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Angiopoietin-1 (ANG-1)

 ANGP1_HUMAN             Reviewed;         498 AA.
Q15389; Q5HYA0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
05-DEC-2018, entry version 168.
RecName: Full=Angiopoietin-1;
Short=ANG-1;
Flags: Precursor;
Name=ANGPT1; Synonyms=KIAA0003;
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 2).
TISSUE=Fetal lung;
PubMed=8980223; DOI=10.1016/S0092-8674(00)81812-7;
Davis S., Aldrich T.H., Jones P.F., Acheson A., Compton D.L., Jain V.,
Ryan T.E., Bruno J., Radziejewski C., Maisonpierre P.C.,
Yancopoulos G.D.;
"Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by
secretion-trap expression cloning.";
Cell 87:1161-1169(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Nakatsukasa M., Komai K., Shiozawa S.;
"Human angiopoietin-1 mRNA variant form.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Shan Z.X., Yu X.Y., Lin Q.Y., Fu Y.H., Tan H.H., Zheng M., Lin S.G.;
"Human angiopoietin-1 mRNA variant forms.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[9]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[10]
FUNCTION, AND INTERACTION WITH TEK.
PubMed=9204896; DOI=10.1126/science.277.5322.55;
Maisonpierre P.C., Suri C., Jones P.F., Bartunkova S., Wiegand S.J.,
Radziejewski C., Compton D.L., McClain J., Aldrich T.H.,
Papadopoulos N., Daly T.J., Davis S., Sato T.N., Yancopoulos G.D.;
"Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo
angiogenesis.";
Science 277:55-60(1997).
[11]
INTERACTION WITH TEK.
PubMed=12427764; DOI=10.1074/jbc.M208550200;
Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U.,
Martiny-Baron G., Marme D., Augustin H.G.;
"Angiopoietin-1 and angiopoietin-2 share the same binding domains in
the Tie-2 receptor involving the first Ig-like loop and the epidermal
growth factor-like repeats.";
J. Biol. Chem. 278:1721-1727(2003).
[12]
FUNCTION IN REGULATION OF ANGIOGENESIS; CELL SURVIVAL; CELL MIGRATION
AND ACTIVATION OF AKT1, AND INTERACTION WITH TEK/TIE2.
PubMed=15284220; DOI=10.1096/fj.03-1466com;
Lee H.J., Cho C.H., Hwang S.J., Choi H.H., Kim K.T., Ahn S.Y.,
Kim J.H., Oh J.L., Lee G.M., Koh G.Y.;
"Biological characterization of angiopoietin-3 and angiopoietin-4.";
FASEB J. 18:1200-1208(2004).
[13]
FUNCTION IN REGULATION OF ENDOTHELIAL CELL MIGRATION AND CELL
SPREADING.
PubMed=18425120; DOI=10.1038/ncb1714;
Fukuhara S., Sako K., Minami T., Noda K., Kim H.Z., Kodama T.,
Shibuya M., Takakura N., Koh G.Y., Mochizuki N.;
"Differential function of Tie2 at cell-cell contacts and cell-
substratum contacts regulated by angiopoietin-1.";
Nat. Cell Biol. 10:513-526(2008).
[14]
FUNCTION IN REGULATION OF ENDOTHELIAL CELL MIGRATION.
PubMed=18425119; DOI=10.1038/ncb1715;
Saharinen P., Eklund L., Miettinen J., Wirkkala R., Anisimov A.,
Winderlich M., Nottebaum A., Vestweber D., Deutsch U., Koh G.Y.,
Olsen B.R., Alitalo K.;
"Angiopoietins assemble distinct Tie2 signalling complexes in
endothelial cell-cell and cell-matrix contacts.";
Nat. Cell Biol. 10:527-537(2008).
[15]
REVIEW.
PubMed=19234476; DOI=10.1038/nrm2639;
Augustin H.G., Koh G.Y., Thurston G., Alitalo K.;
"Control of vascular morphogenesis and homeostasis through the
angiopoietin-Tie system.";
Nat. Rev. Mol. Cell Biol. 10:165-177(2009).
[16]
REVIEW.
PubMed=20054809; DOI=10.14670/HH-25.387;
Fukuhara S., Sako K., Noda K., Zhang J., Minami M., Mochizuki N.;
"Angiopoietin-1/Tie2 receptor signaling in vascular quiescence and
angiogenesis.";
Histol. Histopathol. 25:387-396(2010).
[17]
REVIEW.
PubMed=20651738; DOI=10.1038/nrc2894;
Huang H., Bhat A., Woodnutt G., Lappe R.;
"Targeting the ANGPT-TIE2 pathway in malignancy.";
Nat. Rev. Cancer 10:575-585(2010).
[18]
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).
-!- FUNCTION: Binds and activates TEK/TIE2 receptor by inducing its
dimerization and tyrosine phosphorylation. Plays an important role
in the regulation of angiogenesis, endothelial cell survival,
proliferation, migration, adhesion and cell spreading,
reorganization of the actin cytoskeleton, but also maintenance of
vascular quiescence. Required for normal angiogenesis and heart
development during embryogenesis. After birth, activates or
inhibits angiogenesis, depending on the context. Inhibits
angiogenesis and promotes vascular stability in quiescent vessels,
where endothelial cells have tight contacts. In quiescent vessels,
ANGPT1 oligomers recruit TEK to cell-cell contacts, forming
complexes with TEK molecules from adjoining cells, and this leads
to preferential activation of phosphatidylinositol 3-kinase and
the AKT1 signaling cascades. In migrating endothelial cells that
lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the
extracellular matrix, leading to the formation of focal adhesion
complexes, activation of PTK2/FAK and of the downstream kinases
MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of
sprouting angiogenesis. Mediates blood vessel
maturation/stability. Implicated in endothelial developmental
processes later and distinct from that of VEGF. Appears to play a
crucial role in mediating reciprocal interactions between the
endothelium and surrounding matrix and mesenchyme.
{ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:18425119,
ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:9204896}.
-!- SUBUNIT: Homooligomer. Interacts with TEK/TIE2.
{ECO:0000269|PubMed:12427764, ECO:0000269|PubMed:15284220,
ECO:0000269|PubMed:9204896}.
-!- INTERACTION:
Q13387:MAPK8IP2; NbExp=3; IntAct=EBI-10692491, EBI-722813;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15389-1; Sequence=Displayed;
Name=2; Synonyms=Gly-269 del;
IsoId=Q15389-2; Sequence=VSP_046324;
-!- PTM: Glycosylated.
-!- MISCELLANEOUS: It may have a potential therapeutic utility since
it can be used for specifically targeting tumor vasculature or for
promoting angiogenic processes in certain organs such as an
ischemic heart.
-!- SEQUENCE CAUTION:
Sequence=BAA02793.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Angiopoietin entry;
URL="https://en.wikipedia.org/wiki/Angiopoietin";
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EMBL; U83508; AAB50557.1; -; mRNA.
EMBL; AB084454; BAB91325.1; -; mRNA.
EMBL; AY121504; AAM81745.1; -; mRNA.
EMBL; AY124380; AAM92271.1; -; mRNA.
EMBL; D13628; BAA02793.2; ALT_INIT; mRNA.
EMBL; BX648814; CAI45984.1; -; mRNA.
EMBL; AC091010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471060; EAW91909.1; -; Genomic_DNA.
EMBL; BC152411; AAI52412.1; -; mRNA.
EMBL; BC152419; AAI52420.1; -; mRNA.
CCDS; CCDS56551.1; -. [Q15389-2]
CCDS; CCDS6306.1; -. [Q15389-1]
RefSeq; NP_001137.2; NM_001146.4. [Q15389-1]
RefSeq; NP_001186788.1; NM_001199859.2. [Q15389-2]
RefSeq; NP_001300980.1; NM_001314051.1.
UniGene; Hs.369675; -.
PDB; 4EPU; X-ray; 2.10 A; A/B=282-497.
PDB; 4JYO; X-ray; 2.50 A; X=280-498.
PDB; 4K0V; X-ray; 4.51 A; B=280-498.
PDBsum; 4EPU; -.
PDBsum; 4JYO; -.
PDBsum; 4K0V; -.
ProteinModelPortal; Q15389; -.
SMR; Q15389; -.
BioGrid; 106781; 2.
IntAct; Q15389; 2.
STRING; 9606.ENSP00000428340; -.
ChEMBL; CHEMBL3217395; -.
iPTMnet; Q15389; -.
PhosphoSitePlus; Q15389; -.
BioMuta; ANGPT1; -.
DMDM; 12229574; -.
PaxDb; Q15389; -.
PeptideAtlas; Q15389; -.
PRIDE; Q15389; -.
ProteomicsDB; 60559; -.
DNASU; 284; -.
Ensembl; ENST00000297450; ENSP00000297450; ENSG00000154188. [Q15389-2]
Ensembl; ENST00000517746; ENSP00000428340; ENSG00000154188. [Q15389-1]
GeneID; 284; -.
KEGG; hsa:284; -.
UCSC; uc003ymn.4; human. [Q15389-1]
CTD; 284; -.
DisGeNET; 284; -.
EuPathDB; HostDB:ENSG00000154188.9; -.
GeneCards; ANGPT1; -.
HGNC; HGNC:484; ANGPT1.
HPA; CAB017815; -.
HPA; HPA018793; -.
HPA; HPA018816; -.
MIM; 601667; gene.
neXtProt; NX_Q15389; -.
OpenTargets; ENSG00000154188; -.
PharmGKB; PA24791; -.
eggNOG; KOG2579; Eukaryota.
eggNOG; ENOG410ZYS4; LUCA.
GeneTree; ENSGT00940000158117; -.
HOGENOM; HOG000037128; -.
HOVERGEN; HBG001644; -.
InParanoid; Q15389; -.
KO; K05465; -.
OMA; TQWLQKI; -.
OrthoDB; EOG091G03M1; -.
PhylomeDB; Q15389; -.
TreeFam; TF336658; -.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
SignaLink; Q15389; -.
SIGNOR; Q15389; -.
ChiTaRS; ANGPT1; human.
GeneWiki; Angiopoietin_1; -.
GenomeRNAi; 284; -.
PRO; PR:Q15389; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000154188; Expressed in 188 organ(s), highest expression level in cauda epididymis.
CleanEx; HS_ANGPT1; -.
ExpressionAtlas; Q15389; baseline and differential.
Genevisible; Q15389; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
GO; GO:0072012; P:glomerulus vasculature development; ISS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
GO; GO:0030210; P:heparin biosynthetic process; IDA:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; IDA:UniProtKB.
GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:2000446; P:regulation of macrophage migration inhibitory factor signaling pathway; IEA:Ensembl.
GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IDA:UniProtKB.
GO; GO:0032680; P:regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0002040; P:sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0048014; P:Tie signaling pathway; IDA:UniProtKB.
CDD; cd00087; FReD; 1.
Gene3D; 3.90.215.10; -; 1.
Gene3D; 4.10.530.10; -; 1.
InterPro; IPR028843; Ang-1.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR020837; Fibrinogen_CS.
PANTHER; PTHR19143:SF156; PTHR19143:SF156; 1.
Pfam; PF00147; Fibrinogen_C; 1.
SMART; SM00186; FBG; 1.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS00514; FIBRINOGEN_C_1; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Coiled coil;
Complete proteome; Developmental protein; Differentiation;
Disulfide bond; Glycoprotein; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1 15 {ECO:0000255}.
CHAIN 16 498 Angiopoietin-1.
/FTId=PRO_0000009110.
DOMAIN 277 497 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
COILED 81 119 {ECO:0000255}.
COILED 153 261 {ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 286 315 {ECO:0000255|PROSITE-ProRule:PRU00739}.
DISULFID 439 452 {ECO:0000255|PROSITE-ProRule:PRU00739}.
VAR_SEQ 269 269 Missing (in isoform 2).
{ECO:0000303|PubMed:8980223,
ECO:0000303|Ref.2, ECO:0000303|Ref.3}.
/FTId=VSP_046324.
VARIANT 247 247 L -> P (in dbSNP:rs73701083).
/FTId=VAR_069165.
HELIX 286 291 {ECO:0000244|PDB:4EPU}.
STRAND 298 302 {ECO:0000244|PDB:4EPU}.
STRAND 311 316 {ECO:0000244|PDB:4EPU}.
HELIX 319 321 {ECO:0000244|PDB:4EPU}.
STRAND 324 333 {ECO:0000244|PDB:4EPU}.
HELIX 341 346 {ECO:0000244|PDB:4EPU}.
STRAND 353 356 {ECO:0000244|PDB:4EPU}.
HELIX 359 366 {ECO:0000244|PDB:4EPU}.
STRAND 371 378 {ECO:0000244|PDB:4EPU}.
STRAND 384 394 {ECO:0000244|PDB:4EPU}.
HELIX 397 399 {ECO:0000244|PDB:4EPU}.
STRAND 403 412 {ECO:0000244|PDB:4EPU}.
STRAND 433 437 {ECO:0000244|PDB:4EPU}.
HELIX 439 443 {ECO:0000244|PDB:4EPU}.
STRAND 450 452 {ECO:0000244|PDB:4EPU}.
STRAND 454 456 {ECO:0000244|PDB:4EPU}.
TURN 463 467 {ECO:0000244|PDB:4EPU}.
STRAND 473 476 {ECO:0000244|PDB:4EPU}.
TURN 477 479 {ECO:0000244|PDB:4EPU}.
STRAND 487 495 {ECO:0000244|PDB:4EPU}.
SEQUENCE 498 AA; 57513 MW; 5D5FA63AEF6BE920 CRC64;
MTVFLSFAFL AAILTHIGCS NQRRSPENSG RRYNRIQHGQ CAYTFILPEH DGNCRESTTD
QYNTNALQRD APHVEPDFSS QKLQHLEHVM ENYTQWLQKL ENYIVENMKS EMAQIQQNAV
QNHTATMLEI GTSLLSQTAE QTRKLTDVET QVLNQTSRLE IQLLENSLST YKLEKQLLQQ
TNEILKIHEK NSLLEHKILE MEGKHKEELD TLKEEKENLQ GLVTRQTYII QELEKQLNRA
TTNNSVLQKQ QLELMDTVHN LVNLCTKEGV LLKGGKREEE KPFRDCADVY QAGFNKSGIY
TIYINNMPEP KKVFCNMDVN GGGWTVIQHR EDGSLDFQRG WKEYKMGFGN PSGEYWLGNE
FIFAITSQRQ YMLRIELMDW EGNRAYSQYD RFHIGNEKQN YRLYLKGHTG TAGKQSSLIL
HGADFSTKDA DNDNCMCKCA LMLTGGWWFD ACGPSNLNGM FYTAGQNHGK LNGIKWHYFK
GPSYSLRSTT MMIRPLDF


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E1699h ELISA kit ANG-5,Angiopoietin-5,Angiopoietin-like protein 3,Angiopoietin-related protein 3,ANGPT5,ANGPTL3,Homo sapiens,Human,UNQ153_PRO179 96T
U0668m CLIA Agpt4,Ang3,ANG-3,ANG-4,Angiopoietin-3,Angiopoietin-4,Angpt4,Mouse,Mus musculus 96T
E0668m ELISA kit Agpt4,Ang3,ANG-3,ANG-4,Angiopoietin-3,Angiopoietin-4,Angpt4,Mouse,Mus musculus 96T
E0668m ELISA Agpt4,Ang3,ANG-3,ANG-4,Angiopoietin-3,Angiopoietin-4,Angpt4,Mouse,Mus musculus 96T
U0668h CLIA ANG3,ANG-3,ANG4,ANG-4,Angiopoietin-3,Angiopoietin-4,ANGPT4,Homo sapiens,Human 96T
E0668h ELISA kit ANG3,ANG-3,ANG4,ANG-4,Angiopoietin-3,Angiopoietin-4,ANGPT4,Homo sapiens,Human 96T
E0668h ELISA ANG3,ANG-3,ANG4,ANG-4,Angiopoietin-3,Angiopoietin-4,ANGPT4,Homo sapiens,Human 96T
U1919h CLIA kit Angiopoietin-like protein 2,Angiopoietin-related protein 2,ANGPTL2,ARP2,Homo sapiens,Human,UNQ170_PRO196 96T
U1919h CLIA Angiopoietin-like protein 2,Angiopoietin-related protein 2,ANGPTL2,ARP2,Homo sapiens,Human,UNQ170_PRO196 96T
E1919h ELISA kit Angiopoietin-like protein 2,Angiopoietin-related protein 2,ANGPTL2,ARP2,Homo sapiens,Human,UNQ170_PRO196 96T
E1919h ELISA Angiopoietin-like protein 2,Angiopoietin-related protein 2,ANGPTL2,ARP2,Homo sapiens,Human,UNQ170_PRO196 96T
E1919m ELISA Angiopoietin-like protein 2,Angiopoietin-related protein 2,Angptl2,Arp2,Mouse,Mus musculus 96T
U1919m CLIA Angiopoietin-like protein 2,Angiopoietin-related protein 2,Angptl2,Arp2,Mouse,Mus musculus 96T
U1919m CLIA kit Angiopoietin-like protein 2,Angiopoietin-related protein 2,Angptl2,Arp2,Mouse,Mus musculus 96T
E1919m ELISA kit Angiopoietin-like protein 2,Angiopoietin-related protein 2,Angptl2,Arp2,Mouse,Mus musculus 96T
U2085b CLIA Angiopoietin-like protein 4,Angiopoietin-related protein 4,ANGPTL4,Bos taurus,Bovine 96T
E1699m ELISA kit Angiopoietin-like protein 3,Angiopoietin-related protein 3,Angptl3,Mouse,Mus musculus 96T
U2085p CLIA Angiopoietin-like protein 4,Angiopoietin-related protein 4,ANGPTL4,PGAR,Pig,Sus scrofa 96T
U1699m CLIA Angiopoietin-like protein 3,Angiopoietin-related protein 3,Angptl3,Mouse,Mus musculus 96T
E2085p ELISA kit Angiopoietin-like protein 4,Angiopoietin-related protein 4,ANGPTL4,PGAR,Pig,Sus scrofa 96T
E2085b ELISA Angiopoietin-like protein 4,Angiopoietin-related protein 4,ANGPTL4,Bos taurus,Bovine 96T
E1699m ELISA Angiopoietin-like protein 3,Angiopoietin-related protein 3,Angptl3,Mouse,Mus musculus 96T
U2085p CLIA kit Angiopoietin-like protein 4,Angiopoietin-related protein 4,ANGPTL4,PGAR,Pig,Sus scrofa 96T


 

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