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alphaIIb beta3 antagonist TMV-7/trimucrin prevents thrombosis with causing Fc receptor gamma-chain IIa-mediated thrombocytopenia.
Kindlin supports platelet GPIIB IIIA activation by interacting with paxillin (show PXN Proteins).
Platelets from Dok-1 (show DOK1 Proteins)-/- mice displayed normal aggregation, activation of integrin alphaIIbbeta3, P-selectin (show SELP Proteins) surface expression, and soluble fibrinogen binding. These findings indicate that Dok-1 (show DOK1 Proteins) does not affect "inside-out" platelet signalling.
platelets clearly support early steps in pulmonary metastasis via GPIIb-dependent formation of platelet-tumor-aggregates
ITGA2b expression increases in response to immunization, raising the possibility that heterogeneous ITGA2b levels reflect variation in exposure to activation signals.
Thrombopoietin (show THPO Proteins)/MPL (show MPL Proteins) signaling confers growth and survival capacity to CD41-positive cells in a mouse model of Evi1 (show MECOM Proteins) leukemia.
Direct binding of kindlin-3 (show FERMT3 Proteins) to integrin alphaIIbbeta3 is involved in supporting integrin alphaIIbbeta3 activation and integrin alphaIIbbeta3-dependent responses of platelets and consequently contributes significantly to arterial thrombus formation.
ADAP interacts with talin and kindlin-3 to promote platelet Integrin alphaIIbbeta3 activation and stable fibrinogen binding.
reduction of talin-beta3 integrin (show ITGB3 Proteins) binding affinity results in decelerated alphaIIbbeta3 integrin activation and protection from arterial thrombosis without pathological bleeding
deficiency of Dok-2 leads to dysregulated integrin alphaIIbbeta3-dependent cytosolic calcium flux and phosphatidylinositol(3,4)P2 accumulation.
Type I Glanzmann thrombasthenia (GT)was found most common in our patients and with lowered mean CD41 expression in comparison with CD61 (show ITGB3 Proteins). Type III GT patients had significantly lower numbers of severe bleeders, but the severity of bleeding did not vary significantly in type I and II GT patients
Case Reports: alterations in the platelet proteome in type I Glanzmann thrombasthenia patients caused by different homozygous delG frameshift mutations in ITGA2B.
study strongly supported the contribution of the genes ITGA2B, GSN and RHOA and the two pathways "regulation of actin cytoskeleton" and "leukocyte transendothelial migration" to osteoporosis risk.
Meta-analysis found that glycoprotein Ia (show MMRN1 Proteins) C807T T allele or the TT genotype, the Ser (show SIGLEC1 Proteins)-allele of HPA-3 and B allele of glycoprotein Ibalpha (show GP1BA Proteins) variable number tandem repeat polymorphisms were associated with increased risk for ischemic stroke.
Furthermore, the inside-out activation of GPIIb/IIIa of platelets mediated Streptococcus suis suilysin-induced platelet aggregation.
Data suggest that the extreme C terminus of kindlin-2 (show FERMT2 Proteins) is essential for interaction with and activation of integrin alphaIIBbeta3; these studies were conducted in macrophage cell line and erythroleukemia cell line.
Both in cell lines and in mouse model, the extracellular matrix receptors including the integrin ( ITGA3 (show ITGA3 Proteins) and ITGA2B), collagen ( COL5A1), and laminin ( LAMA5 (show LAMA5 Proteins)) were significantly inhibited by curcumin at messenger RNA and protein levels.
Case Report: Reduced binding of mutant FLNa (show FLNA Proteins) to beta3 and the facilitated recruitment of talin by beta3 on platelet stimulation, explaining the increased alphaIIbbeta3 activation and the ensuing gain-of-platelet functions.
Mechanistic basis for the binding of fibrinogen-derived RGD- and AGDV-peptides to the platelet integrin alphaIIb-beta3 has been described.
ITGA2B encodes integrin alpha chain 2b. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 2b undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibronectin receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.
, GPalpha IIb
, alpha IIb
, integrin alpha-IIb
, platelet glycoprotein IIb of IIb/II Ia complex
, platelet membrane glycoprotein IIb
, platelet fibrinogen receptor, alpha subunit
, platelet-specific antigen BAK