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

Protein NOV homolog (NovH) (CCN family member 3) (Insulin-like growth factor-binding protein 9) (IBP-9) (IGF-binding protein 9) (IGFBP-9) (Nephroblastoma-overexpressed gene protein homolog)

 NOV_HUMAN               Reviewed;         357 AA.
P48745; B2R5X7; Q6I9S3; Q96BY5; Q9UDE4;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 152.
RecName: Full=Protein NOV homolog;
Short=NovH;
AltName: Full=CCN family member 3;
AltName: Full=Insulin-like growth factor-binding protein 9;
Short=IBP-9;
Short=IGF-binding protein 9;
Short=IGFBP-9;
AltName: Full=Nephroblastoma-overexpressed gene protein homolog;
Flags: Precursor;
Name=NOV; Synonyms=CCN3, IGFBP9, NOVH;
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].
TISSUE=Placenta;
PubMed=7520150;
Martinerie C., Huff V., Joubert I., Badzioch M., Saunders G.F.,
Strong L.C., Perbal B.;
"Structural analysis of the human nov proto-oncogene and expression in
Wilms tumor.";
Oncogene 9:2729-2732(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=8622864;
Martinerie C., Chevalier G., Rauscher F.J. III, Perbal B.;
"Regulation of nov by WT1: a potential role for nov in
nephrogenesis.";
Oncogene 12:1479-1492(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Jiang D., Gou D., Li W.;
"Cloning, sequencing and expression of human nov gene.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-102, AND TISSUE SPECIFICITY.
PubMed=1756408;
Martinerie C., Perbal B.;
"Expression of a gene encoding a novel potential IGF binding protein
in human tissues.";
C. R. Acad. Sci. III, Sci. Vie 313:345-351(1991).
[8]
PROTEIN SEQUENCE OF 32-46.
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).
[9]
INTERACTION WITH FBLN1.
PubMed=9927660; DOI=10.1073/pnas.96.3.869;
Perbal B., Martinerie C., Sainson R., Werner M., He B., Roizman B.;
"The C-terminal domain of the regulatory protein NOVH is sufficient to
promote interaction with fibulin 1C: a clue for a role of NOVH in
cell-adhesion signaling.";
Proc. Natl. Acad. Sci. U.S.A. 96:869-874(1999).
[10]
FUNCTION, AND INTERACTION WITH NOTCH1.
PubMed=12050162; DOI=10.1074/jbc.M203727200;
Sakamoto K., Yamaguchi S., Ando R., Miyawaki A., Kabasawa Y.,
Takagi M., Li C.L., Perbal B., Katsube K.;
"The nephroblastoma overexpressed gene (NOV/ccn3) protein associates
with Notch1 extracellular domain and inhibits myoblast differentiation
via Notch signaling pathway.";
J. Biol. Chem. 277:29399-29405(2002).
[11]
FUNCTION, AND INTERACTION WITH ITGA5; ITGAV; ITGB1 AND ITGB3.
PubMed=12695522; DOI=10.1074/jbc.M302028200;
Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
Lau L.F.;
"CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
family.";
J. Biol. Chem. 278:24200-24208(2003).
[12]
FUNCTION, INTERACTION WITH GJA1, AND SUBCELLULAR LOCATION.
PubMed=15181016; DOI=10.1074/jbc.M404073200;
Gellhaus A., Dong X., Propson S., Maass K., Klein-Hitpass L.,
Kibschull M., Traub O., Willecke K., Perbal B., Lye S.J.,
Winterhager E.;
"Connexin43 interacts with NOV: a possible mechanism for negative
regulation of cell growth in choriocarcinoma cells.";
J. Biol. Chem. 279:36931-36942(2004).
[13]
INTERACTION WITH GJA1.
PubMed=15213231; DOI=10.1074/jbc.M403952200;
Fu C.T., Bechberger J.F., Ozog M.A., Perbal B., Naus C.C.;
"CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible
mechanism of connexin-mediated growth suppression.";
J. Biol. Chem. 279:36943-36950(2004).
[14]
FUNCTION, AND INTERACTION WITH ITGAV AND ITGB5.
PubMed=15611078; DOI=10.1074/jbc.M404903200;
Lin C.G., Chen C.C., Leu S.J., Grzeszkiewicz T.M., Lau L.F.;
"Integrin-dependent functions of the angiogenic inducer NOV (CCN3):
implication in wound healing.";
J. Biol. Chem. 280:8229-8237(2005).
[15]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=17463287; DOI=10.1126/science.1136031;
Gupta R., Hong D., Iborra F., Sarno S., Enver T.;
"NOV (CCN3) functions as a regulator of human hematopoietic stem or
progenitor cells.";
Science 316:590-593(2007).
[16]
FUNCTION.
PubMed=20139355; DOI=10.1161/ATVBAHA.110.203356;
Shimoyama T., Hiraoka S., Takemoto M., Koshizaka M., Tokuyama H.,
Tokuyama T., Watanabe A., Fujimoto M., Kawamura H., Sato S.,
Tsurutani Y., Saito Y., Perbal B., Koseki H., Yokote K.;
"CCN3 inhibits neointimal hyperplasia through modulation of smooth
muscle cell growth and migration.";
Arterioscler. Thromb. Vasc. Biol. 30:675-682(2010).
[17]
FUNCTION, INDUCTION BY LAMINAR SHEAR STRESS; STATINS AND TNF, AND
TISSUE SPECIFICITY.
PubMed=21063504; DOI=10.1007/s12079-010-0095-x;
Lin Z., Natesan V., Shi H., Hamik A., Kawanami D., Hao C.,
Mahabaleshwar G.H., Wang W., Jin Z.G., Atkins G.B., Firth S.M.,
Rittie L., Perbal B., Jain M.K.;
"A novel role of CCN3 in regulating endothelial inflammation.";
J. Cell Commun. Signal. 4:141-153(2010).
[18]
FUNCTION.
PubMed=21871891; DOI=10.1016/j.febslet.2011.08.024;
Janune D., Kubota S., Nishida T., Kawaki H., Perbal B., Iida S.,
Takigawa M.;
"Novel effects of CCN3 that may direct the differentiation of
chondrocytes.";
FEBS Lett. 585:3033-3040(2011).
[19]
FUNCTION.
PubMed=21344378; DOI=10.1002/jcp.22672;
Tzeng H.E., Chen J.C., Tsai C.H., Kuo C.C., Hsu H.C., Hwang W.L.,
Fong Y.C., Tang C.H.;
"CCN3 increases cell motility and MMP-13 expression in human
chondrosarcoma through integrin-dependent pathway.";
J. Cell. Physiol. 226:3181-3189(2011).
[20]
INDUCTION BY TNF AND IL1B.
PubMed=24722330; DOI=10.1371/journal.pone.0094912;
Liu J., Ren Y., Kang L., Zhang L.;
"Overexpression of CCN3 inhibits inflammation and progression of
atherosclerosis in apolipoprotein E-deficient mice.";
PLoS ONE 9:E94912-E94912(2014).
-!- FUNCTION: Immediate-early protein playing a role in various
cellular processes including proliferation, adhesion, migration,
differentiation and survival (PubMed:15181016, PubMed:15611078,
PubMed:12695522, PubMed:21344378, PubMed:12050162). Acts by
binding to integrins or membrane receptors such as NOTCH1
(PubMed:12695522, PubMed:21344378, PubMed:15611078). Essential
regulator of hematopoietic stem and progenitor cell function
(PubMed:17463287). Inhibits myogenic differentiation through the
activation of Notch-signaling pathway (PubMed:12050162). Inhibits
vascular smooth muscle cells proliferation by increasing
expression of cell-cycle regulators such as CDKN2B or CDKN1A
independently of TGFB1 signaling (PubMed:20139355). Ligand of
integrins ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon
endothelial cells to stimulate pro-angiogenic activities and
induces angiogenesis. In endothelial cells, supports cell
adhesion, induces directed cell migration (chemotaxis) and
promotes cell survival (PubMed:12695522). Plays also a role in
cutaneous wound healing acting as integrin receptor ligand.
Supports skin fibroblast adhesion through ITGA5:ITGB1 and
ITGA6:ITGB1 and induces fibroblast chemotaxis through ITGAV:ITGB5.
Seems to enhance bFGF-induced DNA synthesis in fibroblasts
(PubMed:15611078). Involved in bone regeneration as a negative
regulator (By similarity). Enhances the articular chondrocytic
phenotype, whereas it repressed the one representing endochondral
ossification (PubMed:21871891). Impairs pancreatic beta-cell
function, inhibits beta-cell proliferation and insulin secretion
(By similarity). Plays a role as negative regulator of endothelial
pro-inflammatory activation reducing monocyte adhesion, its anti-
inflammatory effects occur secondary to the inhibition of NF-
kappaB signaling pathway (PubMed:21063504). Contributes to the
control and coordination of inflammatory processes in
atherosclerosis (By similarity). Attenuates inflammatory pain
through regulation of IL1B- and TNF-induced MMP9, MMP2 and CCL2
expression. Inhibits MMP9 expression through ITGB1 engagement
(PubMed:21871891). {ECO:0000250|UniProtKB:Q64299,
ECO:0000269|PubMed:12050162, ECO:0000269|PubMed:12695522,
ECO:0000269|PubMed:15181016, ECO:0000269|PubMed:15611078,
ECO:0000269|PubMed:17463287, ECO:0000269|PubMed:20139355,
ECO:0000269|PubMed:21063504, ECO:0000269|PubMed:21344378,
ECO:0000269|PubMed:21871891}.
-!- SUBUNIT: Interacts with FBLN1. Interacts (via CTCK domain) with
NOTCH1 (via the EGF-like repeat region) (PubMed:12050162).
Interacts with GJA1/CX43 (PubMed:15181016, PubMed:15213231).
Interacts with ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB5
(PubMed:12695522, PubMed:15611078). {ECO:0000269|PubMed:12050162,
ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:15181016,
ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:15611078,
ECO:0000269|PubMed:9927660}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasm
{ECO:0000269|PubMed:15181016}. Cell junction, gap junction
{ECO:0000269|PubMed:15181016}. Note=Localizes at the Gap junction
in presence of GJA1/CX43. {ECO:0000250|UniProtKB:Q9QZQ5}.
-!- TISSUE SPECIFICITY: Expressed in endiothelial cells (at protein
level) (PubMed:21063504). Expressed in bone marrow, thymic cells
and nephroblastoma. Increased expression in Wilms tumor of the
stromal type. {ECO:0000269|PubMed:1756408,
ECO:0000269|PubMed:21063504}.
-!- DEVELOPMENTAL STAGE: Expressed in primitive compartments of
umbilical vein cord. {ECO:0000269|PubMed:17463287}.
-!- INDUCTION: Expression is down-regulated by WT1. Expression is
down-regulated by proinflammatory stimuli such as TNF or IL1B
(PubMed:24722330, PubMed:21063504). Expression is induced by
laminar shear stress and statins (PubMed:21063504).
{ECO:0000269|PubMed:21063504, ECO:0000269|PubMed:24722330,
ECO:0000269|PubMed:8622864}.
-!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X78351; CAA55146.1; -; Genomic_DNA.
EMBL; X78352; CAA55146.1; JOINED; Genomic_DNA.
EMBL; X78353; CAA55146.1; JOINED; Genomic_DNA.
EMBL; X78354; CAA55146.1; JOINED; Genomic_DNA.
EMBL; X96584; CAA65403.1; -; mRNA.
EMBL; AY082381; AAL92490.1; -; mRNA.
EMBL; AK312355; BAG35274.1; -; mRNA.
EMBL; CR457432; CAG33713.1; -; mRNA.
EMBL; BC015028; AAH15028.1; -; mRNA.
CCDS; CCDS6328.1; -.
PIR; I38069; I38069.
RefSeq; NP_002505.1; NM_002514.3.
UniGene; Hs.235935; -.
ProteinModelPortal; P48745; -.
SMR; P48745; -.
BioGrid; 110918; 15.
CORUM; P48745; -.
IntAct; P48745; 14.
STRING; 9606.ENSP00000259526; -.
DrugBank; DB00030; Insulin Human.
DrugBank; DB00071; Insulin Pork.
iPTMnet; P48745; -.
PhosphoSitePlus; P48745; -.
BioMuta; NOV; -.
DMDM; 1352515; -.
MaxQB; P48745; -.
PaxDb; P48745; -.
PeptideAtlas; P48745; -.
PRIDE; P48745; -.
DNASU; 4856; -.
Ensembl; ENST00000259526; ENSP00000259526; ENSG00000136999.
GeneID; 4856; -.
KEGG; hsa:4856; -.
UCSC; uc003yoq.3; human.
CTD; 4856; -.
DisGeNET; 4856; -.
EuPathDB; HostDB:ENSG00000136999.4; -.
GeneCards; NOV; -.
HGNC; HGNC:7885; NOV.
HPA; CAB034423; -.
HPA; HPA018449; -.
HPA; HPA019684; -.
MIM; 164958; gene.
neXtProt; NX_P48745; -.
OpenTargets; ENSG00000136999; -.
PharmGKB; PA31687; -.
eggNOG; ENOG410IH0W; Eukaryota.
eggNOG; ENOG4111F77; LUCA.
GeneTree; ENSGT00760000119225; -.
HOGENOM; HOG000231462; -.
HOVERGEN; HBG000635; -.
InParanoid; P48745; -.
OMA; CEMVKQT; -.
OrthoDB; EOG091G0SQP; -.
PhylomeDB; P48745; -.
TreeFam; TF326070; -.
SignaLink; P48745; -.
SIGNOR; P48745; -.
ChiTaRS; NOV; human.
GeneWiki; NOV_(gene); -.
GenomeRNAi; 4856; -.
PRO; PR:P48745; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000136999; -.
CleanEx; HS_NOV; -.
ExpressionAtlas; P48745; baseline and differential.
Genevisible; P48745; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005921; C:gap junction; IMP:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0008201; F:heparin binding; IBA:GO_Central.
GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:1990523; P:bone regeneration; ISS:UniProtKB.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0002062; P:chondrocyte differentiation; IMP:UniProtKB.
GO; GO:0035767; P:endothelial cell chemotaxis; IDA:UniProtKB.
GO; GO:0071603; P:endothelial cell-cell adhesion; IDA:UniProtKB.
GO; GO:0010761; P:fibroblast migration; IDA:UniProtKB.
GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0090027; P:negative regulation of monocyte chemotaxis; IMP:UniProtKB.
GO; GO:0010832; P:negative regulation of myotube differentiation; IDA:UniProtKB.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IMP:UniProtKB.
GO; GO:1904057; P:negative regulation of sensory perception of pain; ISS:UniProtKB.
GO; GO:0060392; P:negative regulation of SMAD protein import into nucleus; ISS:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0014909; P:smooth muscle cell migration; IDA:UniProtKB.
GO; GO:0048659; P:smooth muscle cell proliferation; IDA:UniProtKB.
GO; GO:0044342; P:type B pancreatic cell proliferation; ISS:UniProtKB.
InterPro; IPR006207; Cys_knot_C.
InterPro; IPR006208; Glyco_hormone_CN.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR012395; IGFBP_CNN.
InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
InterPro; IPR001007; VWF_dom.
Pfam; PF00007; Cys_knot; 1.
Pfam; PF00219; IGFBP; 1.
Pfam; PF00093; VWC; 1.
PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
SMART; SM00041; CT; 1.
SMART; SM00121; IB; 1.
SMART; SM00209; TSP1; 1.
SMART; SM00214; VWC; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS01185; CTCK_1; 1.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS00222; IGFBP_N_1; 1.
PROSITE; PS51323; IGFBP_N_2; 1.
PROSITE; PS50092; TSP1; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
Cell junction; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Gap junction; Glycoprotein;
Growth factor; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 31 {ECO:0000269|PubMed:15340161}.
CHAIN 32 357 Protein NOV homolog.
/FTId=PRO_0000014415.
DOMAIN 32 105 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 108 174 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 205 250 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 264 338 CTCK. {ECO:0000255|PROSITE-
ProRule:PRU00039}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 264 301 {ECO:0000250}.
DISULFID 281 315 {ECO:0000250}.
DISULFID 292 331 {ECO:0000250}.
DISULFID 295 333 {ECO:0000250}.
DISULFID 300 337 {ECO:0000250}.
VARIANT 42 42 R -> Q (in dbSNP:rs2279112).
/FTId=VAR_049568.
VARIANT 233 233 R -> H (in dbSNP:rs11538929).
/FTId=VAR_049569.
CONFLICT 26 27 LG -> CL (in Ref. 7). {ECO:0000305}.
CONFLICT 97 97 N -> K (in Ref. 5; CAG33713 and 6;
AAH15028). {ECO:0000305}.
CONFLICT 231 231 R -> G (in Ref. 4; BAG35274).
{ECO:0000305}.
CONFLICT 357 357 M -> I (in Ref. 5; CAG33713).
{ECO:0000305}.
SEQUENCE 357 AA; 39162 MW; 035D5BF4576BD85B CRC64;
MQSVQSTSFC LRKQCLCLTF LLLHLLGQVA ATQRCPPQCP GRCPATPPTC APGVRAVLDG
CSCCLVCARQ RGESCSDLEP CDESSGLYCD RSADPSNQTG ICTAVEGDNC VFDGVIYRSG
EKFQPSCKFQ CTCRDGQIGC VPRCQLDVLL PEPNCPAPRK VEVPGECCEK WICGPDEEDS
LGGLTLAAYR PEATLGVEVS DSSVNCIEQT TEWTACSKSC GMGFSTRVTN RNRQCEMLKQ
TRLCMVRPCE QEPEQPTDKK GKKCLRTKKS LKAIHLQFKN CTSLHTYKPR FCGVCSDGRC
CTPHNTKTIQ AEFQCSPGQI VKKPVMVIGT CTCHTNCPKN NEAFLQELEL KTTRGKM


Related products :

Catalog number Product name Quantity
EIAAB27560 CCN family member 3,CCN3,Homo sapiens,Human,IBP-9,IGF-binding protein 9,IGFBP9,IGFBP-9,Insulin-like growth factor-binding protein 9,Nephroblastoma-overexpressed gene protein homolog,NOV,NovH,NOVH,Prot
EIAAB27559 CCN family member 3,Ccn3,Nephroblastoma-overexpressed gene protein homolog,Nov,NovH,Protein NOV homolog,Rat,Rattus norvegicus
EIAAB27561 CCN family member 3,Ccn3,Mouse,Mus musculus,Nephroblastoma-overexpressed gene protein homolog,Nov,NovH,Protein NOV homolog
Y050616 Anti-NovH(Nephroblastoma overexpressed gene protein homolog) Antibody 100ug
EIAAB10298 CCN family member 1,Ccn1,Cyr61,Cysteine-rich angiogenic inducer 61,IBP-10,IGF-binding protein 10,Igfbp10,IGFBP-10,Insulin-like growth factor-binding protein 10,Protein CYR61,Rat,Rattus norvegicus
EIAAB10296 3CH61,CCN family member 1,Ccn1,Cyr61,Cysteine-rich angiogenic inducer 61,IBP-10,IGF-binding protein 10,Igfbp10,IGFBP-10,Insulin-like growth factor-binding protein 10,Mouse,Mus musculus,Protein CYR61
EIAAB10297 CCN family member 1,CCN1,CYR61,Cysteine-rich angiogenic inducer 61,GIG1,Homo sapiens,Human,IBP-10,IGF-binding protein 10,IGFBP10,IGFBP-10,Insulin-like growth factor-binding protein 10,Protein CYR61,Pr
26-065 IGFBP4 is a member of the insulin-like growth factor binding protein (IGFBP) family. IGFBP4 is a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like gro 0.05 mg
18-003-44208 Insulin-like growth factor 2 mRNA-binding protein 1 - IGF2 mRNA-binding protein 1; IGF-II mRNA-binding protein 1; IMP-1; Coding region determinant-binding protein; CRD-BP; VICKZ family member 1 Polycl 0.05 mg Aff Pur
U0010h CLIA CCN family member 2,CCN2,Connective tissue growth factor,CTGF,HCS24,Homo sapiens,Human,Hypertrophic chondrocyte-specific protein 24,IBP-8,IGF-binding protein 8,IGFBP8,IGFBP-8,Insulin-like growth 96T
E0010h ELISA CCN family member 2,CCN2,Connective tissue growth factor,CTGF,HCS24,Homo sapiens,Human,Hypertrophic chondrocyte-specific protein 24,IBP-8,IGF-binding protein 8,IGFBP8,IGFBP-8,Insulin-like growth 96T
20-783-72936 MOUSE ANTI HUMAN INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN 3 - INSULIN LIKE GROWTH FACTOR BINDING PROTEIN 3; IGFBP-3; IBP-3; IGF-binding protein 3 Monoclonal 0.2 mg
10-663-45148 Insulin Like Growth Factor Binding Protein-1 (IGFBP-1) Human - IGFBP-1; IBP-1; IGF-binding protein 1; Placental protein 12; PP12 N_A 0.005 mg
10-663-45148 Insulin Like Growth Factor Binding Protein-1 (IGFBP-1) Human - IGFBP-1; IBP-1; IGF-binding protein 1; Placental protein 12; PP12 N_A 0.02 mg
10-663-45148 Insulin Like Growth Factor Binding Protein-1 (IGFBP-1) Human - IGFBP-1; IBP-1; IGF-binding protein 1; Placental protein 12; PP12 N_A 1 mg
E0010h ELISA kit CCN family member 2,CCN2,Connective tissue growth factor,CTGF,HCS24,Homo sapiens,Human,Hypertrophic chondrocyte-specific protein 24,IBP-8,IGF-binding protein 8,IGFBP8,IGFBP-8,Insulin-like g 96T
E0053m ELISA kit IBP-2,IGF-binding protein 2,Igfbp2,IGFBP-2,Igfbp-2,Insulin-like growth factor-binding protein 2,mIGFBP-2,Mouse,Mus musculus 96T
U0053m CLIA IBP-2,IGF-binding protein 2,Igfbp2,IGFBP-2,Igfbp-2,Insulin-like growth factor-binding protein 2,mIGFBP-2,Mouse,Mus musculus 96T
E0053m ELISA IBP-2,IGF-binding protein 2,Igfbp2,IGFBP-2,Igfbp-2,Insulin-like growth factor-binding protein 2,mIGFBP-2,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
E0053r ELISA BRL-BP,IBP-2,IGF-binding protein 2,Igfbp2,IGFBP-2,Igfbp-2,Insulin-like growth factor-binding protein 2,Rat,Rattus norvegicus 96T
E0274m ELISA IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,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
E0274r ELISA IBP-6,IGF-binding protein 6,Igfbp6,IGFBP-6,Igfbp-6,Insulin-like growth factor-binding protein 6,Rat,Rattus norvegicus 96T


 

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