase response factor Polyclonal 0.1 mg
15-288-22759 Signal transducer and activator of transcription 3 - Acute-phase response factor Polyclonal 0.05 mg


 

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