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Integrin alpha-IIb (GPalpha IIb) (GPIIb) (Platelet membrane glycoprotein IIb) (CD antigen CD41) [Cleaved into: Integrin alpha-IIb heavy chain; Integrin alpha-IIb light chain, form 1; Integrin alpha-IIb light chain, form 2]

 ITA2B_HUMAN             Reviewed;        1039 AA.
P08514; B2RCY8; O95366; Q14443; Q17R67;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 3.
27-SEP-2017, entry version 220.
RecName: Full=Integrin alpha-IIb;
AltName: Full=GPalpha IIb;
Short=GPIIb;
AltName: Full=Platelet membrane glycoprotein IIb;
AltName: CD_antigen=CD41;
Contains:
RecName: Full=Integrin alpha-IIb heavy chain;
Contains:
RecName: Full=Integrin alpha-IIb light chain, form 1;
Contains:
RecName: Full=Integrin alpha-IIb light chain, form 2;
Flags: Precursor;
Name=ITGA2B; Synonyms=GP2B, ITGAB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-313.
PubMed=2439501;
Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G.,
Surrey S., Schwartz E., Bennett J.S.;
"Structure of the platelet membrane glycoprotein IIb. Homology to the
alpha subunits of the vitronectin and fibronectin membrane
receptors.";
J. Biol. Chem. 262:8476-8482(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-313.
PubMed=2345548; DOI=10.1007/BF00422712;
Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H.,
Marguerie G.;
"GPIIb and GPIIIa amino acid sequences deduced from human
megakaryocyte cDNAs.";
Mol. Biol. Rep. 14:27-33(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=2322558; DOI=10.1021/bi00457a020;
Heidenreich R., Eisman R., Surrey S., Delgrosso K., Bennett J.S.,
Schwartz E., Poncz M.;
"Organization of the gene for platelet glycoprotein IIb.";
Biochemistry 29:1232-1244(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
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 GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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 [GENOMIC DNA] OF 1-62 AND 1021-1039.
PubMed=2845986; DOI=10.1016/S0006-291X(88)80884-2;
Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G.;
"Isolation of the human platelet glycoprotein IIb gene and
characterization of the 5' flanking region.";
Biochem. Biophys. Res. Commun. 156:595-601(1988).
[8]
PROTEIN SEQUENCE OF 32-56 AND 903-917.
PubMed=3534886; DOI=10.1073/pnas.83.21.8351;
Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S.,
Phillips D.R.;
"Platelet glycoproteins IIb and IIIa: evidence for a family of
immunologically and structurally related glycoproteins in mammalian
cells.";
Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986).
[9]
PROTEIN SEQUENCE OF 32-42.
PubMed=1953640; DOI=10.1042/bj2790419;
Catimel B., Parmentier S., Leung L.L., McGregor J.L.;
"Separation of important new platelet glycoproteins (GPIa, GPIc,
GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal
antibodies and gas-phase sequencing.";
Biochem. J. 279:419-425(1991).
[10]
PROTEIN SEQUENCE OF 32 AND 872.
PubMed=8620874; DOI=10.1111/j.1432-1033.1996.0205n.x;
Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V.;
"Thermal stability of individual domains in platelet glycoprotein
IIbIIIa.";
Eur. J. Biochem. 237:205-211(1996).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 392-1039 (ISOFORM 1).
PubMed=3422188; DOI=10.1111/j.1432-1033.1988.tb13762.x;
Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E.,
Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G.;
"cDNA clones for human platelet GPIIb corresponding to mRNA from
megakaryocytes and HEL cells. Evidence for an extensive homology to
other Arg-Gly-Asp adhesion receptors.";
Eur. J. Biochem. 171:87-93(1988).
[12]
PROTEIN SEQUENCE OF 487-501 AND 1026-1038.
PubMed=3801670;
Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.;
"Purification and partial amino acid sequence of human platelet
membrane glycoproteins IIb and IIIa.";
Blood 69:560-564(1987).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 753-1039 (ISOFORM 3), AND TISSUE
SPECIFICITY.
PubMed=9809974;
Trikha M., Cai Y., Grignon D., Honn K.V.;
"Identification of a novel truncated alphaIIb integrin.";
Cancer Res. 58:4771-4775(1998).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 868-1039 (ISOFORM 1).
PubMed=3479442; DOI=10.1172/JCI113277;
Bray P.F., Rosa J.P., Johnston G.I., Shiu D.T., Cook R.G., Lau C.,
Kan Y.W., McEver R.P., Shuman M.A.;
"Platelet glycoprotein IIb. Chromosomal localization and tissue
expression.";
J. Clin. Invest. 80:1812-1817(1987).
[15]
PROTEIN SEQUENCE OF 903-922 AND 934-939.
PubMed=2476117; DOI=10.1042/bj2610551;
Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A.,
Gonzalez-Rodriguez J.;
"Interchain and intrachain disulphide bonds in human platelet
glycoprotein IIb. Localization of the epitopes for several monoclonal
antibodies.";
Biochem. J. 261:551-560(1989).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 938-997 (ISOFORMS 1 AND 2), AND
TISSUE SPECIFICITY.
TISSUE=Erythroleukemia;
PubMed=2351656;
Bray P.F., Leung C.S.-I., Shuman M.A.;
"Human platelets and megakaryocytes contain alternately spliced
glycoprotein IIb mRNAs.";
J. Biol. Chem. 265:9587-9590(1990).
[17]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND GLYCOSYLATION AT
ASN-46; ASN-280; ASN-601 AND ASN-711.
PubMed=2775232; DOI=10.1042/bj2610561;
Calvete J.J., Henschen A., Gonzalez-Rodriguez J.;
"Complete localization of the intrachain disulphide bonds and the N-
glycosylation points in the alpha-subunit of human platelet
glycoprotein IIb.";
Biochem. J. 261:561-568(1989).
[18]
PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT SER-878.
PubMed=7688323; DOI=10.1016/0014-5793(93)80959-X;
Calvete J.J., Muniz-Diaz E.;
"Localization of an O-glycosylation site in the alpha-subunit of the
human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a)
alloantigen expression.";
FEBS Lett. 328:30-34(1993).
[19]
PROTEOLYTIC CLEAVAGE, AND PYROGLUTAMATE FORMATION AT GLN-891.
PubMed=2226834; DOI=10.1016/0014-5793(90)80443-M;
Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J.;
"Characterization of the beta-chain N-terminus heterogeneity and the
alpha-chain C-terminus of human platelet GPIIb. Posttranslational
cleavage sites.";
FEBS Lett. 272:37-40(1990).
[20]
INTERACTION WITH CIB1.
TISSUE=Fetal liver;
PubMed=9030514; DOI=10.1074/jbc.272.8.4651;
Naik U.P., Patel P.M., Parise L.V.;
"Identification of a novel calcium-binding protein that interacts with
the integrin alphaIIb cytoplasmic domain.";
J. Biol. Chem. 272:4651-4654(1997).
[21]
INTERACTION WITH CIB1.
PubMed=10477286; DOI=10.1042/bj3420729;
Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J.,
Parise L.V.;
"Calcium-dependent properties of CIB binding to the integrin alphaIIb
cytoplasmic domain and translocation to the platelet cytoskeleton.";
Biochem. J. 342:729-735(1999).
[22]
MUTAGENESIS OF 1029-PRO-PRO-1030.
PubMed=10212286; DOI=10.1074/jbc.274.18.12945;
Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C.;
"Bidirectional transmembrane modulation of integrin alphaIIbbeta3
conformations.";
J. Biol. Chem. 274:12945-12949(1999).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601.
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).
[24]
INTERACTION WITH RNF181.
PubMed=18331836; DOI=10.1016/j.bbrc.2008.02.142;
Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I.,
Chubb A.J., Treumann A., Moran N.;
"RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR
motif of platelet integrin alpha(IIb)beta3.";
Biochem. Biophys. Res. Commun. 369:1088-1093(2008).
[25]
INTERACTION WITH CIB1.
PubMed=21388953; DOI=10.1074/jbc.M110.179028;
Huang H., Ishida H., Yamniuk A.P., Vogel H.J.;
"Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions
with the platelet integrin alphaIIb cytoplasmic domain.";
J. Biol. Chem. 286:17181-17192(2011).
[26]
INTERACTION WITH CIB1; CIB2; CIB3 AND CIB4.
PubMed=22779914; DOI=10.1139/o2012-021;
Huang H., Bogstie J.N., Vogel H.J.;
"Biophysical and structural studies of the human calcium- and
integrin-binding protein family: understanding their functional
similarities and differences.";
Biochem. Cell Biol. 90:646-656(2012).
[27]
INTERACTION WITH CIB1.
PubMed=22283712; DOI=10.1021/ja2111306;
Huang H., Vogel H.J.;
"Structural basis for the activation of platelet integrin
alphaIIbbeta3 by calcium- and integrin-binding protein 1.";
J. Am. Chem. Soc. 134:3864-3872(2012).
[28]
REVIEW ON GT VARIANTS.
PubMed=7878622;
Bray P.F.;
"Inherited diseases of platelet glycoproteins: considerations for
rapid molecular characterization.";
Thromb. Haemost. 72:492-502(1994).
[29]
VARIANT HPA-3 (BAK).
PubMed=2350579;
Lyman S., Aster R.H., Visentin G.P., Newman P.J.;
"Polymorphism of human platelet membrane glycoprotein IIb associated
with the Baka/Bakb alloantigen system.";
Blood 75:2343-2348(1990).
[30]
VARIANT GT ASP-273.
PubMed=8282784; DOI=10.1172/JCI116942;
Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J.,
Parrella T., Fortina P., Bennett J.S.;
"Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation
adjacent to the first calcium-binding domain of platelet glycoprotein
IIb.";
J. Clin. Invest. 93:172-179(1994).
[31]
VARIANT GT ASP-449.
PubMed=7508443;
Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J.;
"A single amino acid substitution flanking the fourth calcium binding
domain of alpha IIb prevents maturation of the alpha IIb beta 3
integrin complex.";
J. Biol. Chem. 269:4450-4457(1994).
[32]
VARIANT GT HIS-358.
PubMed=7706461; DOI=10.1172/JCI117828;
Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J.;
"Glanzmann thrombasthenia resulting from a single amino acid
substitution between the second and third calcium-binding domains of
GPIIb. Role of the GPIIb amino terminus in integrin subunit
association.";
J. Clin. Invest. 95:1553-1560(1995).
[33]
VARIANT GT VAL-456-457-ASP DEL, AND CHARACTERIZATION OF VARIANT GT
VAL-456-457-ASP DEL.
PubMed=8704171;
Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S.,
Poncz M.;
"Glanzmann thrombasthenia due to a two amino acid deletion in the
fourth calcium-binding domain of alpha IIb: demonstration of the
importance of calcium-binding domains in the conformation of alpha IIb
beta 3.";
Blood 88:167-173(1996).
[34]
VARIANTS GT ILE-207; THR-596 AND GLN-1026.
PubMed=9215749; DOI=10.1006/bcmd.1997.0117;
French D.L., Coller B.S.;
"Hematologically important mutations: Glanzmann thrombasthenia.";
Blood Cells Mol. Dis. 23:39-51(1997).
[35]
VARIANT GT PRO-214, AND CHARACTERIZATION OF VARIANT GT PRO-214.
PubMed=9473221;
Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L.;
"Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia
with both quantitative and qualitative abnormalities in GPIIb/IIIa.";
Blood 91:1562-1571(1998).
[36]
VARIANT GT PRO-778.
PubMed=9763559;
Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M.,
Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y.;
"A Gln747-->Pro substitution in the IIb subunit is responsible for a
moderate IIbbeta3 deficiency in Glanzmann thrombasthenia.";
Blood 92:2750-2758(1998).
[37]
VARIANT BDPLT16 GLN-1026, AND CHARACTERIZATION OF VARIANT BDPLT16
GLN-1026.
PubMed=9834222;
Peyruchaud O., Nurden A.T., Milet S., Macchi L., Pannochia A.,
Bray P.F., Kieffer N., Bourre F.;
"R to Q amino acid substitution in the GFFKR sequence of the
cytoplasmic domain of the integrin IIb subunit in a patient with a
Glanzmann's thrombasthenia-like syndrome.";
Blood 92:4178-4187(1998).
[38]
VARIANTS GT SER-320; LYS-355 AND PRO-778.
PubMed=9722314; DOI=10.1046/j.1365-2141.1998.00824.x;
Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y.,
Ikeda Y.;
"Novel point mutations in the alphaIIb subunit (Phe289-->Ser,
Glu324-->Lys and Gln747-->Pro) causing thrombasthenic phenotypes in
four Japanese patients.";
Br. J. Haematol. 102:829-840(1998).
[39]
VARIANTS GT LYS-355 AND THR-596.
PubMed=9734640; DOI=10.1046/j.1365-2141.1998.00852.x;
Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K.,
Bourre F., Nurden A.T.;
"Double heterozygosity of the GPIIb gene in a Swiss patient with
Glanzmann's thrombasthenia.";
Br. J. Haematol. 102:918-925(1998).
[40]
VARIANTS ILE-40; SER-874 AND ASN-968, AND POLYMORPHISM.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[41]
VARIANT GT ARG-705, AND CHARACTERIZATION OF VARIANT GT ARG-705.
PubMed=9920835;
Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G.,
Ferrer M., Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R.;
"Molecular genetic analysis of a compound heterozygote for the
glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia:
disruption of the 674-687 disulfide bridge in GPIIb prevents surface
exposure of GPIIb-IIIa complexes.";
Blood 93:866-875(1999).
[42]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[43]
VARIANTS GT ALA-176 AND LEU-176.
PubMed=10607701;
Basani R.B., French D.L., Vilaire G., Brown D.L., Chen F.,
Coller B.S., Derrick J.M., Gartner T.K., Bennett J.S., Poncz M.;
"A naturally occurring mutation near the amino terminus of alphaIIb
defines a new region involved in ligand binding to alphaIIbbeta3.";
Blood 95:180-188(2000).
[44]
VARIANTS GT TRP-161; LEU-222; ARG-412 AND PRO-847.
PubMed=11798398; DOI=10.1080/095371001317126383;
Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M.,
Negrier C.;
"Description of 10 new mutations in platelet glycoprotein IIb
(alphaIIb) and glycoprotein IIIa (beta3) genes.";
Platelets 12:486-495(2001).
[45]
VARIANT GT PRO-86, AND CHARACTERIZATION OF VARIANT GT PRO-86.
PubMed=12181054; DOI=10.1046/j.1365-2141.2002.03678.x;
Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S.,
Bourre F., Tani Y.;
"A Leu55 to Pro substitution in the integrin alphaIIb is responsible
for a case of Glanzmann's thrombasthenia.";
Br. J. Haematol. 118:833-835(2002).
[46]
VARIANTS GT VAL-139; ALA-176; GLU-267; ASP-380; THR-405; ASP-581;
ARG-705; VAL-752 AND PRO-755.
PubMed=12083483;
D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G.,
Margaglione M.;
"Glanzmann's thrombasthenia: identification of 19 new mutations in 30
patients.";
Thromb. Haemost. 87:1034-1042(2002).
[47]
VARIANTS GT PHE-329 AND THR-405, AND CHARACTERIZATION OF VARIANTS GT
PHE-329 AND THR-405.
PubMed=12424194; DOI=10.1182/blood-2002-07-2266;
Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J.,
Coller B.S., French D.L.;
"Two novel mutations in the alpha IIb calcium-binding domains identify
hydrophobic regions essential for alpha IIbbeta 3 biogenesis.";
Blood 101:2268-2276(2003).
[48]
VARIANT GT HIS-174, AND CHARACTERIZATION OF VARIANT GT HIS-174.
PubMed=12506038; DOI=10.1182/blood-2002-07-2144;
Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H.,
Kosugi S., Kato H., Kurata Y., Matsuzawa Y.;
"A naturally occurring Tyr143His alpha IIb mutation abolishes alpha
IIb beta 3 function for soluble ligands but retains its ability for
mediating cell adhesion and clot retraction: comparison with other
mutations causing ligand-binding defects.";
Blood 101:3485-3491(2003).
[49]
VARIANT GT MET-982, CHARACTERIZATION OF VARIANT GT MET-982, AND
VARIANT THR-989.
PubMed=15099289; DOI=10.1046/j.1538-7836.2004.00711.x;
Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J.,
Blanchette V.S., Schmugge M., Rand M.L.;
"Triple heterozygosity in the integrin alphaIIb subunit in a patient
with Glanzmann's thrombasthenia.";
J. Thromb. Haemost. 2:813-819(2004).
[50]
VARIANT GT CYS-202, AND CHARACTERIZATION OF VARIANT GT CYS-202.
PubMed=15219201; DOI=10.1111/j.1538-7836.2004.00758.x;
Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U.;
"A novel Phe171Cys mutation in integrin alpha causes Glanzmann
thrombasthenia by abrogating alphaIIbbeta3 complex formation.";
J. Thromb. Haemost. 2:1167-1175(2004).
[51]
VARIANT GT LEU-943, AND CHARACTERIZATION OF VARIANT GT LEU-943.
PubMed=17018384;
Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C.;
"Type II Glanzmann thrombasthenia in a compound heterozygote for the
alpha IIb gene. A novel missense mutation in exon 27.";
Haematologica 91:1352-1359(2006).
[52]
VARIANTS GT THR-405; THR-596; ARG-705; PRO-778; PHE-934; LEU-957;
MET-982 AND THR-989, AND CHARACTERIZATION OF VARIANTS GT PHE-934 AND
LEU-957.
PubMed=20020534; DOI=10.1002/humu.21179;
Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N.,
Goudemand J., de Brevern A.G., Kaplan C.;
"AlphaIIbbeta3 integrin: new allelic variants in Glanzmann
thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression,
and structure-function.";
Hum. Mutat. 31:237-246(2010).
[53]
VARIANT BDPLT16 TRP-1026, AND CHARACTERIZATION OF VARIANT BDPLT16
TRP-1026.
PubMed=21454453; DOI=10.1182/blood-2010-12-323691;
Kunishima S., Kashiwagi H., Otsu M., Takayama N., Eto K., Onodera M.,
Miyajima Y., Takamatsu Y., Suzumiya J., Matsubara K., Tomiyama Y.,
Saito H.;
"Heterozygous ITGA2B R995W mutation inducing constitutive activation
of the alphaIIbbeta3 receptor affects proplatelet formation and causes
congenital macrothrombocytopenia.";
Blood 117:5479-5484(2011).
-!- FUNCTION: Integrin alpha-IIb/beta-3 is a receptor for fibronectin,
fibrinogen, plasminogen, prothrombin, thrombospondin and
vitronectin. It recognizes the sequence R-G-D in a wide array of
ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in
fibrinogen gamma chain. Following activation integrin alpha-
IIb/beta-3 brings about platelet/platelet interaction through
binding of soluble fibrinogen. This step leads to rapid platelet
aggregation which physically plugs ruptured endothelial cell
surface.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit is composed of a heavy and a light chain linked by a
disulfide bond. Alpha-IIb associates with beta-3. Directly
interacts with RNF181. Interacts (via C-terminus cytoplasmic tail
region) with CIB1; the interaction is direct and calcium-
dependent. Interacts (via C-terminus cytoplasmic tail region) with
CIB2, CIB3 and CIB4; the interactions are stabilized/increased in
a calcium and magnesium-dependent manner.
{ECO:0000269|PubMed:10477286, ECO:0000269|PubMed:18331836,
ECO:0000269|PubMed:21388953, ECO:0000269|PubMed:22283712,
ECO:0000269|PubMed:22779914, ECO:0000269|PubMed:9030514}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-702693, EBI-702693;
P05106:ITGB3; NbExp=11; IntAct=EBI-702693, EBI-702847;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P08514-1; Sequence=Displayed;
Name=2;
IsoId=P08514-2; Sequence=VSP_002737;
Name=3; Synonyms=tr-alpha-IIb {ECO:0000303|PubMed:9809974};
IsoId=P08514-3; Sequence=VSP_002736;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in
platelets and megakaryocytes, but not in reticulocytes. Not
detected in Jurkat, nor in U937 cell lines (PubMed:2351656).
Isoform 3 is expressed in prostate adenocarcinoma, as well as in
several erythroleukemia, prostate adenocarcinoma and melanoma cell
lines, including PC-3, DU-145, HEL, WM983A, WM983B and WM35. Not
detected in platelets, nor in normal prostate (at protein level)
(PubMed:9809974). {ECO:0000269|PubMed:2351656,
ECO:0000269|PubMed:9809974}.
-!- POLYMORPHISM: Position 874 is associated with platelet-specific
alloantigen HPA-3/BAK/LEK. HPA-3A/BAK(A)/LEK(A) has Ile-874 and
HPA-3B/BAK(B)/LEK(B) has Ser-874. HPA-3B is involved in neonatal
alloimmune thrombocytopenia (NAIT or NATP).
{ECO:0000269|PubMed:10391209}.
-!- DISEASE: Glanzmann thrombasthenia (GT) [MIM:273800]: A common
inherited disease of platelet aggregation. It is characterized by
mucocutaneous bleeding of mild-to-moderate severity. GT has been
classified clinically into types I and II. In type I, platelets
show absence of the glycoprotein IIb-IIIa complexes at their
surface and lack fibrinogen and clot retraction capability. In
type II, the platelets express the GPIIb-IIIa complex at reduced
levels, have detectable amounts of fibrinogen, and have low or
moderate clot retraction capability. {ECO:0000269|PubMed:10607701,
ECO:0000269|PubMed:11798398, ECO:0000269|PubMed:12083483,
ECO:0000269|PubMed:12181054, ECO:0000269|PubMed:12424194,
ECO:0000269|PubMed:12506038, ECO:0000269|PubMed:15099289,
ECO:0000269|PubMed:15219201, ECO:0000269|PubMed:17018384,
ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:7508443,
ECO:0000269|PubMed:7706461, ECO:0000269|PubMed:8282784,
ECO:0000269|PubMed:8704171, ECO:0000269|PubMed:9215749,
ECO:0000269|PubMed:9473221, ECO:0000269|PubMed:9722314,
ECO:0000269|PubMed:9734640, ECO:0000269|PubMed:9763559,
ECO:0000269|PubMed:9920835}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Bleeding disorder, platelet-type 16 (BDPLT16)
[MIM:187800]: An autosomal dominant form of congenital
macrothrombocytopenia associated with platelet anisocytosis. It is
a disorder of platelet production. Affected individuals may have
no or only mildly increased bleeding tendency. In vitro studies
show mild platelet functional abnormalities.
{ECO:0000269|PubMed:21454453, ECO:0000269|PubMed:9834222}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02764; AAA60114.1; -; mRNA.
EMBL; M34480; AAA35926.1; -; mRNA.
EMBL; M34344; AAA53150.1; -; Genomic_DNA.
EMBL; M33319; AAA53150.1; JOINED; Genomic_DNA.
EMBL; M33320; AAA53150.1; JOINED; Genomic_DNA.
EMBL; AK315335; BAG37735.1; -; mRNA.
EMBL; AC003043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC117443; AAI17444.1; -; mRNA.
EMBL; BC126442; AAI26443.1; -; mRNA.
EMBL; M22568; AAA52587.1; -; Genomic_DNA.
EMBL; M22569; AAA52588.1; -; Genomic_DNA.
EMBL; X06831; CAA29987.1; -; mRNA.
EMBL; AF098114; AAC98507.1; -; mRNA.
EMBL; M18085; AAA52597.1; -; mRNA.
EMBL; M54799; AAA52599.1; -; Genomic_DNA.
CCDS; CCDS32665.1; -. [P08514-1]
PIR; A34269; A34269.
RefSeq; NP_000410.2; NM_000419.4. [P08514-1]
RefSeq; XP_011523051.1; XM_011524749.1. [P08514-2]
UniGene; Hs.411312; -.
PDB; 1DPK; NMR; -; A=1020-1039.
PDB; 1DPQ; NMR; -; A=1020-1039.
PDB; 1JX5; Model; -; A=32-483.
PDB; 1KUP; NMR; -; A=1018-1028.
PDB; 1KUZ; NMR; -; A=1018-1028.
PDB; 1M8O; NMR; -; A=1020-1039.
PDB; 1RN0; Model; -; A=32-482.
PDB; 1S4W; NMR; -; A=1020-1039.
PDB; 1TYE; X-ray; 2.90 A; A/C/E=32-483.
PDB; 1UV9; Model; -; A=32-973.
PDB; 2K1A; NMR; -; A=989-1029.
PDB; 2K9J; NMR; -; A=989-1029.
PDB; 2KNC; NMR; -; A=991-1039.
PDB; 2MTP; NMR; -; B=1019-1039.
PDB; 2N9Y; NMR; -; A=989-1029.
PDB; 2VC2; X-ray; 3.10 A; A=32-483.
PDB; 2VDK; X-ray; 2.80 A; A=32-483.
PDB; 2VDL; X-ray; 2.75 A; A=32-483.
PDB; 2VDM; X-ray; 2.90 A; A=32-483.
PDB; 2VDN; X-ray; 2.90 A; A=32-483.
PDB; 2VDO; X-ray; 2.51 A; A=32-483.
PDB; 2VDP; X-ray; 2.80 A; A=32-483.
PDB; 2VDQ; X-ray; 2.59 A; A=32-483.
PDB; 2VDR; X-ray; 2.40 A; A=32-483.
PDB; 3FCS; X-ray; 2.55 A; A/C=32-989.
PDB; 3FCU; X-ray; 2.90 A; A/C/E=32-488.
PDB; 3NID; X-ray; 2.30 A; A/C=32-488.
PDB; 3NIF; X-ray; 2.40 A; A/C=32-488.
PDB; 3NIG; X-ray; 2.25 A; A/C=32-488.
PDB; 3T3M; X-ray; 2.60 A; A/C=32-488.
PDB; 3T3P; X-ray; 2.20 A; A/C=32-488.
PDB; 3ZDX; X-ray; 2.45 A; A/C=32-488.
PDB; 3ZDY; X-ray; 2.45 A; A/C=32-488.
PDB; 3ZDZ; X-ray; 2.75 A; A/C=32-488.
PDB; 3ZE0; X-ray; 2.95 A; A/C=32-488.
PDB; 3ZE1; X-ray; 3.00 A; A/C=32-488.
PDB; 3ZE2; X-ray; 2.35 A; A/C=32-488.
PDB; 4CAK; EM; 20.50 A; A=32-989.
PDB; 4Z7N; X-ray; 2.60 A; A/C=32-486.
PDB; 4Z7O; X-ray; 2.85 A; A/C=32-486.
PDB; 4Z7Q; X-ray; 2.70 A; A/C=32-485.
PDB; 5HDB; X-ray; 2.70 A; A/C=32-485.
PDBsum; 1DPK; -.
PDBsum; 1DPQ; -.
PDBsum; 1JX5; -.
PDBsum; 1KUP; -.
PDBsum; 1KUZ; -.
PDBsum; 1M8O; -.
PDBsum; 1RN0; -.
PDBsum; 1S4W; -.
PDBsum; 1TYE; -.
PDBsum; 1UV9; -.
PDBsum; 2K1A; -.
PDBsum; 2K9J; -.
PDBsum; 2KNC; -.
PDBsum; 2MTP; -.
PDBsum; 2N9Y; -.
PDBsum; 2VC2; -.
PDBsum; 2VDK; -.
PDBsum; 2VDL; -.
PDBsum; 2VDM; -.
PDBsum; 2VDN; -.
PDBsum; 2VDO; -.
PDBsum; 2VDP; -.
PDBsum; 2VDQ; -.
PDBsum; 2VDR; -.
PDBsum; 3FCS; -.
PDBsum; 3FCU; -.
PDBsum; 3NID; -.
PDBsum; 3NIF; -.
PDBsum; 3NIG; -.
PDBsum; 3T3M; -.
PDBsum; 3T3P; -.
PDBsum; 3ZDX; -.
PDBsum; 3ZDY; -.
PDBsum; 3ZDZ; -.
PDBsum; 3ZE0; -.
PDBsum; 3ZE1; -.
PDBsum; 3ZE2; -.
PDBsum; 4CAK; -.
PDBsum; 4Z7N; -.
PDBsum; 4Z7O; -.
PDBsum; 4Z7Q; -.
PDBsum; 5HDB; -.
ProteinModelPortal; P08514; -.
SMR; P08514; -.
BioGrid; 109881; 13.
CORUM; P08514; -.
DIP; DIP-68N; -.
IntAct; P08514; 2.
STRING; 9606.ENSP00000262407; -.
BindingDB; P08514; -.
ChEMBL; CHEMBL212; -.
DrugBank; DB00054; Abciximab.
DrugBank; DB04863; Lefradafiban.
DrugBank; DB00775; Tirofiban.
GuidetoPHARMACOLOGY; 2440; -.
iPTMnet; P08514; -.
PhosphoSitePlus; P08514; -.
BioMuta; ITGA2B; -.
DMDM; 226694183; -.
OGP; P08514; -.
EPD; P08514; -.
PaxDb; P08514; -.
PeptideAtlas; P08514; -.
PRIDE; P08514; -.
TopDownProteomics; P08514-1; -. [P08514-1]
Ensembl; ENST00000262407; ENSP00000262407; ENSG00000005961. [P08514-1]
GeneID; 3674; -.
KEGG; hsa:3674; -.
UCSC; uc002igt.2; human. [P08514-1]
CTD; 3674; -.
DisGeNET; 3674; -.
EuPathDB; HostDB:ENSG00000005961.17; -.
GeneCards; ITGA2B; -.
HGNC; HGNC:6138; ITGA2B.
HPA; CAB018611; -.
HPA; HPA031168; -.
HPA; HPA031169; -.
HPA; HPA031170; -.
HPA; HPA031171; -.
MalaCards; ITGA2B; -.
MIM; 187800; phenotype.
MIM; 273800; phenotype.
MIM; 607759; gene.
neXtProt; NX_P08514; -.
OpenTargets; ENSG00000005961; -.
Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
Orphanet; 849; Glanzmann thrombasthenia.
PharmGKB; PA29938; -.
eggNOG; KOG3637; Eukaryota.
eggNOG; ENOG410XPVZ; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000231603; -.
HOVERGEN; HBG006186; -.
InParanoid; P08514; -.
KO; K06476; -.
OMA; LWLLEWV; -.
OrthoDB; EOG091G05Z4; -.
PhylomeDB; P08514; -.
TreeFam; TF105391; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
SignaLink; P08514; -.
SIGNOR; P08514; -.
ChiTaRS; ITGA2B; human.
EvolutionaryTrace; P08514; -.
GeneWiki; ITGA2B; -.
GenomeRNAi; 3674; -.
PMAP-CutDB; Q17R67; -.
PRO; PR:P08514; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000005961; -.
CleanEx; HS_ITGA2B; -.
ExpressionAtlas; P08514; baseline and differential.
Genevisible; P08514; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0008305; C:integrin complex; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
GO; GO:0070051; F:fibrinogen binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF00357; Integrin_alpha; 1.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Integrin; Membrane; Metal-binding; Polymorphism;
Pyrrolidone carboxylic acid; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000269|PubMed:1953640,
ECO:0000269|PubMed:3534886,
ECO:0000269|PubMed:8620874}.
CHAIN 32 1039 Integrin alpha-IIb.
/FTId=PRO_0000016275.
CHAIN 32 887 Integrin alpha-IIb heavy chain.
/FTId=PRO_0000016276.
CHAIN 891 1039 Integrin alpha-IIb light chain, form 1.
/FTId=PRO_0000292348.
CHAIN 903 1039 Integrin alpha-IIb light chain, form 2.
/FTId=PRO_0000016277.
TOPO_DOM 32 993 Extracellular. {ECO:0000255}.
TRANSMEM 994 1019 Helical. {ECO:0000255}.
TOPO_DOM 1020 1039 Cytoplasmic. {ECO:0000255}.
REPEAT 35 96 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 110 173 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 187 238 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 251 305 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 306 371 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 373 432 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 435 496 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 274 282 {ECO:0000255}.
CA_BIND 328 336 {ECO:0000255}.
CA_BIND 396 404 {ECO:0000255}.
CA_BIND 457 465 {ECO:0000255}.
MOTIF 1022 1026 GFFKR motif.
MOD_RES 891 891 Pyrrolidone carboxylic acid; in light
chain form 1.
{ECO:0000269|PubMed:2226834}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2775232}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2775232}.
CARBOHYD 601 601 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:2775232}.
CARBOHYD 711 711 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2775232}.
CARBOHYD 874 874 O-linked (GalNAc...) serine; in variant
S-874.
CARBOHYD 878 878 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:7688323}.
CARBOHYD 962 962 N-linked (GlcNAc...) asparagine.
DISULFID 87 96 {ECO:0000269|PubMed:2775232}.
DISULFID 138 161 {ECO:0000269|PubMed:2775232}.
DISULFID 177 198 {ECO:0000269|PubMed:2775232}.
DISULFID 504 515 {ECO:0000269|PubMed:2775232}.
DISULFID 521 576 {ECO:0000269|PubMed:2775232}.
DISULFID 633 639 {ECO:0000269|PubMed:2775232}.
DISULFID 705 718 {ECO:0000269|PubMed:2775232}.
DISULFID 857 911 Interchain (between heavy and light
chains). {ECO:0000269|PubMed:2775232}.
DISULFID 916 921 {ECO:0000269|PubMed:2775232}.
VAR_SEQ 910 1039 SCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPL
DQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALE
ERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFFKRNRPPLE
EDDEEGE -> VSRLSGLWPGLPGTHGAEGMGGGRGVRVCC
GPLWATLGPWEHFK (in isoform 3).
{ECO:0000305}.
/FTId=VSP_002736.
VAR_SEQ 948 981 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_002737.
VARIANT 40 40 T -> I (in dbSNP:rs5915).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014176.
VARIANT 86 86 L -> P (in GT; cells co-transfected with
mutated alpha-IIb and wild-type beta-3
scarcely expressed the alpha-IIb/beta-3
complex). {ECO:0000269|PubMed:12181054}.
/FTId=VAR_030445.
VARIANT 139 139 A -> V (in GT).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030446.
VARIANT 161 161 C -> W (in GT).
{ECO:0000269|PubMed:11798398}.
/FTId=VAR_030447.
VARIANT 174 174 Y -> H (in GT; abolishes the binding
function of alpha-IIb/beta-3 for soluble
ligands without disturbing alpha-IIb/
beta-3 expression; functional defect is
likely caused by its allosteric effect
rather than by a defect in the ligand-
binding site itself).
{ECO:0000269|PubMed:12506038}.
/FTId=VAR_030448.
VARIANT 176 176 P -> A (in GT; impairs surface expression
of alpha-IIb/beta-3 and abrogates ligand
binding to the activated integrin).
{ECO:0000269|PubMed:10607701,
ECO:0000269|PubMed:12083483}.
/FTId=VAR_009885.
VARIANT 176 176 P -> L (in GT; impairs surface expression
of alpha-IIb/beta-3).
{ECO:0000269|PubMed:10607701}.
/FTId=VAR_009886.
VARIANT 202 202 F -> C (in GT; associated with abrogation
of alpha-IIb/beta-3 complex formation).
{ECO:0000269|PubMed:15219201}.
/FTId=VAR_030449.
VARIANT 207 207 T -> I (in GT).
{ECO:0000269|PubMed:9215749}.
/FTId=VAR_030450.
VARIANT 214 214 L -> P (in GT; disrupts the structural
conformation and the ligand binding
properties of the heterodimeric complex;
in addition the mutation appears to
confer susceptibility to proteolysis;
dbSNP:rs137852911).
{ECO:0000269|PubMed:9473221}.
/FTId=VAR_030451.
VARIANT 222 222 F -> L (in GT).
{ECO:0000269|PubMed:11798398}.
/FTId=VAR_030452.
VARIANT 267 267 G -> E (in GT).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030453.
VARIANT 273 273 G -> D (in GT; alters the heterodimer
conformation thus impairing their
intracellular transport;
dbSNP:rs137852907).
{ECO:0000269|PubMed:8282784}.
/FTId=VAR_003979.
VARIANT 313 313 G -> A (in dbSNP:rs1126554).
{ECO:0000269|PubMed:2345548,
ECO:0000269|PubMed:2439501}.
/FTId=VAR_054820.
VARIANT 320 320 F -> S (in GT; type I; impairs surface
expression of alpha-IIb/beta-3).
{ECO:0000269|PubMed:9722314}.
/FTId=VAR_009887.
VARIANT 329 329 V -> F (in GT; expression of mutant
subunit alpha-IIb/bet-3 is 28% of
control; mutant pro-alpha-IIb subunit is
retained in the endoplasmic reticulum).
{ECO:0000269|PubMed:12424194}.
/FTId=VAR_030454.
VARIANT 355 355 E -> K (in GT; type I; impairs surface
expression of alpha-IIb/beta-3;
dbSNP:rs137852910).
{ECO:0000269|PubMed:9722314,
ECO:0000269|PubMed:9734640}.
/FTId=VAR_009888.
VARIANT 358 358 R -> H (in GT; type II;
dbSNP:rs137852908).
{ECO:0000269|PubMed:7706461}.
/FTId=VAR_003980.
VARIANT 380 380 G -> D (in GT; dbSNP:rs766006685).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030455.
VARIANT 405 405 I -> T (in GT; expression of mutant
subunit alpha-IIb/bet-3 is 11% of
control; mutant pro-alpha-IIb subunit is
retained in the endoplasmic reticulum;
dbSNP:rs75622274).
{ECO:0000269|PubMed:12083483,
ECO:0000269|PubMed:12424194,
ECO:0000269|PubMed:20020534}.
/FTId=VAR_030456.
VARIANT 412 412 G -> R (in GT; dbSNP:rs780786843).
{ECO:0000269|PubMed:11798398}.
/FTId=VAR_030457.
VARIANT 449 449 G -> D (in GT; type I).
{ECO:0000269|PubMed:7508443}.
/FTId=VAR_003981.
VARIANT 456 457 Missing (in GT; alteres the conformation
of heterodimers such that they were
neither recognized by the heterodimer-
specific antibody A2A9 nor able to
undergo further intracellular processing
or transport to the cell surface).
/FTId=VAR_030458.
VARIANT 581 581 A -> D (in GT).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030459.
VARIANT 596 596 I -> T (in GT; type I; dbSNP:rs76811038).
{ECO:0000269|PubMed:20020534,
ECO:0000269|PubMed:9215749,
ECO:0000269|PubMed:9734640}.
/FTId=VAR_030460.
VARIANT 649 649 V -> L (in dbSNP:rs7207402).
/FTId=VAR_054821.
VARIANT 705 705 C -> R (in GT; type II; the rate of
subunit maturation and the surface
exposure of ghlycoprotein IIb/beta-3 are
strongly reduced; dbSNP:rs77961246).
{ECO:0000269|PubMed:12083483,
ECO:0000269|PubMed:20020534,
ECO:0000269|PubMed:9920835}.
/FTId=VAR_030461.
VARIANT 752 752 L -> V (in GT; dbSNP:rs761174160).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030462.
VARIANT 755 755 R -> P (in GT; dbSNP:rs763762304).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030463.
VARIANT 778 778 Q -> P (in GT; type II;
dbSNP:rs74475415).
{ECO:0000269|PubMed:20020534,
ECO:0000269|PubMed:9722314,
ECO:0000269|PubMed:9763559}.
/FTId=VAR_003982.
VARIANT 847 847 L -> P (in GT).
{ECO:0000269|PubMed:11798398}.
/FTId=VAR_030464.
VARIANT 874 874 I -> S (alloantigen HPA-3B;
dbSNP:rs5911).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_003983.
VARIANT 934 934 V -> F (in GT; severe type 1 phenotype;
the mutation prevented normal ITGA2B/
ITGB3 complex expression on the cell
surface; dbSNP:rs77458039).
{ECO:0000269|PubMed:20020534}.
/FTId=VAR_069917.
VARIANT 943 943 P -> L (in GT; marked reduction in the
rate of surface expression).
{ECO:0000269|PubMed:17018384}.
/FTId=VAR_030465.
VARIANT 957 957 S -> L (in GT; severe type 1 phenotype;
the mutation prevented normal ITGA2B/
ITGB3 complex expression on the cell
surface; the mutation may interfere with
correct folding of the protein;
dbSNP:rs80002943).
{ECO:0000269|PubMed:20020534}.
/FTId=VAR_069918.
VARIANT 968 968 Y -> N (in dbSNP:rs5914).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014177.
VARIANT 982 982 V -> M (in GT; much reduced surface
expression of alpha-IIb/beta-3 and a
block in the maturation of pro-alpha-IIb;
dbSNP:rs78657866).
{ECO:0000269|PubMed:15099289,
ECO:0000269|PubMed:20020534}.
/FTId=VAR_030466.
VARIANT 989 989 A -> T (in dbSNP:rs78165611).
{ECO:0000269|PubMed:15099289,
ECO:0000269|PubMed:20020534}.
/FTId=VAR_030467.
VARIANT 1026 1026 R -> Q (in GT and BDPLT16; results in low
surface expression of the mutant protein;
dbSNP:rs879255514).
{ECO:0000269|PubMed:9215749,
ECO:0000269|PubMed:9834222}.
/FTId=VAR_030468.
VARIANT 1026 1026 R -> W (in BDPLT16; results in abnormal
membrane ruffling and cytoplasmic
protrusions as well as defective
proplatelet formation).
{ECO:0000269|PubMed:21454453}.
/FTId=VAR_069919.
MUTAGEN 1029 1030 PP->AA: Imparts constitutive activity
(ligand-binding) to alpha-IIb/beta-3.
{ECO:0000269|PubMed:10212286}.
CONFLICT 23 23 P -> A (in Ref. 2; AAA35926).
{ECO:0000305}.
CONFLICT 120 120 A -> S (in Ref. 4; BAG37735).
{ECO:0000305}.
CONFLICT 287 288 GA -> VP (in Ref. 3; AAA53150).
{ECO:0000305}.
CONFLICT 346 346 E -> D (in Ref. 2; AAA35926).
{ECO:0000305}.
CONFLICT 565 565 N -> D (in Ref. 2; AAA35926).
{ECO:0000305}.
CONFLICT 566 566 L -> V (in Ref. 11; CAA29987).
{ECO:0000305}.
CONFLICT 633 633 C -> S (in Ref. 1; AAA60114).
{ECO:0000305}.
CONFLICT 729 729 Q -> E (in Ref. 11; CAA29987).
{ECO:0000305}.
CONFLICT 971 971 P -> A (in Ref. 3; AAA53150).
{ECO:0000305}.
CONFLICT 1029 1029 P -> H (in Ref. 2; AAA35926 and 7;
AAA52588). {ECO:0000305}.
CONFLICT 1030 1030 P -> T (in Ref. 7; AAA52588).
{ECO:0000305}.
STRAND 36 38 {ECO:0000244|PDB:3T3P}.
STRAND 40 43 {ECO:0000244|PDB:3T3P}.
STRAND 52 58 {ECO:0000244|PDB:3T3P}.
STRAND 60 62 {ECO:0000244|PDB:1TYE}.
STRAND 64 70 {ECO:0000244|PDB:3T3P}.
STRAND 78 80 {ECO:0000244|PDB:3T3P}.
STRAND 82 88 {ECO:0000244|PDB:3T3P}.
STRAND 93 95 {ECO:0000244|PDB:3FCS}.
STRAND 107 110 {ECO:0000244|PDB:3T3P}.
STRAND 113 118 {ECO:0000244|PDB:3T3P}.
STRAND 126 131 {ECO:0000244|PDB:3T3P}.
STRAND 134 139 {ECO:0000244|PDB:3T3P}.
STRAND 143 148 {ECO:0000244|PDB:3T3P}.
STRAND 151 153 {ECO:0000244|PDB:2VDL}.
STRAND 160 164 {ECO:0000244|PDB:3T3P}.
TURN 166 168 {ECO:0000244|PDB:3T3P}.
STRAND 171 174 {ECO:0000244|PDB:3T3P}.
HELIX 183 188 {ECO:0000244|PDB:3T3P}.
TURN 189 193 {ECO:0000244|PDB:3T3P}.
STRAND 202 206 {ECO:0000244|PDB:3T3P}.
STRAND 211 216 {ECO:0000244|PDB:3T3P}.
HELIX 219 222 {ECO:0000244|PDB:3T3P}.
STRAND 225 230 {ECO:0000244|PDB:3T3P}.
HELIX 231 237 {ECO:0000244|PDB:3T3P}.
HELIX 259 261 {ECO:0000244|PDB:3T3P}.
STRAND 268 273 {ECO:0000244|PDB:3T3P}.
STRAND 279 281 {ECO:0000244|PDB:3FCS}.
STRAND 283 288 {ECO:0000244|PDB:3T3P}.
HELIX 291 294 {ECO:0000244|PDB:3T3P}.
STRAND 297 301 {ECO:0000244|PDB:3T3P}.
STRAND 307 312 {ECO:0000244|PDB:3T3P}.
STRAND 324 327 {ECO:0000244|PDB:3T3P}.
STRAND 330 333 {ECO:0000244|PDB:3T3P}.
STRAND 336 341 {ECO:0000244|PDB:3T3P}.
STRAND 345 348 {ECO:0000244|PDB:3T3P}.
TURN 349 351 {ECO:0000244|PDB:3T3P}.
STRAND 352 355 {ECO:0000244|PDB:3T3P}.
STRAND 358 362 {ECO:0000244|PDB:3T3P}.
STRAND 366 368 {ECO:0000244|PDB:3T3P}.
STRAND 375 379 {ECO:0000244|PDB:3T3P}.
STRAND 391 395 {ECO:0000244|PDB:3T3P}.
STRAND 400 402 {ECO:0000244|PDB:3T3P}.
STRAND 404 409 {ECO:0000244|PDB:3T3P}.
STRAND 413 417 {ECO:0000244|PDB:1TYE}.
STRAND 419 423 {ECO:0000244|PDB:3T3P}.
STRAND 427 430 {ECO:0000244|PDB:1TYE}.
STRAND 435 439 {ECO:0000244|PDB:3T3P}.
STRAND 450 456 {ECO:0000244|PDB:3T3P}.
STRAND 458 463 {ECO:0000244|PDB:3T3P}.
STRAND 465 470 {ECO:0000244|PDB:3T3P}.
HELIX 471 473 {ECO:0000244|PDB:3T3P}.
STRAND 475 479 {ECO:0000244|PDB:3T3P}.
STRAND 484 493 {ECO:0000244|PDB:3FCS}.
STRAND 507 509 {ECO:0000244|PDB:3FCS}.
STRAND 512 525 {ECO:0000244|PDB:3FCS}.
STRAND 534 541 {ECO:0000244|PDB:3FCS}.
TURN 542 544 {ECO:0000244|PDB:3FCS}.
HELIX 547 549 {ECO:0000244|PDB:3FCS}.
STRAND 551 554 {ECO:0000244|PDB:3FCS}.
TURN 555 557 {ECO:0000244|PDB:3FCS}.
STRAND 559 567 {ECO:0000244|PDB:3FCS}.
STRAND 575 583 {ECO:0000244|PDB:3FCS}.
HELIX 586 588 {ECO:0000244|PDB:3FCS}.
STRAND 596 603 {ECO:0000244|PDB:3FCS}.
STRAND 616 619 {ECO:0000244|PDB:3FCS}.
STRAND 622 627 {ECO:0000244|PDB:3FCS}.
TURN 634 637 {ECO:0000244|PDB:3FCS}.
STRAND 643 651 {ECO:0000244|PDB:3FCS}.
STRAND 653 655 {ECO:0000244|PDB:3FCS}.
STRAND 662 670 {ECO:0000244|PDB:3FCS}.
STRAND 678 683 {ECO:0000244|PDB:3FCS}.
STRAND 688 695 {ECO:0000244|PDB:3FCS}.
STRAND 705 708 {ECO:0000244|PDB:3FCS}.
STRAND 710 713 {ECO:0000244|PDB:3FCS}.
STRAND 715 721 {ECO:0000244|PDB:3FCS}.
STRAND 728 738 {ECO:0000244|PDB:3FCS}.
STRAND 746 755 {ECO:0000244|PDB:3FCS}.
STRAND 759 761 {ECO:0000244|PDB:3FCS}.
STRAND 767 774 {ECO:0000244|PDB:3FCS}.
STRAND 779 792 {ECO:0000244|PDB:3FCS}.
STRAND 810 819 {ECO:0000244|PDB:3FCS}.
STRAND 821 823 {ECO:0000244|PDB:3FCS}.
STRAND 825 836 {ECO:0000244|PDB:3FCS}.
STRAND 842 854 {ECO:0000244|PDB:3FCS}.
STRAND 856 861 {ECO:0000244|PDB:3FCS}.
STRAND 906 909 {ECO:0000244|PDB:3FCS}.
TURN 911 913 {ECO:0000244|PDB:3FCS}.
STRAND 916 926 {ECO:0000244|PDB:3FCS}.
STRAND 931 940 {ECO:0000244|PDB:3FCS}.
HELIX 942 945 {ECO:0000244|PDB:3FCS}.
STRAND 952 965 {ECO:0000244|PDB:3FCS}.
STRAND 967 969 {ECO:0000244|PDB:3FCS}.
STRAND 977 988 {ECO:0000244|PDB:3FCS}.
TURN 991 994 {ECO:0000244|PDB:2KNC}.
HELIX 997 1020 {ECO:0000244|PDB:2K1A}.
STRAND 1022 1024 {ECO:0000244|PDB:1DPK}.
TURN 1025 1027 {ECO:0000244|PDB:1DPK}.
HELIX 1028 1031 {ECO:0000244|PDB:1DPK}.
TURN 1035 1038 {ECO:0000244|PDB:1DPQ}.
SEQUENCE 1039 AA; 113377 MW; 063EE298E026F116 CRC64;
MARALCPLQA LWLLEWVLLL LGPCAAPPAW ALNLDPVQLT FYAGPNGSQF GFSLDFHKDS
HGRVAIVVGA PRTLGPSQEE TGGVFLCPWR AEGGQCPSLL FDLRDETRNV GSQTLQTFKA
RQGLGASVVS WSDVIVACAP WQHWNVLEKT EEAEKTPVGS CFLAQPESGR RAEYSPCRGN
TLSRIYVEND FSWDKRYCEA GFSSVVTQAG ELVLGAPGGY YFLGLLAQAP VADIFSSYRP
GILLWHVSSQ SLSFDSSNPE YFDGYWGYSV AVGEFDGDLN TTEYVVGAPT WSWTLGAVEI
LDSYYQRLHR LRGEQMASYF GHSVAVTDVN GDGRHDLLVG APLYMESRAD RKLAEVGRVY
LFLQPRGPHA LGAPSLLLTG TQLYGRFGSA IAPLGDLDRD GYNDIAVAAP YGGPSGRGQV
LVFLGQSEGL RSRPSQVLDS PFPTGSAFGF SLRGAVDIDD NGYPDLIVGA YGANQVAVYR
AQPVVKASVQ LLVQDSLNPA VKSCVLPQTK TPVSCFNIQM CVGATGHNIP QKLSLNAELQ
LDRQKPRQGR RVLLLGSQQA GTTLNLDLGG KHSPICHTTM AFLRDEADFR DKLSPIVLSL
NVSLPPTEAG MAPAVVLHGD THVQEQTRIV LDCGEDDVCV PQLQLTASVT GSPLLVGADN
VLELQMDAAN EGEGAYEAEL AVHLPQGAHY MRALSNVEGF ERLICNQKKE NETRVVLCEL
GNPMKKNAQI GIAMLVSVGN LEEAGESVSF QLQIRSKNSQ NPNSKIVLLD VPVRAEAQVE
LRGNSFPASL VVAAEEGERE QNSLDSWGPK VEHTYELHNN GPGTVNGLHL SIHLPGQSQP
SDLLYILDIQ PQGGLQCFPQ PPVNPLKVDW GLPIPSPSPI HPAHHKRDRR QIFLPEPEQP
SRLQDPVLVS CDSAPCTVVQ CDLQEMARGQ RAMVTVLAFL WLPSLYQRPL DQFVLQSHAW
FNVSSLPYAV PPLSLPRGEA QVWTQLLRAL EERAIPIWWV LVGVLGGLLL LTILVLAMWK
VGFFKRNRPP LEEDDEEGE


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