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Periostin (PN) (Osteoblast-specific factor 2) (OSF-2)

 POSTN_HUMAN             Reviewed;         836 AA.
Q15063; B1ALD8; C0IMJ1; C0IMJ2; C0IMJ4; D2KRH7; F5H628; Q15064;
Q29XZ0; Q3KPJ5; Q5VSY5; Q8IZF9;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
07-NOV-2018, entry version 166.
RecName: Full=Periostin;
Short=PN;
AltName: Full=Osteoblast-specific factor 2;
Short=OSF-2;
Flags: Precursor;
Name=POSTN; Synonyms=OSF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Osteosarcoma {ECO:0000269|PubMed:8363580}, and
Placenta {ECO:0000269|PubMed:8363580};
PubMed=8363580; DOI=10.1042/bj2940271;
Takeshita S., Kikuno R., Tezuka K., Amann E.;
"Osteoblast-specific factor 2: cloning of a putative bone adhesion
protein with homology with the insect protein fasciclin I.";
Biochem. J. 294:271-278(1993).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=12235007;
Gillan L., Matei D., Fishman D.A., Gerbin C.S., Karlan B.Y.,
Chang D.D.;
"Periostin secreted by epithelial ovarian carcinoma is a ligand for
alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell
motility.";
Cancer Res. 62:5358-5364(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5; 6; 7), ALTERNATIVE SPLICING,
AND TISSUE SPECIFICITY.
PubMed=23946676; DOI=10.4137/JCM.S5899;
Bai Y., Nakamura M., Zhou G., Li Y., Liu Z., Ozaki T., Mori I.,
Kakudo K.;
"Novel isoforms of periostin expressed in the human thyroid.";
Jpn. Clin. Med. 1:13-20(2010).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Periodontal ligament;
Yamada S., Maeda K., Matsubara K., Murakami S.;
"Identification and characterization of a novel periodontal ligament-
specific periostin isoform.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-798 (ISOFORM 5).
Habtemichael N., Schweitzer A., Knauer S., Stauber R.H.;
"OSF-2 expression in head and neck squamous cell carcinomas.";
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=11550156;
DOI=10.1002/1097-0142(20010815)92:4<843::AID-CNCR1391>3.0.CO;2-P;
Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
Fujii Y., Chen L.B.;
"Serum level of the periostin, a homologue of an insect cell adhesion
molecule, as a prognostic marker in nonsmall cell lung carcinomas.";
Cancer 92:843-848(2001).
[10]
ERRATUM.
Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
Fujii Y., Chen L.B.;
Cancer 95:2580-2580(2002).
[11]
TISSUE SPECIFICITY.
PubMed=15082792; DOI=10.1128/MCB.24.9.3992-4003.2004;
Shao R., Bao S., Bai X., Blanchette C., Anderson R.M., Dang T.,
Gishizky M.L., Marks J.R., Wang X.-F.;
"Acquired expression of periostin by human breast cancers promotes
tumor angiogenesis through up-regulation of vascular endothelial
growth factor receptor 2 expression.";
Mol. Cell. Biol. 24:3992-4003(2004).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
SUBCELLULAR LOCATION, AND GAMMA-CARBOXYGLUTAMATION.
PubMed=18450759; DOI=10.1074/jbc.M708029200;
Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D.,
Galipeau J.;
"Periostin, a member of a novel family of vitamin K-dependent
proteins, is expressed by mesenchymal stromal cells.";
J. Biol. Chem. 283:17991-18001(2008).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
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).
[16]
SUBCELLULAR LOCATION, AND LACK OF GAMMA-CARBOXYGLUTAMATION.
PubMed=26273833; DOI=10.1371/journal.pone.0135374;
Annis D.S., Ma H., Balas D.M., Kumfer K.T., Sandbo N., Potts G.K.,
Coon J.J., Mosher D.F.;
"Absence of vitamin K-dependent gamma-carboxylation in human periostin
extracted from fibrotic lung or secreted from a cell line engineered
to optimize gamma-carboxylation.";
PLoS ONE 10:E0135374-E0135374(2015).
-!- FUNCTION: Induces cell attachment and spreading and plays a role
in cell adhesion (PubMed:12235007). Enhances incorporation of BMP1
in the fibronectin matrix of connective tissues, and subsequent
proteolytic activation of lysyl oxidase LOX (By similarity).
{ECO:0000250|UniProtKB:Q62009, ECO:0000269|PubMed:12235007}.
-!- SUBUNIT: Interacts with BMP1 and fibronectin.
{ECO:0000250|UniProtKB:Q62009}.
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000250|UniProtKB:Q62009}. Secreted
{ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}.
Secreted, extracellular space, extracellular matrix
{ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:18450759}.
Note=Colocalizes with BMP1 in the Golgi.
{ECO:0000250|UniProtKB:Q62009}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1 {ECO:0000269|PubMed:8363580}; Synonyms=OSF-2OS
{ECO:0000303|PubMed:8363580};
IsoId=Q15063-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:8363580}; Synonyms=OSF-2p1;
IsoId=Q15063-2; Sequence=VSP_050005;
Name=3 {ECO:0000269|PubMed:12235007};
IsoId=Q15063-3; Sequence=VSP_050669, VSP_050670;
Name=4;
IsoId=Q15063-4; Sequence=VSP_050005, VSP_050670;
Name=5;
IsoId=Q15063-5; Sequence=VSP_050669;
Name=6;
IsoId=Q15063-6; Sequence=VSP_055183;
Name=7;
IsoId=Q15063-7; Sequence=VSP_055183, VSP_050670;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in aorta,
stomach, lower gastrointestinal tract, placenta, uterus, thyroid
tissue and breast. Up-regulated in epithelial ovarian tumors. Not
expressed in normal ovaries. Also highly expressed at the tumor
periphery of lung carcinoma tissue but not within the tumor.
Overexpressed in breast cancers. {ECO:0000269|PubMed:11550156,
ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:15082792,
ECO:0000269|PubMed:23946676}.
-!- PTM: Gamma-carboxylation is controversial. Gamma-
carboxyglutamated; gamma-carboxyglutamate residues are formed by
vitamin K dependent carboxylation; this may be required for
calcium binding (PubMed:18450759). According to a more recent
report, does not contain vitamin K-dependent gamma-
carboxyglutamate residues (PubMed:26273833).
{ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}.
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EMBL; D13665; BAA02836.1; -; mRNA.
EMBL; D13666; BAA02837.1; -; mRNA.
EMBL; AY140646; AAN17733.1; -; mRNA.
EMBL; EU262883; ABY86630.1; -; mRNA.
EMBL; EU262884; ABY86631.1; -; mRNA.
EMBL; EU262886; ABY86633.1; -; mRNA.
EMBL; AY918092; AAY15840.1; -; mRNA.
EMBL; AL138679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL646087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08590.1; -; Genomic_DNA.
EMBL; BC106709; AAI06710.1; -; mRNA.
EMBL; BC106710; AAI06711.1; -; mRNA.
EMBL; GU354210; ADA79517.1; -; mRNA.
CCDS; CCDS45034.1; -. [Q15063-2]
CCDS; CCDS53864.1; -. [Q15063-3]
CCDS; CCDS66530.1; -. [Q15063-6]
CCDS; CCDS66531.1; -. [Q15063-5]
CCDS; CCDS9364.1; -. [Q15063-1]
PIR; S36110; S36110.
PIR; S36111; S36111.
RefSeq; NP_001129406.1; NM_001135934.1. [Q15063-2]
RefSeq; NP_001129407.1; NM_001135935.1. [Q15063-3]
RefSeq; NP_001129408.1; NM_001135936.1. [Q15063-4]
RefSeq; NP_001273594.1; NM_001286665.1. [Q15063-5]
RefSeq; NP_001273595.1; NM_001286666.1. [Q15063-6]
RefSeq; NP_001273596.1; NM_001286667.1. [Q15063-7]
RefSeq; NP_001317446.1; NM_001330517.1.
RefSeq; NP_006466.2; NM_006475.2. [Q15063-1]
UniGene; Hs.136348; -.
UniGene; Hs.721018; -.
PDB; 5WT7; NMR; -; A=496-632.
PDB; 5YJG; X-ray; 2.40 A; A=22-631.
PDB; 5YJH; X-ray; 2.96 A; A=17-631.
PDBsum; 5WT7; -.
PDBsum; 5YJG; -.
PDBsum; 5YJH; -.
ProteinModelPortal; Q15063; -.
SMR; Q15063; -.
BioGrid; 115875; 5.
IntAct; Q15063; 3.
MINT; Q15063; -.
STRING; 9606.ENSP00000369071; -.
GlyConnect; 1599; -.
iPTMnet; Q15063; -.
PhosphoSitePlus; Q15063; -.
BioMuta; POSTN; -.
DMDM; 93138709; -.
EPD; Q15063; -.
MaxQB; Q15063; -.
PaxDb; Q15063; -.
PeptideAtlas; Q15063; -.
PRIDE; Q15063; -.
ProteomicsDB; 60417; -.
ProteomicsDB; 60418; -. [Q15063-2]
ProteomicsDB; 60419; -. [Q15063-3]
ProteomicsDB; 60420; -. [Q15063-4]
Ensembl; ENST00000379742; ENSP00000369066; ENSG00000133110. [Q15063-2]
Ensembl; ENST00000379743; ENSP00000369067; ENSG00000133110. [Q15063-5]
Ensembl; ENST00000379747; ENSP00000369071; ENSG00000133110. [Q15063-1]
Ensembl; ENST00000541179; ENSP00000437959; ENSG00000133110. [Q15063-3]
Ensembl; ENST00000541481; ENSP00000437953; ENSG00000133110. [Q15063-6]
GeneID; 10631; -.
KEGG; hsa:10631; -.
UCSC; uc001uwo.5; human. [Q15063-1]
CTD; 10631; -.
DisGeNET; 10631; -.
EuPathDB; HostDB:ENSG00000133110.14; -.
GeneCards; POSTN; -.
HGNC; HGNC:16953; POSTN.
HPA; HPA012306; -.
MIM; 608777; gene.
neXtProt; NX_Q15063; -.
OpenTargets; ENSG00000133110; -.
PharmGKB; PA134900304; -.
eggNOG; KOG1437; Eukaryota.
eggNOG; COG2335; LUCA.
GeneTree; ENSGT00530000063860; -.
HOGENOM; HOG000220865; -.
HOVERGEN; HBG000715; -.
InParanoid; Q15063; -.
OMA; ANGHYDK; -.
OrthoDB; EOG091G020T; -.
PhylomeDB; Q15063; -.
TreeFam; TF316269; -.
SIGNOR; Q15063; -.
ChiTaRS; POSTN; human.
GeneWiki; Periostin; -.
GeneWiki; POSTN; -.
GenomeRNAi; 10631; -.
PRO; PR:Q15063; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000133110; Expressed in 203 organ(s), highest expression level in periodontal ligament.
CleanEx; HS_POSTN; -.
ExpressionAtlas; Q15063; baseline and differential.
Genevisible; Q15063; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:1990523; P:bone regeneration; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0071307; P:cellular response to vitamin K; IDA:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:1990138; P:neuron projection extension; IEA:Ensembl.
GO; GO:1904209; P:positive regulation of chemokine (C-C motif) ligand 2 secretion; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
Gene3D; 2.30.180.10; -; 4.
InterPro; IPR011489; EMI_domain.
InterPro; IPR036378; FAS1_dom_sf.
InterPro; IPR000782; FAS1_domain.
InterPro; IPR016666; TGFBI/POSTN.
Pfam; PF02469; Fasciclin; 4.
PIRSF; PIRSF016553; BIGH3_OSF2; 1.
SMART; SM00554; FAS1; 4.
SUPFAM; SSF82153; SSF82153; 4.
PROSITE; PS51041; EMI; 1.
PROSITE; PS50213; FAS1; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Complete proteome;
Disulfide bond; Extracellular matrix; Gamma-carboxyglutamic acid;
Glycoprotein; Golgi apparatus; Heparin-binding; Polymorphism;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 836 Periostin.
/FTId=PRO_0000008789.
DOMAIN 40 94 EMI. {ECO:0000255|PROSITE-
ProRule:PRU00384}.
DOMAIN 97 230 FAS1 1. {ECO:0000255|PROSITE-
ProRule:PRU00082, ECO:0000305}.
DOMAIN 234 365 FAS1 2. {ECO:0000255|PROSITE-
ProRule:PRU00082, ECO:0000305}.
DOMAIN 368 492 FAS1 3. {ECO:0000255|PROSITE-
ProRule:PRU00082, ECO:0000305}.
DOMAIN 496 628 FAS1 4. {ECO:0000255|PROSITE-
ProRule:PRU00082, ECO:0000305}.
CARBOHYD 599 599 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 44 80 {ECO:0000255|PROSITE-ProRule:PRU00384}.
DISULFID 60 69 {ECO:0000255|PROSITE-ProRule:PRU00384}.
DISULFID 79 92 {ECO:0000255|PROSITE-ProRule:PRU00384}.
VAR_SEQ 670 757 TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPE
FRLIKEGETITEVIHGEPIIKKYTKIIDGVPVEITEKETRE
ERIITG -> S (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:23946676}.
/FTId=VSP_055183.
VAR_SEQ 670 727 TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPE
FRLIKEGETITEVIHGE -> K (in isoform 2 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8363580,
ECO:0000303|Ref.4}.
/FTId=VSP_050005.
VAR_SEQ 670 697 TTKIITKVVEPKIKVIEGSLQPIIKTEG -> R (in
isoform 3 and isoform 5).
{ECO:0000303|PubMed:12235007,
ECO:0000303|PubMed:23946676,
ECO:0000303|Ref.8}.
/FTId=VSP_050669.
VAR_SEQ 783 810 Missing (in isoform 3, isoform 4 and
isoform 7). {ECO:0000303|PubMed:12235007,
ECO:0000303|PubMed:23946676,
ECO:0000303|Ref.4}.
/FTId=VSP_050670.
VARIANT 339 339 T -> I (in dbSNP:rs9594223).
/FTId=VAR_049115.
VARIANT 814 814 V -> M (in dbSNP:rs9547952).
/FTId=VAR_049116.
CONFLICT 290 290 I -> F (in Ref. 1; BAA02836/BAA02837, 3;
ABY86630/ABY86631/ABY86633 and 4;
AAY15840). {ECO:0000305}.
CONFLICT 421 421 D -> V (in Ref. 1; BAA02836/BAA02837, 3;
ABY86630/ABY86631/ABY86633 and 4;
AAY15840). {ECO:0000305}.
STRAND 43 49 {ECO:0000244|PDB:5YJG}.
STRAND 55 62 {ECO:0000244|PDB:5YJG}.
STRAND 73 79 {ECO:0000244|PDB:5YJG}.
HELIX 101 107 {ECO:0000244|PDB:5YJG}.
HELIX 111 119 {ECO:0000244|PDB:5YJG}.
HELIX 123 126 {ECO:0000244|PDB:5YJG}.
STRAND 128 130 {ECO:0000244|PDB:5YJG}.
STRAND 132 137 {ECO:0000244|PDB:5YJG}.
HELIX 139 144 {ECO:0000244|PDB:5YJG}.
HELIX 147 154 {ECO:0000244|PDB:5YJG}.
TURN 157 159 {ECO:0000244|PDB:5YJG}.
HELIX 160 167 {ECO:0000244|PDB:5YJG}.
STRAND 169 172 {ECO:0000244|PDB:5YJG}.
HELIX 176 178 {ECO:0000244|PDB:5YJG}.
STRAND 184 186 {ECO:0000244|PDB:5YJG}.
STRAND 193 198 {ECO:0000244|PDB:5YJG}.
STRAND 204 206 {ECO:0000244|PDB:5YJG}.
STRAND 209 218 {ECO:0000244|PDB:5YJG}.
STRAND 221 228 {ECO:0000244|PDB:5YJG}.
HELIX 237 243 {ECO:0000244|PDB:5YJG}.
HELIX 245 247 {ECO:0000244|PDB:5YJG}.
HELIX 248 257 {ECO:0000244|PDB:5YJG}.
HELIX 262 264 {ECO:0000244|PDB:5YJG}.
STRAND 265 267 {ECO:0000244|PDB:5YJG}.
STRAND 269 274 {ECO:0000244|PDB:5YJG}.
HELIX 276 281 {ECO:0000244|PDB:5YJG}.
HELIX 286 292 {ECO:0000244|PDB:5YJG}.
HELIX 294 302 {ECO:0000244|PDB:5YJG}.
STRAND 305 308 {ECO:0000244|PDB:5YJG}.
HELIX 312 314 {ECO:0000244|PDB:5YJG}.
STRAND 319 323 {ECO:0000244|PDB:5YJG}.
STRAND 326 334 {ECO:0000244|PDB:5YJG}.
STRAND 337 340 {ECO:0000244|PDB:5YJG}.
STRAND 346 353 {ECO:0000244|PDB:5YJG}.
STRAND 356 363 {ECO:0000244|PDB:5YJG}.
HELIX 368 370 {ECO:0000244|PDB:5YJG}.
HELIX 373 376 {ECO:0000244|PDB:5YJG}.
HELIX 379 381 {ECO:0000244|PDB:5YJG}.
HELIX 382 390 {ECO:0000244|PDB:5YJG}.
HELIX 394 396 {ECO:0000244|PDB:5YJG}.
STRAND 403 408 {ECO:0000244|PDB:5YJG}.
HELIX 410 412 {ECO:0000244|PDB:5YJG}.
HELIX 415 418 {ECO:0000244|PDB:5YJG}.
HELIX 422 430 {ECO:0000244|PDB:5YJG}.
STRAND 433 436 {ECO:0000244|PDB:5YJG}.
HELIX 440 442 {ECO:0000244|PDB:5YJG}.
STRAND 448 451 {ECO:0000244|PDB:5YJG}.
STRAND 456 461 {ECO:0000244|PDB:5YJG}.
STRAND 466 468 {ECO:0000244|PDB:5YJG}.
STRAND 471 473 {ECO:0000244|PDB:5YJG}.
STRAND 481 490 {ECO:0000244|PDB:5YJG}.
HELIX 499 505 {ECO:0000244|PDB:5YJG}.
HELIX 507 509 {ECO:0000244|PDB:5YJG}.
HELIX 510 518 {ECO:0000244|PDB:5YJG}.
HELIX 522 526 {ECO:0000244|PDB:5YJG}.
STRAND 527 529 {ECO:0000244|PDB:5WT7}.
STRAND 531 536 {ECO:0000244|PDB:5YJG}.
HELIX 538 542 {ECO:0000244|PDB:5YJG}.
TURN 543 546 {ECO:0000244|PDB:5YJG}.
HELIX 547 553 {ECO:0000244|PDB:5YJG}.
HELIX 558 564 {ECO:0000244|PDB:5YJG}.
STRAND 567 570 {ECO:0000244|PDB:5YJG}.
HELIX 574 576 {ECO:0000244|PDB:5YJG}.
STRAND 582 586 {ECO:0000244|PDB:5YJG}.
STRAND 590 598 {ECO:0000244|PDB:5YJG}.
STRAND 601 606 {ECO:0000244|PDB:5YJG}.
STRAND 614 616 {ECO:0000244|PDB:5YJG}.
STRAND 619 626 {ECO:0000244|PDB:5YJG}.
SEQUENCE 836 AA; 93314 MW; 55E7B82D094824FD CRC64;
MIPFLPMFSL LLLLIVNPIN ANNHYDKILA HSRIRGRDQG PNVCALQQIL GTKKKYFSTC
KNWYKKSICG QKTTVLYECC PGYMRMEGMK GCPAVLPIDH VYGTLGIVGA TTTQRYSDAS
KLREEIEGKG SFTYFAPSNE AWDNLDSDIR RGLESNVNVE LLNALHSHMI NKRMLTKDLK
NGMIIPSMYN NLGLFINHYP NGVVTVNCAR IIHGNQIATN GVVHVIDRVL TQIGTSIQDF
IEAEDDLSSF RAAAITSDIL EALGRDGHFT LFAPTNEAFE KLPRGVLERI MGDKVASEAL
MKYHILNTLQ CSESIMGGAV FETLEGNTIE IGCDGDSITV NGIKMVNKKD IVTNNGVIHL
IDQVLIPDSA KQVIELAGKQ QTTFTDLVAQ LGLASALRPD GEYTLLAPVN NAFSDDTLSM
DQRLLKLILQ NHILKVKVGL NELYNGQILE TIGGKQLRVF VYRTAVCIEN SCMEKGSKQG
RNGAIHIFRE IIKPAEKSLH EKLKQDKRFS TFLSLLEAAD LKELLTQPGD WTLFVPTNDA
FKGMTSEEKE ILIRDKNALQ NIILYHLTPG VFIGKGFEPG VTNILKTTQG SKIFLKEVND
TLLVNELKSK ESDIMTTNGV IHVVDKLLYP ADTPVGNDQL LEILNKLIKY IQIKFVRGST
FKEIPVTVYT TKIITKVVEP KIKVIEGSLQ PIIKTEGPTL TKVKIEGEPE FRLIKEGETI
TEVIHGEPII KKYTKIIDGV PVEITEKETR EERIITGPEI KYTRISTGGG ETEETLKKLL
QEEVTKVTKF IEGGDGHLFE DEEIKRLLQG DTPVRKLQAN KKVQGSRRRL REGRSQ


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