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Insulin-like growth factor-binding protein 4 (IBP-4) (IGF-binding protein 4) (IGFBP-4)

 IBP4_HUMAN              Reviewed;         258 AA.
P22692; A0N9W2; B4E351; Q5U012; Q9UCL6;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 2.
30-AUG-2017, entry version 177.
RecName: Full=Insulin-like growth factor-binding protein 4;
Short=IBP-4;
Short=IGF-binding protein 4;
Short=IGFBP-4;
Flags: Precursor;
Name=IGFBP4; Synonyms=IBP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=1704481; DOI=10.1210/mend-4-10-1451;
Shimasaki S., Uchiyama F., Shimonaka M., Ling N.;
"Molecular cloning of the cDNAs encoding a novel insulin-like growth
factor-binding protein from rat and human.";
Mol. Endocrinol. 4:1451-1458(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1707125; DOI=10.1210/mend-4-12-1806;
Latour D., Mohan S., Linkhart T.A., Baylink D.J., Strong D.D.;
"Inhibitory insulin-like growth factor-binding protein: cloning,
complete sequence, and physiological regulation.";
Mol. Endocrinol. 4:1806-1814(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 22-41.
TISSUE=Osteosarcoma;
PubMed=1709161;
Kiefer M.C., Masiarz F.R., Bauer D.M., Zapf J.;
"Identification and molecular cloning of two new 30-kDa insulin-like
growth factor binding proteins isolated from adult human serum.";
J. Biol. Chem. 266:9043-9049(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=9048882; DOI=10.1016/S0167-4781(96)00220-5;
Qin X., Morales S., Lee K.-W., Boonyaratanakornkit V., Baylink D.J.,
Mohan S., Strong D.D.;
"Structural and functional analysis of the 5'-flanking region of the
human insulin-like growth factor binding protein (IGFBP)-4 gene.";
Biochim. Biophys. Acta 1350:136-140(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9615225; DOI=10.1006/geno.1998.5283;
Zazzi H., Nikoshkov A., Hall K., Luthman H.;
"Structure and transcription regulation of the human insulin-like
growth factor binding protein 4 gene (IGFBP4).";
Genomics 49:401-410(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[10]
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[12]
PROTEIN SEQUENCE OF 22-53.
TISSUE=Colon;
PubMed=1709585;
Culouscou J.-M., Shoyab M.;
"Purification of a colon cancer cell growth inhibitor and its
identification as an insulin-like growth factor binding protein.";
Cancer Res. 51:2813-2819(1991).
[13]
PROTEIN SEQUENCE OF 22-42, AND INDUCTION.
TISSUE=Osteosarcoma;
PubMed=1726835;
Mohan S., Baylink D.J.;
"Evidence that the inhibition of TE85 human bone cell proliferation by
agents which stimulate cAMP production may in part be mediated by
changes in the IGF-II regulatory system.";
Growth Regul. 1:110-118(1991).
[14]
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).
[15]
PHOSPHORYLATION AT SER-255.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[16]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 24-103 IN COMPLEX WITH IGF1,
AND DISULFIDE BONDS.
PubMed=15642270; DOI=10.1016/j.str.2004.11.009;
Siwanowicz I., Popowicz G.M., Wisniewska M., Huber R., Kuenkele K.-P.,
Lang K., Engh R.A., Holak T.A.;
"Structural basis for the regulation of insulin-like growth factors by
IGF binding proteins.";
Structure 13:155-167(2005).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-253 IN COMPLEX WITH IGF1,
AND DISULFIDE BONDS.
PubMed=16924115; DOI=10.1073/pnas.0605652103;
Sitar T., Popowicz G.M., Siwanowicz I., Huber R., Holak T.A.;
"Structural basis for the inhibition of insulin-like growth factors by
insulin-like growth factor-binding proteins.";
Proc. Natl. Acad. Sci. U.S.A. 103:13028-13033(2006).
-!- FUNCTION: IGF-binding proteins prolong the half-life of the IGFs
and have been shown to either inhibit or stimulate the growth
promoting effects of the IGFs on cell culture. They alter the
interaction of IGFs with their cell surface receptors.
-!- SUBUNIT: Binds IGF2 more than IGF1. {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P22692-1; Sequence=Displayed;
Name=2;
IsoId=P22692-2; Sequence=VSP_057034;
Note=No experimental confirmation available.;
-!- INDUCTION: By forskolin and N6,O2'dibutyryl adenosine 3',5'-cyclic
monophosphate, but not by 1,9 dideoxyforskolin.
{ECO:0000269|PubMed:1726835}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/igfbp4/";
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EMBL; M38177; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M62403; AAB06189.1; -; mRNA.
EMBL; U20982; AAA62670.1; -; Genomic_DNA.
EMBL; Y12508; CAA73110.1; -; Genomic_DNA.
EMBL; AK304572; BAG65363.1; -; mRNA.
EMBL; BT019891; AAV38694.1; -; mRNA.
EMBL; BT019892; AAV38695.1; -; mRNA.
EMBL; AY442346; AAR05443.1; -; Genomic_DNA.
EMBL; AC018629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60664.1; -; Genomic_DNA.
EMBL; BC016041; AAH16041.1; -; mRNA.
CCDS; CCDS11367.1; -. [P22692-1]
PIR; G01662; B37252.
RefSeq; NP_001543.2; NM_001552.2. [P22692-1]
UniGene; Hs.462998; -.
PDB; 1WQJ; X-ray; 1.60 A; B=24-103.
PDB; 2DSP; X-ray; 2.50 A; B=22-113.
PDB; 2DSQ; X-ray; 2.80 A; A/B=22-113.
PDB; 2DSR; X-ray; 2.10 A; B=24-103, G=172-253.
PDBsum; 1WQJ; -.
PDBsum; 2DSP; -.
PDBsum; 2DSQ; -.
PDBsum; 2DSR; -.
ProteinModelPortal; P22692; -.
SMR; P22692; -.
BioGrid; 109708; 9.
DIP; DIP-48432N; -.
IntAct; P22692; 4.
MINT; MINT-6630380; -.
STRING; 9606.ENSP00000269593; -.
BindingDB; P22692; -.
ChEMBL; CHEMBL2310; -.
MEROPS; I31.952; -.
iPTMnet; P22692; -.
PhosphoSitePlus; P22692; -.
BioMuta; IGFBP4; -.
DMDM; 124065; -.
EPD; P22692; -.
MaxQB; P22692; -.
PaxDb; P22692; -.
PeptideAtlas; P22692; -.
PRIDE; P22692; -.
DNASU; 3487; -.
Ensembl; ENST00000269593; ENSP00000269593; ENSG00000141753. [P22692-1]
GeneID; 3487; -.
KEGG; hsa:3487; -.
UCSC; uc002hus.4; human. [P22692-1]
CTD; 3487; -.
DisGeNET; 3487; -.
GeneCards; IGFBP4; -.
HGNC; HGNC:5473; IGFBP4.
HPA; HPA066240; -.
MIM; 146733; gene.
neXtProt; NX_P22692; -.
OpenTargets; ENSG00000141753; -.
PharmGKB; PA29706; -.
eggNOG; ENOG410IKZ1; Eukaryota.
eggNOG; ENOG4111HXV; LUCA.
GeneTree; ENSGT00550000074457; -.
HOGENOM; HOG000253012; -.
HOVERGEN; HBG002631; -.
InParanoid; P22692; -.
OMA; KGMPCGV; -.
OrthoDB; EOG091G0EIN; -.
PhylomeDB; P22692; -.
TreeFam; TF331211; -.
BioCyc; MetaCyc:ENSG00000141753-MONOMER; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; IGFBP4; human.
EvolutionaryTrace; P22692; -.
GeneWiki; IGFBP4; -.
GenomeRNAi; 3487; -.
PMAP-CutDB; P22692; -.
PRO; PR:P22692; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141753; -.
CleanEx; HS_IGFBP4; -.
ExpressionAtlas; P22692; baseline and differential.
Genevisible; P22692; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0031994; F:insulin-like growth factor I binding; IBA:GO_Central.
GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; TAS:ParkinsonsUK-UCL.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006259; P:DNA metabolic process; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR022327; IGFBP-4.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR009168; IGFBP1-6.
InterPro; IPR022321; IGFBP_1-6_chordata.
InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
InterPro; IPR000716; Thyroglobulin_1.
PANTHER; PTHR11551; PTHR11551; 1.
Pfam; PF00219; IGFBP; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
PRINTS; PR01976; IGFBPFAMILY.
PRINTS; PR01980; IGFBPFAMILY4.
SMART; SM00121; IB; 1.
SMART; SM00211; TY; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS00222; IGFBP_N_1; 1.
PROSITE; PS51323; IGFBP_N_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Growth factor binding; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:1709161,
ECO:0000269|PubMed:1709585,
ECO:0000269|PubMed:1726835}.
CHAIN 22 258 Insulin-like growth factor-binding
protein 4.
/FTId=PRO_0000014382.
DOMAIN 23 103 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 171 249 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
MOD_RES 255 255 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000303|PubMed:1709161}.
DISULFID 27 53 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 30 55 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 38 59 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 44 56 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 67 80 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 74 100 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 131 138 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 174 204 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 215 226 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
DISULFID 228 249 {ECO:0000269|PubMed:15642270,
ECO:0000269|PubMed:16924115}.
VAR_SEQ 1 100 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057034.
VARIANT 42 42 V -> G (in dbSNP:rs599199).
/FTId=VAR_011906.
CONFLICT 51 51 P -> A (in Ref. 2; M38177, 4; AAA62670
and 12; AA sequence). {ECO:0000305}.
CONFLICT 160 160 G -> E (in Ref. 7; AAV38694).
{ECO:0000305}.
CONFLICT 198 198 I -> F (in Ref. 2; M38177 and 4;
AAA62670). {ECO:0000305}.
HELIX 32 36 {ECO:0000244|PDB:1WQJ}.
STRAND 45 49 {ECO:0000244|PDB:1WQJ}.
STRAND 56 59 {ECO:0000244|PDB:1WQJ}.
STRAND 69 71 {ECO:0000244|PDB:2DSQ}.
STRAND 78 81 {ECO:0000244|PDB:1WQJ}.
HELIX 89 94 {ECO:0000244|PDB:1WQJ}.
STRAND 98 102 {ECO:0000244|PDB:1WQJ}.
HELIX 103 110 {ECO:0000244|PDB:2DSP}.
HELIX 173 186 {ECO:0000244|PDB:2DSR}.
HELIX 195 198 {ECO:0000244|PDB:2DSR}.
STRAND 208 210 {ECO:0000244|PDB:2DSR}.
STRAND 212 215 {ECO:0000244|PDB:2DSR}.
STRAND 226 229 {ECO:0000244|PDB:2DSR}.
TURN 231 233 {ECO:0000244|PDB:2DSR}.
HELIX 244 246 {ECO:0000244|PDB:2DSR}.
SEQUENCE 258 AA; 27934 MW; 5E8F4638D99F0A94 CRC64;
MLPLCLVAAL LLAAGPGPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE PGCGCCATCA
LGLGMPCGVY TPRCGSGLRC YPPRGVEKPL HTLMHGQGVC MELAEIEAIQ ESLQPSDKDE
GDHPNNSFSP CSAHDRRCLQ KHFAKIRDRS TSGGKMKVNG APREDARPVP QGSCQSELHR
ALERLAASQS RTHEDLYIIP IPNCDRNGNF HPKQCHPALD GQRGKCWCVD RKTGVKLPGG
LEPKGELDCH QLADSFRE


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E0274m ELISA kit IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,Mouse,Mus musculus 96T
E0274r ELISA kit IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,Rat,Rattus norvegicus 96T
E0055r ELISA IBP-4,IGF-binding protein 4,Igfbp4,IGFBP-4,Igfbp-4,Insulin-like growth factor-binding protein 4,Rat,Rattus norvegicus 96T
E0055r ELISA kit IBP-4,IGF-binding protein 4,Igfbp4,IGFBP-4,Igfbp-4,Insulin-like growth factor-binding protein 4,Rat,Rattus norvegicus 96T
E0055m ELISA kit IBP-4,IGF-binding protein 4,Igfbp4,IGFBP-4,Igfbp-4,Insulin-like growth factor-binding protein 4,Mouse,Mus musculus 96T
E0052m ELISA IBP-1,IGF-binding protein 1,Igfbp1,IGFBP-1,Igfbp-1,Insulin-like growth factor-binding protein 1,Mouse,Mus musculus 96T
E0052r ELISA IBP-1,IGF-binding protein 1,Igfbp1,IGFBP-1,Igfbp-1,Insulin-like growth factor-binding protein 1,Rat,Rattus norvegicus 96T
E0054m ELISA kit IBP-3,IGF-binding protein 3,Igfbp3,IGFBP-3,Igfbp-3,Insulin-like growth factor-binding protein 3,Mouse,Mus musculus 96T
U0055m CLIA IBP-4,IGF-binding protein 4,Igfbp4,IGFBP-4,Igfbp-4,Insulin-like growth factor-binding protein 4,Mouse,Mus musculus 96T
E0054r ELISA kit IBP-3,IGF-binding protein 3,Igfbp3,IGFBP-3,Igfbp-3,Insulin-like growth factor-binding protein 3,Rat,Rattus norvegicus 96T
U0274m CLIA IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,Mouse,Mus musculus 96T
U0274r CLIA IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,Rat,Rattus norvegicus 96T
E0054m ELISA IBP-3,IGF-binding protein 3,Igfbp3,IGFBP-3,Igfbp-3,Insulin-like growth factor-binding protein 3,Mouse,Mus musculus 96T
E0052m ELISA kit IBP-1,IGF-binding protein 1,Igfbp1,IGFBP-1,Igfbp-1,Insulin-like growth factor-binding protein 1,Mouse,Mus musculus 96T
E0274r ELISA IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,Rat,Rattus norvegicus 96T
U0054m CLIA IBP-3,IGF-binding protein 3,Igfbp3,IGFBP-3,Igfbp-3,Insulin-like growth factor-binding protein 3,Mouse,Mus musculus 96T


 

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