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Follistatin (FS) (Activin-binding protein)

 FST_HUMAN               Reviewed;         344 AA.
P19883; B5BU94; Q9BTH0;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 2.
25-OCT-2017, entry version 176.
RecName: Full=Follistatin;
Short=FS;
AltName: Full=Activin-binding protein;
Flags: Precursor;
Name=FST;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=3380788; DOI=10.1073/pnas.85.12.4218;
Shimasaki S., Koga M., Esch F., Cooksey K., Mercado M., Koba A.,
Ueno N., Ying S.-Y., Ling N., Guillemin R.;
"Primary structure of the human follistatin precursor and its genomic
organization.";
Proc. Natl. Acad. Sci. U.S.A. 85:4218-4222(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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 30-44.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[6]
TISSUE SPECIFICITY.
PubMed=15472207; DOI=10.1210/jc.2004-0162;
Schneyer A.L., Wang Q., Sidis Y., Sluss P.M.;
"Differential distribution of follistatin isoforms: application of a
new FS315-specific immunoassay.";
J. Clin. Endocrinol. Metab. 89:5067-5075(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-317 IN COMPLEX WITH
ACTIVIN A, AND DISULFIDE BONDS.
PubMed=16198295; DOI=10.1016/j.devcel.2005.09.008;
Thompson T.B., Lerch T.F., Cook R.W., Woodruff T.K., Jardetzky T.S.;
"The structure of the follistatin:activin complex reveals antagonism
of both type I and type II receptor binding.";
Dev. Cell 9:535-543(2005).
[8]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 30-344 IN COMPLEX WITH
ACTIVIN A, AND DISULFIDE BONDS.
PubMed=17409095; DOI=10.1074/jbc.M700737200;
Lerch T.F., Shimasaki S., Woodruff T.K., Jardetzky T.S.;
"Structural and biophysical coupling of heparin and activin binding to
follistatin isoform functions.";
J. Biol. Chem. 282:15930-15939(2007).
[9]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 30-317 IN COMPLEX WITH MOUSE
MSTN, AND DISULFIDE BONDS.
PubMed=19644449; DOI=10.1038/emboj.2009.205;
Cash J.N., Rejon C.A., McPherron A.C., Bernard D.J., Thompson T.B.;
"The structure of myostatin:follistatin 288: insights into receptor
utilization and heparin binding.";
EMBO J. 28:2662-2676(2009).
[10] {ECO:0000244|PDB:5JHW}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 299-407 IN COMPLEX WITH
GDF11, AND DISULFIDE BONDS.
PubMed=28257634; DOI=10.1186/s12915-017-0350-1;
Walker R.G., Czepnik M., Goebel E.J., McCoy J.C., Vujic A., Cho M.,
Oh J., Aykul S., Walton K.L., Schang G., Bernard D.J., Hinck A.P.,
Harrison C.A., Martinez-Hackert E., Wagers A.J., Lee R.T.,
Thompson T.B.;
"Structural basis for potency differences between GDF8 and GDF11.";
BMC Biol. 15:19-19(2017).
-!- FUNCTION: Binds directly to activin and functions as an activin
antagonist. Specific inhibitor of the biosynthesis and secretion
of pituitary follicle stimulating hormone (FSH).
-!- SUBUNIT: Monomer. Isoform 2/FS-288 interacts with GDF11
(PubMed:28257634). {ECO:0000269|PubMed:28257634, ECO:0000305}.
-!- INTERACTION:
P03950:ANG; NbExp=3; IntAct=EBI-1571188, EBI-525291;
Q14689:DIP2A; NbExp=2; IntAct=EBI-1571188, EBI-2564275;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=FS315, FS-315;
IsoId=P19883-1; Sequence=Displayed;
Name=2; Synonyms=FS288, FS-288;
IsoId=P19883-2; Sequence=VSP_001565;
-!- TISSUE SPECIFICITY: Isoform 1 is the predominant isoform in serum
but is undetectable in follicular fluid.
{ECO:0000269|PubMed:15472207}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FSTID44477ch5q11.html";
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EMBL; M19481; AAA35851.1; -; Genomic_DNA.
EMBL; M19480; AAA35851.1; JOINED; Genomic_DNA.
EMBL; AB451330; BAG70144.1; -; mRNA.
EMBL; AB451474; BAG70288.1; -; mRNA.
EMBL; CH471123; EAW54880.1; -; Genomic_DNA.
EMBL; BC004107; AAH04107.1; -; mRNA.
CCDS; CCDS3959.1; -. [P19883-1]
CCDS; CCDS43315.1; -. [P19883-2]
PIR; A32141; A32141.
RefSeq; NP_006341.1; NM_006350.3. [P19883-2]
RefSeq; NP_037541.1; NM_013409.2. [P19883-1]
UniGene; Hs.9914; -.
PDB; 2B0U; X-ray; 2.80 A; C/D=30-317.
PDB; 2P6A; X-ray; 3.40 A; C/D=30-344.
PDB; 3HH2; X-ray; 2.15 A; C/D=30-317.
PDB; 5JHW; X-ray; 2.35 A; C/D=30-317.
PDBsum; 2B0U; -.
PDBsum; 2P6A; -.
PDBsum; 3HH2; -.
PDBsum; 5JHW; -.
ProteinModelPortal; P19883; -.
SMR; P19883; -.
BioGrid; 115731; 8.
IntAct; P19883; 13.
MINT; MINT-3009113; -.
STRING; 9606.ENSP00000256759; -.
DrugBank; DB01666; D-Myo-Inositol-Hexasulphate.
MEROPS; I01.966; -.
iPTMnet; P19883; -.
PhosphoSitePlus; P19883; -.
UniCarbKB; P19883; -.
BioMuta; FST; -.
DMDM; 23831079; -.
MaxQB; P19883; -.
PaxDb; P19883; -.
PeptideAtlas; P19883; -.
PRIDE; P19883; -.
DNASU; 10468; -.
Ensembl; ENST00000256759; ENSP00000256759; ENSG00000134363. [P19883-1]
Ensembl; ENST00000396947; ENSP00000380151; ENSG00000134363. [P19883-2]
GeneID; 10468; -.
KEGG; hsa:10468; -.
UCSC; uc003jpc.4; human. [P19883-1]
CTD; 10468; -.
DisGeNET; 10468; -.
EuPathDB; HostDB:ENSG00000134363.11; -.
GeneCards; FST; -.
HGNC; HGNC:3971; FST.
HPA; CAB026025; -.
HPA; HPA018155; -.
MIM; 136470; gene.
neXtProt; NX_P19883; -.
OpenTargets; ENSG00000134363; -.
Orphanet; 3185; Polycystic ovary syndrome.
PharmGKB; PA28388; -.
eggNOG; ENOG410IP0F; Eukaryota.
eggNOG; ENOG410YM8Q; LUCA.
GeneTree; ENSGT00440000033501; -.
HOGENOM; HOG000261649; -.
HOVERGEN; HBG051666; -.
InParanoid; P19883; -.
KO; K04661; -.
OMA; DEAVCAS; -.
OrthoDB; EOG091G09I0; -.
PhylomeDB; P19883; -.
TreeFam; TF106409; -.
Reactome; R-HSA-2473224; Antagonism of Activin by Follistatin.
SIGNOR; P19883; -.
ChiTaRS; FST; human.
EvolutionaryTrace; P19883; -.
GeneWiki; Follistatin; -.
GenomeRNAi; 10468; -.
PRO; PR:P19883; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000134363; -.
CleanEx; HS_FST; -.
ExpressionAtlas; P19883; baseline and differential.
Genevisible; P19883; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0048185; F:activin binding; IPI:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
GO; GO:0004871; F:signal transducer activity; NAS:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB.
GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0051798; P:positive regulation of hair follicle development; IDA:MGI.
InterPro; IPR003645; Fol_N.
InterPro; IPR015369; Follistatin/Osteonectin_EGF.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR017878; TB_dom.
InterPro; IPR036773; TB_dom_sf.
Pfam; PF09289; FOLN; 1.
Pfam; PF07648; Kazal_2; 3.
SMART; SM00274; FOLN; 3.
SMART; SM00280; KAZAL; 3.
SUPFAM; SSF100895; SSF100895; 3.
SUPFAM; SSF57581; SSF57581; 1.
PROSITE; PS51465; KAZAL_2; 3.
PROSITE; PS51364; TB; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 29 {ECO:0000269|PubMed:15340161}.
CHAIN 30 344 Follistatin.
/FTId=PRO_0000010103.
DOMAIN 30 103 TB. {ECO:0000255|PROSITE-
ProRule:PRU00697}.
DOMAIN 94 117 Follistatin-like 1.
DOMAIN 112 166 Kazal-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 167 190 Follistatin-like 2.
DOMAIN 186 241 Kazal-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 244 268 Follistatin-like 3.
DOMAIN 264 318 Kazal-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
COMPBIAS 321 333 Asp/Glu-rich (highly acidic).
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 32 55 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000255|PROSITE-ProRule:PRU00697,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 42 88 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000255|PROSITE-ProRule:PRU00697,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 56 91 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000255|PROSITE-ProRule:PRU00697,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 95 106 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 100 116 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 118 150 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 122 143 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 132 164 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 168 179 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 173 189 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 192 225 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 196 218 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 207 239 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 245 256 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 250 267 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 270 302 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 274 295 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
DISULFID 284 316 {ECO:0000244|PDB:2B0U,
ECO:0000244|PDB:2P6A,
ECO:0000244|PDB:3HH2,
ECO:0000244|PDB:5JHW,
ECO:0000269|PubMed:16198295,
ECO:0000269|PubMed:17409095,
ECO:0000269|PubMed:19644449,
ECO:0000269|PubMed:28257634}.
VAR_SEQ 318 344 Missing (in isoform 2).
{ECO:0000303|PubMed:19054851}.
/FTId=VSP_001565.
VARIANT 152 152 E -> Q (in dbSNP:rs11745088).
/FTId=VAR_049091.
STRAND 31 36 {ECO:0000244|PDB:3HH2}.
STRAND 42 49 {ECO:0000244|PDB:3HH2}.
HELIX 52 55 {ECO:0000244|PDB:3HH2}.
STRAND 64 66 {ECO:0000244|PDB:3HH2}.
HELIX 72 81 {ECO:0000244|PDB:3HH2}.
STRAND 82 87 {ECO:0000244|PDB:3HH2}.
STRAND 89 91 {ECO:0000244|PDB:3HH2}.
STRAND 93 95 {ECO:0000244|PDB:3HH2}.
STRAND 104 108 {ECO:0000244|PDB:3HH2}.
TURN 110 112 {ECO:0000244|PDB:2P6A}.
STRAND 114 118 {ECO:0000244|PDB:3HH2}.
HELIX 123 125 {ECO:0000244|PDB:2B0U}.
STRAND 131 133 {ECO:0000244|PDB:3HH2}.
STRAND 138 141 {ECO:0000244|PDB:3HH2}.
HELIX 142 151 {ECO:0000244|PDB:3HH2}.
STRAND 158 163 {ECO:0000244|PDB:3HH2}.
STRAND 166 168 {ECO:0000244|PDB:3HH2}.
STRAND 178 181 {ECO:0000244|PDB:3HH2}.
STRAND 185 190 {ECO:0000244|PDB:3HH2}.
STRAND 202 204 {ECO:0000244|PDB:2B0U}.
STRAND 206 208 {ECO:0000244|PDB:3HH2}.
STRAND 213 216 {ECO:0000244|PDB:3HH2}.
HELIX 217 227 {ECO:0000244|PDB:3HH2}.
STRAND 233 237 {ECO:0000244|PDB:3HH2}.
HELIX 245 247 {ECO:0000244|PDB:3HH2}.
TURN 251 253 {ECO:0000244|PDB:2P6A}.
STRAND 255 259 {ECO:0000244|PDB:3HH2}.
TURN 260 263 {ECO:0000244|PDB:3HH2}.
STRAND 264 268 {ECO:0000244|PDB:3HH2}.
STRAND 283 285 {ECO:0000244|PDB:3HH2}.
STRAND 290 293 {ECO:0000244|PDB:3HH2}.
HELIX 294 304 {ECO:0000244|PDB:3HH2}.
STRAND 310 314 {ECO:0000244|PDB:3HH2}.
SEQUENCE 344 AA; 38007 MW; D9BB45055D84AC90 CRC64;
MVRARHQPGG LCLLLLLLCQ FMEDRSAQAG NCWLRQAKNG RCQVLYKTEL SKEECCSTGR
LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP
DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGRCKKTCRD VFCPGSSTCV
VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI
KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA
ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW


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E0391b ELISA kit Activin-binding protein,Bos taurus,Bovine,Follistatin,FS,FST 96T
E0391m ELISA Activin-binding protein,Follistatin,FS,Fst,Mouse,Mus musculus 96T
E0391r ELISA Activin-binding protein,Follistatin,FS,Fst,Rat,Rattus norvegicus 96T
RF0043-5 Recombinant Human Follistatin Active; FS288; Activin-binding protein 50ug
E0391h ELISA kit Activin-binding protein,Follistatin,FS,FST,Homo sapiens,Human 96T
RF0043-50 Recombinant Human Follistatin Active; FS288; Activin-binding protein 50ug
E0391h ELISA Activin-binding protein,Follistatin,FS,FST,Homo sapiens,Human 96T
U0391h CLIA Activin-binding protein,Follistatin,FS,FST,Homo sapiens,Human 96T
E0391c ELISA kit Activin-binding protein,Chicken,Follistatin,FS,FST,Gallus gallus 96T
E0391c ELISA Activin-binding protein,Chicken,Follistatin,FS,FST,Gallus gallus 96T
U0391c CLIA Activin-binding protein,Chicken,Follistatin,FS,FST,Gallus gallus 96T
EIAAB40761 Activin receptor-interacting protein 2,Activin receptor-interacting protein 4,Arip2,Mitochondrial outer membrane protein 25,Mouse,Mus musculus,Omp25,Synaptojanin-2-binding protein,Synj2bp
15-288-22131 Follistatin-related protein 1 - Follistatin-like 1 Polyclonal 0.1 mg
15-288-22131 Follistatin-related protein 1 - Follistatin-like 1 Polyclonal 0.05 mg
10-288-22131F Follistatin-related protein 1 - Follistatin-like 1 0.1 mg


 

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