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ITGA2B encodes integrin alpha chain 2b. Additionally we are shipping Integrin Alpha2b Antibodies (411) and Integrin Alpha2b Kits (10) and many more products for this protein.
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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.
Platelets lacking ERp57 (show PDIA3 Proteins) have defective activation of the alphaIIbbeta3 integrin and platelet aggregation. The defect in aggregation was corrected by the addition of exogenous ERp57 (show PDIA3 Proteins), implicating surface ERp57 (show PDIA3 Proteins) in platelet aggregation.
Data indicate that Pyk2 (show PTK2B Proteins) is a common signaling effector downstream of both G12 (show TCF3 Proteins)/13 and integrin alphaIIbbeta3 signaling, which contributes to thromboxane generation.
These results identify a novel pathway of integrin alphaIIbbeta3 outside-in signaling and recognize the tyrosine kinase Pyk2 as a major regulator of platelet adhesion and spreading on fibrinogen.
identified Hic-5 (show TGFB1I1 Proteins) as a novel and specific regulatory factor for thrombin (show F2 Proteins)-induced alphaIIbbeta3 activation and subsequent platelet aggregation in mice.
Data show that immune thrombocytopenia (ITP (show ITPA Proteins)) is an autoimmune bleeding disorder characterized by low platelet count and presence of IgG autoantibodies to platelet surface glycoproteins, such as alpha IIbbeta3 integrins.
Data suggest that the ligand AGDV tetrapeptide binds to ITGB3/GPIIIa subunit and induces complete opening of headpiece of integrin alphaIIb/beta3 complex; AGDV appears to have very little contact with ITGA2B/GPIIb subunit.
Analysis showed a protective effect of TT genotype of ITGA2 (show ITGA2 Proteins) 807 C/T on fibrosis progression rate in Chronic Hepatitis C patients.
Report novel ITGA2B mutations causing Glanzmann thrombasthenia.
Ibrutinib causes GPVI (show GP6 Proteins) and integrin alphaIIbbeta3 platelet signaling deficiencies that result in formation of unstable thrombi and may contribute toward bleeding.
Data indicate 114 novel missense variants in integrin alpha 2b (ITGA2B) and 68 novel missense variants in integrin beta 3 (ITGB3 (show ITGB3 Proteins)).
Data (including data from molecular dynamic simulations) suggest specific interactions between glycoprotein GPIIb/GPIIIa (show ITGB3 Proteins) complex transmembrane/C-terminal domains and talin-1 (show TLN1 Proteins) in cell membrane environment during platelet activation.
Anionic lipids in annular positions stabilize the alphaIIbbeta3 transmembrane complex by up to 0.50 +/- 0.02 kcal/mol (show DUOXA1 Proteins) relative to zwitterionic lipids in a headgroup structure-dependent manner.
ITGA2B rs5911 GG genotype is associated with decreased ex vivo antiplatelet activity of ticagrelor in healthy Chinese male subjects.
The genetic polymorphism of GP lIb-Illa (GP Ila (show TNFRSF9 Proteins) Leu33Pro) was not noted to affect platelet aggregation.
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