protein

Recombinant Human Integrin alpha-IIb

MBS956218

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Integrin alpha-IIb

Integrin alpha-IIb

GPalpha IIb; GPIIb; Platelet membrane glycoprotein IIb; CD41

integrin alpha-IIb preproprotein; Integrin alpha-IIb; integrin alpha-IIb; integrin subunit alpha 2b; GPalpha IIb; GPIIb

ITGA2B

ITGA2B; ITGA2B; GT; GTA; CD41; GP2B; HPA3; CD41B; GPIIb; BDPLT2; BDPLT16; PPP1R93; GP2B; ITGAB; GPIIb

ITA2B_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

639-887

1039

CVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYE
AELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVV
LCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIR
SKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAA
EEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIH
LPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGL
PIPSPSPIHPAHHKR

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cardiovascular

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.

Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors.Poncz M., Eisman R., Heidenreich R., Silver S.M., Vilaire G., Surrey S., Schwartz E., Bennett J.S.J. Biol. Chem. 262:8476-8482(1987) GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs.Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G.Mol. Biol. Rep. 14:27-33(1990) Organization of the gene for platelet glycoprotein IIb.Heidenreich R., Eisman R., Surrey S., Delgrosso K., Bennett J.S., Schwartz E., Poncz M.Biochemistry 29:1232-1244(1990) Complete sequencing and characterization of 21,243 full-length human cDNAs.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.Nat. Genet. 36:40-45(2004) DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.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.Nature 440:1045-1049(2006) Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs.Bray P.F., Leung C.S.-I., Shuman M.A.J. Biol. Chem. 265:9587-9590(1990) 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.Uzan G., Frachet P., Lajmanovich A., Prandini M.-H., Denarier E., Duperray A., Loftus J., Ginsberg M., Plow E., Marguerie G.Eur. J. Biochem. 171:87-93(1988) Platelet glycoprotein IIb. Chromosomal localization and tissue expression.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.J. Clin. Invest. 80:1812-1817(1987) Isolation of the human platelet glycoprotein IIb gene and characterization of the 5' flanking region.Prandini M.H., Denarier E., Frachet P., Uzan G., Marguerie G.Biochem. Biophys. Res. Commun. 156:595-601(1988) Platelet glycoproteins IIb and IIIa evidence for a family of immunologically and structurally related glycoproteins in mammalian cells.Charo I.F., Fitzgerald L.A., Steiner B., Rall S.C., Bekeart L.S., Phillips D.R.Proc. Natl. Acad. Sci. U.S.A. 83:8351-8355(1986) 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.Catimel B., Parmentier S., Leung L.L., McGregor J.L.Biochem. J. 279:419-425(1991) Thermal stability of individual domains in platelet glycoprotein IIbIIIa.Makogonenko E.M., Yakubenko V.P., Ingham K.C., Medved L.V.Eur. J. Biochem. 237:205-211(1996) Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa.Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.Blood 69:560-564(1987) Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb. Localization of the epitopes for several monoclonal antibodies.Calvete J.J., Alvarez M.V., Rivas G., Hew C.L., Henschen A., Gonzalez-Rodriguez J.Biochem. J. 261:551-560(1989) Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb.Calvete J.J., Henschen A., Gonzalez-Rodriguez J.Biochem. J. 261:561-568(1989) Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.Calvete J.J., Muniz-Diaz E.FEBS Lett. 328:30-34(1993) Identification of a novel truncated alphaIIb integrin.Trikha M., Cai Y., Grignon D., Honn K.V.Cancer Res. 58:4771-4775(1998) Characterization of the beta-chain N-terminus heterogeneity and the alpha-chain C-terminus of human platelet GPIIb. Posttranslational cleavage sites.Calvete J.J., Schafer W., Henschen A., Gonzalez-Rodriguez J.FEBS Lett. 272:37-40(1990) Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain.Naik U.P., Patel P.M., Parise L.V.J. Biol. Chem. 272:4651-4654(1997) Calcium-dependent properties of CIB binding to the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton.Shock D.D., Naik U.P., Brittain J.E., Alahari S.K., Sondek J., Parise L.V.Biochem. J. 342:729-735(1999) Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations.Leisner T.M., Wencel-Drake J.D., Wang W., Lam S.C.J. Biol. Chem. 274:12945-12949(1999) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb) beta3.Brophy T.M., Raab M., Daxecker H., Culligan K.G., Lehmann I., Chubb A.J., Treumann A., Moran N.Biochem. Biophys. Res. Commun. 369:1088-1093(2008) Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain.Huang H., Ishida H., Yamniuk A.P., Vogel H.J.J. Biol. Chem. 286:17181-17192(2011) Biophysical and structural studies of the human calcium- and integrin-binding protein family understanding their functional similarities and differences.Huang H., Bogstie J.N., Vogel H.J.Biochem. Cell Biol. 90:646-656(2012) Structural basis for the activation of platelet integrin alphaIIbbeta3 by calcium- and integrin-binding protein 1.Huang H., Vogel H.J.J. Am. Chem. Soc. 134:3864-3872(2012) Inherited diseases of platelet glycoproteins considerations for rapid molecular characterization.Bray P.F.Thromb. Haemost. 72:492-502(1994) Polymorphism of human platelet membrane glycoprotein IIb associated with the Baka/Bakb alloantigen system.Lyman S., Aster R.H., Visentin G.P., Newman P.J.Blood 75:2343-2348(1990) Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb.Poncz M., Rifat S., Coller B.S., Newman P.J., Shattil S.J., Parrella T., Fortina P., Bennett J.S.J. Clin. Invest. 93:172-179(1994) A single amino acid substitution flanking the fourth calcium binding domain of alpha IIb prevents maturation of the alpha IIb beta 3 integrin complex.Wilcox D.A., Wautier J.-L., Pidard D., Newman P.J.J. Biol. Chem. 269:4450-4457(1994) 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.Wilcox D.A., Paddock C.M., Lyman S., Gill J.C., Newman P.J.J. Clin. Invest. 95:1553-1560(1995) 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.Basani R.B., Vilaire G., Shattil S.J., Kolodziej M.A., Bennett J.S., Poncz M.Blood 88:167-173(1996) Hematologically important mutations Glanzmann thrombasthenia.French D.L., Coller B.S.Blood Cells Mol. Dis. 23:39-51(1997) Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa.Grimaldi C.M., Chen F., Wu C., Weiss H.J., Coller B.S., French D.L.Blood 91:1562-1571(1998) A Gln747-->Pro substitution in the IIb subunit is responsible for a moderate IIbbeta3 deficiency in Glanzmann thrombasthenia.Tadokoro S., Tomiyama Y., Honda S., Arai M., Yamamoto N., Shiraga M., Kosugi S., Kanakura Y., Kurata Y., Matsuzawa Y.Blood 92:2750-2758(1998) 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.Peyruchaud O., Nurden A.T., Milet S., Macchi L., Pannochia A., Bray P.F., Kieffer N., Bourre F.Blood 92:4178-4187(1998) Novel point mutations in the alphaIIb subunit (Phe289-->Ser, Glu324-->Lys and Gln747-->Pro) causing thrombasthenic phenotypes in four Japanese patients.Ambo H., Kamata T., Handa M., Kawai Y., Oda A., Murata M., Takada Y., Ikeda Y.Br. J. Haematol. 102:829-840(1998) Double heterozygosity of the GPIIb gene in a Swiss patient with Glanzmann's thrombasthenia.Ruan J., Peyruchaud O., Alberio L., Valles G., Clemetson K., Bourre F., Nurden A.T.Br. J. Haematol. 102:918-925(1998) Characterization of single-nucleotide polymorphisms in coding regions of human genes.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. 22:231-238(1999) 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.Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., Alvarez M.-V., Garcia-Munoz S., Ayuso M.S., Parrilla R.Blood 93:866-875(1999) ErratumCargill 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) A naturally occurring mutation near the amino terminus of alphaIIb defines a new region involved in ligand binding to alphaIIbbeta3.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.Blood 95:180-188(2000) Description of 10 new mutations in platelet glycoprotein IIb (alphaIIb) and glycoprotein IIIa (beta3) genes.Vinciguerra C., Bordet J.C., Beaune G., Grenier C., Dechavanne M., Negrier C.Platelets 12:486-495(2001) A Leu55 to Pro substitution in the integrin alphaIIb is responsible for a case of Glanzmann's thrombasthenia.Tanaka S., Hayashi T., Hori Y., Terada C., Han K.S., Ahn H.S., Bourre F., Tani Y.Br. J. Haematol. 118:833-835(2002) Glanzmann's thrombasthenia identification of 19 new mutations in 30 patients.D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M.Thromb. Haemost. 87:1034-1042(2002) Two novel mutations in the alpha IIb calcium-binding domains identify hydrophobic regions essential for alpha IIbbeta 3 biogenesis.Mitchell W.B., Li J.H., Singh F., Michelson A.D., Bussel J., Coller B.S., French D.L.Blood 101:2268-2276(2003) 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.Kiyoi T., Tomiyama Y., Honda S., Tadokoro S., Arai M., Kashiwagi H., Kosugi S., Kato H., Kurata Y., Matsuzawa Y.Blood 101:3485-3491(2003) Triple heterozygosity in the integrin alphaIIb subunit in a patient with Glanzmann's thrombasthenia.Nurden A.T., Breillat C., Jacquelin B., Combrie R., Freedman J., Blanchette V.S., Schmugge M., Rand M.L.J. Thromb. Haemost. 2:813-819(2004) A novel Phe171Cys mutation in integrin alpha causes Glanzmann thrombasthenia by abrogating alphaIIbbeta3 complex formation.Rosenberg N., Landau M., Luboshitz J., Rechavi G., Seligsohn U.J. Thromb. Haemost. 2:1167-1175(2004) Type II Glanzmann thrombasthenia in a compound heterozygote for the alpha IIb gene. A novel missense mutation in exon 27.Jayo A., Pabon D., Lastres P., Jimenez-Yuste V., Gonzalez-Manchon C.Haematologica 91:1352-1359(2006) AlphaIIbbeta3 integrin new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function.Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N., Goudemand J., de Brevern A.G., Kaplan C.Hum. Mutat. 31:237-246(2010) Heterozygous ITGA2B R995W mutation inducing constitutive activation of the alphaIIbbeta3 receptor affects proplatelet formation and causes congenital macrothrombocytopenia.Kunishima S., Kashiwagi H., Otsu M., Takayama N., Eto K., Onodera M., Miyajima Y., Takamatsu Y., Suzumiya J., Matsubara K., Tomiyama Y., Saito H.Blood 117:5479-5484(2011) +Additional computationally mapped references. p>Provides general information on the entry.

88758615

NP_000410.2

NM_000419.4

P08514

42.97kD

ARMS-mediated Activation Pathway (1269471); Arf6 Signaling Events Pathway (138034); Arrhythmogenic Right Ventricular Cardiomyopathy Pathway (672454); Arrhythmogenic Right Ventricular Cardiomyopathy (ARVC) Pathway (117293); Arrhythmogenic Right Ventricular Cardiomyopathy (ARVC) Pathway (116129); Axon Guidance Pathway (1270303); Cytokine Signaling In Immune System Pathway (1269310); DAP12 Interactions Pathway (1269283); DAP12 Signaling Pathway (1269284); Developmental Biology Pathway (1270302)

This gene encodes a member of the integrin alpha chain family of proteins. The encoded preproprotein is proteolytically processed to generate light and heavy chains that associate through disulfide linkages to form a subunit of the alpha-IIb/beta-3 integrin cell adhesion receptor. This receptor plays a crucial role in the blood coagulation system, by mediating platelet aggregation. Mutations in this gene are associated with platelet-type bleeding disorders, which are characterized by a failure of platelet aggregation, including Glanzmann thrombasthenia. [provided by RefSeq, Jan 2016]

ITGA2B: 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. Belongs to the integrin alpha chain family. Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chain linked by a disulfide bond. Alpha-IIb associates with beta-3. Directly interacts with RNF181. 3 isoforms of the human protein are produced by alternative splicing. Protein type: Motility/polarity/chemotaxis; Membrane protein, integral; Cell adhesion. Chromosomal Location of Human Ortholog: 17q21.32. Cellular Component: cell surface; external side of plasma membrane; focal adhesion; integral to plasma membrane; integrin complex; plasma membrane; platelet alpha granule membrane. Molecular Function: extracellular matrix binding; identical protein binding; metal ion binding; protein binding. Biological Process: axon guidance; blood coagulation; cell adhesion; cell-matrix adhesion; extracellular matrix organization and biogenesis; integrin-mediated signaling pathway; platelet activation; platelet degranulation; positive regulation of leukocyte migration. Disease: Bleeding Disorder, Platelet-type, 16; Glanzmann Thrombasthenia

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (E-Coli)

750