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Insulin-like growth factor II (IGF-II) (Somatomedin-A) (T3M-11-derived growth factor) [Cleaved into: Insulin-like growth factor II; Insulin-like growth factor II Ala-25 Del; Preptin]

 IGF2_HUMAN              Reviewed;         180 AA.
P01344; B3KX48; B7WP08; C9JAF2; E3UN45; P78449; Q14299; Q1WM26;
Q9UC68; Q9UC69;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
18-JUL-2018, entry version 227.
RecName: Full=Insulin-like growth factor II;
Short=IGF-II;
AltName: Full=Somatomedin-A;
AltName: Full=T3M-11-derived growth factor;
Contains:
RecName: Full=Insulin-like growth factor II;
Contains:
RecName: Full=Insulin-like growth factor II Ala-25 Del;
Contains:
RecName: Full=Preptin;
Flags: Precursor;
Name=IGF2; ORFNames=PP1446;
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] (ISOFORM 1).
PubMed=6382022; DOI=10.1038/310777a0;
Dull T.J., Gray A., Hayflick J.S., Ullrich A.;
"Insulin-like growth factor II precursor gene organization in relation
to insulin gene family.";
Nature 310:777-781(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND MISCELLANEOUS.
PubMed=6382021; DOI=10.1038/310775a0;
Bell G.I., Merryweather J.P., Sanchez-Pescador R., Stempien M.M.,
Priestley L., Scott J., Rall L.B.;
"Sequence of a cDNA clone encoding human preproinsulin-like growth
factor II.";
Nature 310:775-777(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2450353; DOI=10.1073/pnas.85.6.1947;
Shen S.-J., Daimon M., Wang C.-Y., Jansen M., Ilan J.;
"Isolation of an insulin-like growth factor II cDNA with a unique 5'
untranslated region from human placenta.";
Proc. Natl. Acad. Sci. U.S.A. 85:1947-1951(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=3002851; DOI=10.1016/0014-5793(86)80156-9;
de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M.,
van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.;
"Organization of the human genes for insulin-like growth factors I and
II.";
FEBS Lett. 195:179-184(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3476948; DOI=10.1073/pnas.84.18.6330;
Irminger J.C., Rosen K.M., Humbel R.E., Villa-Komaroff L.;
"Tissue-specific expression of insulin-like growth factor II mRNAs
with distinct 5' untranslated regions.";
Proc. Natl. Acad. Sci. U.S.A. 84:6330-6334(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3683205;
Rall L.B., Scott J., Bell G.I.;
"Human insulin-like growth factor I and II messenger RNA: isolation of
complementary DNA and analysis of expression.";
Methods Enzymol. 146:239-248(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=3881277; DOI=10.1016/0014-5793(85)80527-5;
Jansen M., van Schaik F.M.A., van Tol H., van den Brande J.L.,
Sussenbach J.S.;
"Nucleotide sequences of cDNAs encoding precursors of human insulin-
like growth factor II (IGF-II) and an IGF-II variant.";
FEBS Lett. 179:243-246(1985).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7730145; DOI=10.1111/j.1349-7006.1995.tb03040.x;
Hagiwara K., Kobayashi T., Tobita M., Kikyo N., Yazaki Y., Okabe T.;
"Isolation of a cDNA for a growth factor of vascular endothelial cells
from human lung cancer cells: its identity with insulin-like growth
factor II.";
Jpn. J. Cancer Res. 86:202-207(1995).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=16531418; DOI=10.1093/hmg/ddl041;
Monk D., Sanches R., Arnaud P., Apostolidou S., Hills F.A.,
Abu-Amero S., Murrell A., Friess H., Reik W., Stanier P.,
Constancia M., Moore G.E.;
"Imprinting of IGF2 P0 transcript and novel alternatively spliced INS-
IGF2 isoforms show differences between mouse and human.";
Hum. Mol. Genet. 15:1259-1269(2006).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-165 (ISOFORM 3), AND ALTERNATIVE
SPLICING.
PubMed=20842449; DOI=10.1007/s11033-010-0259-z;
Li J., Neumann I., Volkmer I., Staege M.S.;
"Down-regulation of achaete-scute complex homolog 1 (ASCL1) in
neuroblastoma cells induces up-regulation of insulin-like growth
factor 2 (IGF2).";
Mol. Biol. Rep. 38:1515-1521(2011).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[12]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
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).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[16]
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.
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
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).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-180.
PubMed=3167054; DOI=10.1016/0167-4781(88)90124-8;
de Pagter-Holthuizen P., van der Kammen R.A., Jansen M.,
van Schaik F.M.A., Sussenbach J.S.;
"Differential expression of the human insulin-like growth factor II
gene. Characterization of the IGF-II mRNAs and an mRNA encoding a
putative IGF-II-associated protein.";
Biochim. Biophys. Acta 950:282-295(1988).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-161 (ISOFORM 2).
PubMed=3653397; DOI=10.1016/0014-5793(87)80216-8;
le Bouc Y., Noguiez P., Sondermeijer P., Dreyer D., Girard F.,
Binoux M.;
"A new 5'-non-coding region for human placental insulin-like growth
factor II mRNA expression.";
FEBS Lett. 222:181-185(1987).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
TISSUE=Liver;
PubMed=3652904; DOI=10.1089/dna.1987.6.283;
Gray A., Tam A.W., Dull T.J., Hayflick J.S., Pintar J., Cavenee W.K.,
Koufos A., Ullrich A.;
"Tissue-specific and developmentally regulated transcription of the
insulin-like growth factor 2 gene.";
DNA 6:283-295(1987).
[21]
PROTEIN SEQUENCE OF 25-91.
PubMed=658418; DOI=10.1016/0014-5793(78)80237-3;
Rinderknecht E., Humbel R.E.;
"Primary structure of human insulin-like growth factor II.";
FEBS Lett. 89:283-286(1978).
[22]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=2722836;
Smith M.C., Cook J.A., Furman T.C., Occolowitz J.L.;
"Structure and activity dependence of recombinant human insulin-like
growth factor II on disulfide bond pairing.";
J. Biol. Chem. 264:9314-9321(1989).
[23]
PROTEIN SEQUENCE OF 25-68.
PubMed=7633596; DOI=10.1016/0378-4347(94)00576-Q;
De Ceuninck F., Willeput J., Corvol M.;
"Purification and characterization of insulin-like growth factor II
(IGF II) and an IGF II variant from human placenta.";
J. Chromatogr. B 666:203-214(1995).
[24]
GLYCOSYLATION AT THR-99.
PubMed=1569071;
Hudgins W.R., Hampton B., Burgess W.H., Perdue J.F.;
"The identification of O-glycosylated precursors of insulin-like
growth factor II.";
J. Biol. Chem. 267:8153-8160(1992).
[25]
POLYMORPHISM, AND ASSOCIATION WITH WITH BODY MASS INDEX.
PubMed=11448941; DOI=10.1093/hmg/10.14.1491;
Gaunt T.R., Cooper J.A., Miller G.J., Day I.N.M., O'Dell S.D.;
"Positive associations between single nucleotide polymorphisms in the
IGF2 gene region and body mass index in adult males.";
Hum. Mol. Genet. 10:1491-1501(2001).
[26]
MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
PubMed=12586351; DOI=10.1016/S0014-5793(03)00042-5;
Nedelkov D., Nelson R.W., Kiernan U.A., Niederkofler E.E., Tubbs K.A.;
"Detection of bound and free IGF-1 and IGF-2 in human plasma via
biomolecular interaction analysis mass spectrometry.";
FEBS Lett. 536:130-134(2003).
[27]
MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
PubMed=15359740; DOI=10.1021/pr0499388;
Nelson R.W., Nedelkov D., Tubbs K.A., Kiernan U.A.;
"Quantitative mass spectrometric immunoassay of insulin like growth
factor 1.";
J. Proteome Res. 3:851-855(2004).
[28]
PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
MUTAGENESIS OF ARG-92; LYS-112 AND ARG-128, AND GLYCOSYLATION.
PubMed=16040806; DOI=10.1073/pnas.0502357102;
Qiu Q., Basak A., Mbikay M., Tsang B.K., Gruslin A.;
"Role of pro-IGF-II processing by proprotein convertase 4 in human
placental development.";
Proc. Natl. Acad. Sci. U.S.A. 102:11047-11052(2005).
[29]
OSTEOGENIC FUNCTION OF PREPTIN.
PubMed=16912056; DOI=10.1152/ajpendo.00642.2005;
Cornish J., Callon K.E., Bava U., Watson M., Xu X., Lin J.M.,
Chan V.A., Grey A.B., Naot D., Buchanan C.M., Cooper G.J., Reid I.R.;
"Preptin, another peptide product of the pancreatic beta-cell, is
osteogenic in vitro and in vivo.";
Am. J. Physiol. 292:E117-E122(2007).
[30]
INVOLVEMENT IN SRS.
PubMed=19066168; DOI=10.1136/jmg.2008.061820;
Bartholdi D., Krajewska-Walasek M., Ounap K., Gaspar H.,
Chrzanowska K.H., Ilyana H., Kayserili H., Lurie I.W., Schinzel A.,
Baumer A.;
"Epigenetic mutations of the imprinted IGF2-H19 domain in Silver-
Russell syndrome (SRS): results from a large cohort of patients with
SRS and SRS-like phenotypes.";
J. Med. Genet. 46:192-197(2009).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-163, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[32]
GLYCOSYLATION AT THR-96; THR-99 AND THR-163, STRUCTURE OF
CARBOHYDRATES, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 11:1-17(2012).
[33]
GLYCOSYLATION AT THR-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[34]
REVIEW OF FUNCTION.
PubMed=24593700; DOI=10.1111/cen.12446;
Livingstone C., Borai A.;
"Insulin-like growth factor-II: its role in metabolic and endocrine
disease.";
Clin. Endocrinol. (Oxf.) 80:773-781(2014).
[35]
INVOLVEMENT IN GRDF.
PubMed=26154720; DOI=10.1056/NEJMoa1415227;
Begemann M., Zirn B., Santen G., Wirthgen E., Soellner L.,
Buettel H.M., Schweizer R., van Workum W., Binder G., Eggermann T.;
"Paternally inherited IGF2 mutation and growth restriction.";
N. Engl. J. Med. 373:349-356(2015).
[36]
FUNCTION, INTERACTION WITH INTEGRINS ITGAV:ITGB3 AND ITGA6:ITGB4,
SITES IMPORTANT FOR INTEGRIN BINDING, AND MUTAGENESIS OF ARG-48;
ARG-58; ARG-61; ARG-62 AND ARG-64.
PubMed=28873464; DOI=10.1371/journal.pone.0184285;
Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K.,
Takada Y.;
"Direct integrin binding to insulin-like growth factor-2 through the
C-domain is required for insulin-like growth factor receptor type 1
(IGF1R) signaling.";
PLoS ONE 12:E0184285-E0184285(2017).
[37]
3D-STRUCTURE MODELING.
PubMed=6189745;
Blundell T.L., Bedarkar S., Humbel R.E.;
"Tertiary structures, receptor binding, and antigenicity of
insulinlike growth factors.";
Fed. Proc. 42:2592-2597(1983).
[38]
STRUCTURE BY NMR.
PubMed=7527339;
Terasawa H., Kohda D., Hatanaka H., Nagata K., Higashihashi N.,
Fujiwara H., Sakano K., Inagaki F.;
"Solution structure of human insulin-like growth factor II;
recognition sites for receptors and binding proteins.";
EMBO J. 13:5590-5597(1994).
[39]
X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 25-91 IN COMPLEX WITH IGF2R,
AND DISULFIDE BONDS.
PubMed=18046459; DOI=10.1038/sj.emboj.7601938;
Brown J., Delaine C., Zaccheo O.J., Siebold C., Gilbert R.J.,
van Boxel G., Denley A., Wallace J.C., Hassan A.B., Forbes B.E.,
Jones E.Y.;
"Structure and functional analysis of the IGF-II/IGF2R interaction.";
EMBO J. 27:265-276(2008).
-!- FUNCTION: The insulin-like growth factors possess growth-promoting
activity. Major fetal growth hormone in mammals. Plays a key role
in regulating fetoplacental development. IGF-II is influenced by
placental lactogen. Also involved in tissue differentiation.
Positively regulates myogenic transcription factor MYOD1 function
by facilitating the recruitment of transcriptional coactivators,
thereby controlling muscle terminal differentiation (By
similarity). In adults, involved in glucose metabolism in adipose
tissue, skeletal muscle and liver (Probable). Acts as a ligand for
integrin which is required for IGF2 signaling (PubMed:28873464).
{ECO:0000250|UniProtKB:P09535, ECO:0000269|PubMed:28873464,
ECO:0000305|PubMed:24593700}.
-!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with
insulin, and acts as physiological amplifier of glucose-mediated
insulin secretion. Exhibits osteogenic properties by increasing
osteoblast mitogenic activity through phosphoactivation of MAPK1
and MAPK3. {ECO:0000269|PubMed:16912056}.
-!- SUBUNIT: Interacts with MYORG; this interaction is required for
IGF2 secretion (By similarity). Interacts with integrins
ITGAV:ITGB3 and ITGA6:ITGB4; integrin-binding is required for IGF2
signaling (PubMed:28873464). {ECO:0000250|UniProtKB:P09535,
ECO:0000269|PubMed:28873464}.
-!- INTERACTION:
P11717:IGF2R; NbExp=17; IntAct=EBI-7178764, EBI-1048580;
Q93062:RBPMS; NbExp=3; IntAct=EBI-7178764, EBI-740322;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16040806}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P01344-1; Sequence=Displayed;
Note=Product of 5 different transcripts regulated by 5 different
promoters, denominated P0, P1, P2, P3 and P4.
{ECO:0000305|PubMed:16531418};
Name=2;
IsoId=P01344-2; Sequence=VSP_002708;
Name=3;
IsoId=P01344-3; Sequence=VSP_045624;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in heart, placenta, lung, liver,
muscle, kidney, tongue, limb, eye and pancreas.
{ECO:0000269|PubMed:16531418}.
-!- DEVELOPMENTAL STAGE: During embryogenesis, detected in liver,
lung, skeletal muscle and placenta. {ECO:0000269|PubMed:16531418}.
-!- PTM: O-glycosylated with core 1 or possibly core 8 glycans. Thr-96
is a minor glycosylation site compared to Thr-99.
{ECO:0000269|PubMed:1569071, ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360}.
-!- PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at
Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2.
{ECO:0000269|PubMed:16040806}.
-!- MASS SPECTROMETRY: Mass=7469.4; Method=MALDI; Range=25-91;
Evidence={ECO:0000269|PubMed:12586351,
ECO:0000269|PubMed:15359740};
-!- MASS SPECTROMETRY: Mass=7398.3; Method=MALDI; Range=26-91;
Evidence={ECO:0000269|PubMed:12586351,
ECO:0000269|PubMed:15359740};
-!- POLYMORPHISM: Genetic variations in IGF2 are associated with body
mass index (BMI). The BMI is a statistical measurement which
compares a person's weight and height.
{ECO:0000269|PubMed:11448941}.
-!- DISEASE: Silver-Russell syndrome (SRS) [MIM:180860]: A clinically
heterogeneous condition characterized by severe intrauterine
growth retardation, poor postnatal growth, craniofacial features
such as a triangular shaped face and a broad forehead, body
asymmetry, and a variety of minor malformations. The phenotypic
expression changes during childhood and adolescence, with the
facial features and asymmetry usually becoming more subtle with
age. {ECO:0000269|PubMed:19066168}. Note=The gene represented in
this entry is involved in disease pathogenesis. Most of the cases
of Silver-Russell syndrome are caused by the epigenetic changes of
DNA hypomethylation at the telomeric imprinting control region
(ICR1) on chromosome 11p15, involving the H19 and IGF2 genes.
-!- DISEASE: Growth restriction, severe, with distinctive facies
(GRDF) [MIM:616489]: A disease characterized by severe prenatal
and postnatal growth restriction, facial dysmorphism, and short
stature in the presence of normal or slightly elevated growth
hormone levels. {ECO:0000269|PubMed:26154720}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The IGF2 locus is imprinted. Paternal inherited
gene is expressed, while the maternal inherited gene is imprinted,
hence silenced. Transcripts from 5 promoters P0, P1, P2, P3 and P4
code for the same protein but are differentially regulated in a
developmental stage and tissue specificity.
{ECO:0000305|PubMed:16531418}.
-!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Insulin-like growth factor 2
entry;
URL="https://en.wikipedia.org/wiki/Insulin-like_growth_factor_2";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/igf2/";
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EMBL; X03562; CAA27249.1; -; Genomic_DNA.
EMBL; X00910; CAA25426.1; -; mRNA.
EMBL; J03242; AAA52545.1; -; mRNA.
EMBL; X03425; CAA27155.1; -; Genomic_DNA.
EMBL; X03426; CAA27156.1; -; Genomic_DNA.
EMBL; X03427; CAA27157.1; -; Genomic_DNA.
EMBL; M17426; AAA60088.1; -; mRNA.
EMBL; M29645; AAA52544.1; -; mRNA.
EMBL; M17863; AAA52443.1; ALT_SEQ; mRNA.
EMBL; S77035; AAB34155.1; -; mRNA.
EMBL; DQ104203; ABD93451.1; -; mRNA.
EMBL; HM481219; ADO21454.1; -; mRNA.
EMBL; AF217977; AAG17220.1; -; mRNA.
EMBL; BT007013; AAP35659.1; -; mRNA.
EMBL; AF517226; AAM51825.1; -; Genomic_DNA.
EMBL; AC132217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK126688; BAG54360.1; -; mRNA.
EMBL; CH471158; EAX02485.1; -; Genomic_DNA.
EMBL; BC000531; AAH00531.1; -; mRNA.
EMBL; X07868; CAA30717.1; -; Genomic_DNA.
EMBL; X06159; CAA29516.1; -; mRNA.
EMBL; X06160; CAA29517.1; -; Transcribed_RNA.
EMBL; X06161; CAA29518.1; -; mRNA.
EMBL; M22373; AAA52536.1; -; Genomic_DNA.
CCDS; CCDS44517.1; -. [P01344-3]
CCDS; CCDS7728.1; -. [P01344-1]
PIR; B23614; IGHU2.
PIR; I67610; I67610.
PIR; S02423; S02423.
RefSeq; NP_000603.1; NM_000612.5. [P01344-1]
RefSeq; NP_001007140.2; NM_001007139.5. [P01344-1]
RefSeq; NP_001121070.1; NM_001127598.2. [P01344-3]
RefSeq; NP_001278790.1; NM_001291861.2. [P01344-1]
RefSeq; NP_001278791.1; NM_001291862.2. [P01344-1]
UniGene; Hs.272259; -.
PDB; 1GF2; Model; -; A=25-91.
PDB; 1IGL; NMR; -; A=25-91.
PDB; 2L29; NMR; -; B=25-91.
PDB; 2V5P; X-ray; 4.10 A; C/D=25-91.
PDB; 3E4Z; X-ray; 2.28 A; C/D=25-91.
PDB; 3KR3; X-ray; 2.20 A; D=25-91.
PDB; 5L3L; NMR; -; A=25-91.
PDB; 5L3M; NMR; -; A=25-91.
PDB; 5L3N; NMR; -; A=25-91.
PDBsum; 1GF2; -.
PDBsum; 1IGL; -.
PDBsum; 2L29; -.
PDBsum; 2V5P; -.
PDBsum; 3E4Z; -.
PDBsum; 3KR3; -.
PDBsum; 5L3L; -.
PDBsum; 5L3M; -.
PDBsum; 5L3N; -.
ProteinModelPortal; P01344; -.
SMR; P01344; -.
BioGrid; 109702; 30.
CORUM; P01344; -.
DIP; DIP-29508N; -.
IntAct; P01344; 10.
MINT; P01344; -.
STRING; 9606.ENSP00000391826; -.
ChEMBL; CHEMBL3712957; -.
GlyConnect; 760; -.
iPTMnet; P01344; -.
PhosphoSitePlus; P01344; -.
UniCarbKB; P01344; -.
BioMuta; IGF2; -.
DMDM; 124255; -.
MaxQB; P01344; -.
PaxDb; P01344; -.
PeptideAtlas; P01344; -.
PRIDE; P01344; -.
ProteomicsDB; 12641; -. [P01344-2]
ProteomicsDB; 51375; -.
ProteomicsDB; 51376; -. [P01344-2]
DNASU; 3481; -.
Ensembl; ENST00000381389; ENSP00000370796; ENSG00000167244. [P01344-1]
Ensembl; ENST00000381392; ENSP00000370799; ENSG00000167244. [P01344-2]
Ensembl; ENST00000381395; ENSP00000370802; ENSG00000167244. [P01344-1]
Ensembl; ENST00000381406; ENSP00000370813; ENSG00000167244. [P01344-2]
Ensembl; ENST00000416167; ENSP00000414497; ENSG00000167244. [P01344-1]
Ensembl; ENST00000418738; ENSP00000402047; ENSG00000167244. [P01344-1]
Ensembl; ENST00000434045; ENSP00000391826; ENSG00000167244. [P01344-3]
Ensembl; ENST00000641326; ENSP00000493122; ENSG00000167244. [P01344-1]
GeneID; 3481; -.
KEGG; hsa:3481; -.
UCSC; uc001lvf.4; human. [P01344-1]
CTD; 3481; -.
DisGeNET; 3481; -.
EuPathDB; HostDB:ENSG00000167244.18; -.
GeneCards; IGF2; -.
GeneReviews; IGF2; -.
H-InvDB; HIX0128667; -.
HGNC; HGNC:5466; IGF2.
HPA; HPA007556; -.
HPA; HPA007993; -.
MalaCards; IGF2; -.
MIM; 147470; gene+phenotype.
MIM; 180860; phenotype.
MIM; 616489; phenotype.
neXtProt; NX_P01344; -.
OpenTargets; ENSG00000167244; -.
Orphanet; 231117; Beckwith-Wiedemann syndrome due to imprinting defect of 11p15.
Orphanet; 2128; Hemihypertrophy.
Orphanet; 231144; Silver-Russell syndrome due to 11p15 microduplication.
Orphanet; 231140; Silver-Russell syndrome due to imprinting defect of 11p15.
PharmGKB; PA29699; -.
eggNOG; ENOG410IY3P; Eukaryota.
eggNOG; ENOG4111KP2; LUCA.
GeneTree; ENSGT00530000063856; -.
HOGENOM; HOG000233362; -.
HOVERGEN; HBG006137; -.
InParanoid; P01344; -.
KO; K13769; -.
OMA; FPRYPVG; -.
OrthoDB; EOG091G0H56; -.
PhylomeDB; P01344; -.
TreeFam; TF332820; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
Reactome; R-HSA-2428928; IRS-related events triggered by IGF1R.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
SignaLink; P01344; -.
SIGNOR; P01344; -.
ChiTaRS; IGF2; human.
EvolutionaryTrace; P01344; -.
GeneWiki; Insulin-like_growth_factor_2; -.
GenomeRNAi; 3481; -.
PMAP-CutDB; P01344; -.
PRO; PR:P01344; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000167244; -.
CleanEx; HS_IGF2; -.
Genevisible; P01344; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0005158; F:insulin receptor binding; IPI:BHF-UCL.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IMP:AgBase.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:BHF-UCL.
GO; GO:0048018; F:receptor ligand activity; ISS:BHF-UCL.
GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB.
GO; GO:0060669; P:embryonic placenta morphogenesis; ISS:UniProtKB.
GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:ProtInc.
GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; ISS:BHF-UCL.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL.
GO; GO:0043085; P:positive regulation of catalytic activity; ISS:BHF-UCL.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; ISS:BHF-UCL.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:BHF-UCL.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:BHF-UCL.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; TAS:ProtInc.
GO; GO:0031056; P:regulation of histone modification; ISS:UniProtKB.
GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
InterPro; IPR022334; IGF2.
InterPro; IPR013576; IGF2_C.
InterPro; IPR016179; Insulin-like.
InterPro; IPR022350; Insulin-like_growth_factor.
InterPro; IPR036438; Insulin-like_sf.
InterPro; IPR022353; Insulin_CS.
InterPro; IPR022352; Insulin_family.
Pfam; PF08365; IGF2_C; 1.
Pfam; PF00049; Insulin; 2.
PRINTS; PR02002; INSLNLIKEGF.
PRINTS; PR02006; INSLNLIKEGF2.
PRINTS; PR00276; INSULINFAMLY.
ProDom; PD005188; IGF2_C; 1.
SMART; SM00078; IlGF; 1.
SUPFAM; SSF56994; SSF56994; 1.
PROSITE; PS00262; INSULIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carbohydrate metabolism;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Dwarfism;
Glucose metabolism; Glycoprotein; Growth factor; Hormone; Mitogen;
Osteogenesis; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:658418,
ECO:0000269|PubMed:7633596}.
CHAIN 25 91 Insulin-like growth factor II.
/FTId=PRO_0000015717.
CHAIN 26 91 Insulin-like growth factor II Ala-25 Del.
/FTId=PRO_0000015718.
PROPEP 92 180 E peptide.
/FTId=PRO_0000015719.
PEPTIDE 93 126 Preptin.
/FTId=PRO_0000370376.
REGION 25 52 B.
REGION 53 64 C.
REGION 65 85 A.
REGION 86 91 D.
SITE 48 48 Important for interaction with integrin.
{ECO:0000269|PubMed:28873464}.
SITE 58 58 Important for interaction with integrin.
{ECO:0000269|PubMed:28873464}.
SITE 61 61 Important for interaction with integrin.
{ECO:0000269|PubMed:28873464}.
SITE 62 62 Important for interaction with integrin.
{ECO:0000269|PubMed:28873464}.
CARBOHYD 96 96 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360}.
CARBOHYD 99 99 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1569071,
ECO:0000269|PubMed:22171320}.
CARBOHYD 163 163 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:22171320}.
DISULFID 33 71 {ECO:0000269|PubMed:2722836}.
DISULFID 45 84 {ECO:0000269|PubMed:2722836}.
DISULFID 70 75 {ECO:0000269|PubMed:2722836}.
VAR_SEQ 1 1 M -> MVSPDPQIIVVAPETELASMQVQRTEDGVTIIQIFW
VGRKGELLRRTPVSSAMQTPM (in isoform 3).
{ECO:0000303|PubMed:20842449}.
/FTId=VSP_045624.
VAR_SEQ 53 53 S -> RLPG (in isoform 2).
{ECO:0000303|PubMed:3653397,
ECO:0000303|PubMed:3881277}.
/FTId=VSP_002708.
VARIANT 120 120 K -> N (in dbSNP:rs14367).
/FTId=VAR_011959.
VARIANT 173 173 P -> Q (in dbSNP:rs1050342).
/FTId=VAR_011960.
VARIANT 180 180 K -> N (in dbSNP:rs12993).
/FTId=VAR_011961.
MUTAGEN 48 48 R->E: Does not affect integrin binding.
Defective integrin binding and IGF2
signaling; when associated with E-58; E-
61 and E-62.
{ECO:0000269|PubMed:28873464}.
MUTAGEN 58 58 R->E: Does not affect integrin binding.
Defective integrin binding and IGF2
signaling; when associated with E-48; E-
61 and E-62.
{ECO:0000269|PubMed:28873464}.
MUTAGEN 61 61 R->E: Does not affect integrin binding.
Defective integrin binding and IGF2
signaling; when associated with E-48; E-
58 and E-62.
{ECO:0000269|PubMed:28873464}.
MUTAGEN 62 62 R->E: Does not affect integrin binding.
Defective integrin binding and IGF2
signaling; when associated with E-48; E-
58 and E-61.
{ECO:0000269|PubMed:28873464}.
MUTAGEN 64 64 R->E: Slight but significant increase in
integrin binding.
{ECO:0000269|PubMed:28873464}.
MUTAGEN 92 92 R->A: Decreases mature IGF2 levels.
{ECO:0000269|PubMed:16040806}.
MUTAGEN 112 112 K->A: No effect in proteolytical
processing.
{ECO:0000269|PubMed:16040806}.
MUTAGEN 128 128 R->A: Abolishes proteolytical processing.
{ECO:0000269|PubMed:16040806}.
CONFLICT 3 3 I -> M (in Ref. 6; AAA52544).
{ECO:0000305}.
CONFLICT 107 110 RYPV -> EIPL (in Ref. 1; CAA27249).
{ECO:0000305}.
CONFLICT 147 147 E -> ELE (in Ref. 5; AAA60088).
{ECO:0000305}.
HELIX 34 44 {ECO:0000244|PDB:3KR3}.
TURN 45 48 {ECO:0000244|PDB:3KR3}.
STRAND 50 52 {ECO:0000244|PDB:3KR3}.
HELIX 55 58 {ECO:0000244|PDB:3KR3}.
HELIX 61 72 {ECO:0000244|PDB:3KR3}.
HELIX 77 82 {ECO:0000244|PDB:3KR3}.
STRAND 86 88 {ECO:0000244|PDB:1IGL}.
SEQUENCE 180 AA; 20140 MW; C1B0EB1E016BA37A CRC64;
MGIPMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF YFSRPASRVS
RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTPPTV LPDNFPRYPV GKFFQYDTWK
QSTQRLRRGL PALLRARRGH VLAKELEAFR EAKRHRPLIA LPTQDPAHGG APPEMASNRK


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