Analytical Data
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Gene name
Integrin alpha 2B beta 3
- Application
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Alternative Names
CD41; CD41B; ITG-A2B; GTA; GP2B; GPIIb; HPA3; Platelet Glycoprotein IIb Of IIb/IIIa Complex; Antigen CD41
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08514
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Expression Region
Gln891~Glu1039
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Molecular Weight
21kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Integrin alpha 2B beta 3, also known as glycoprotein IIb/IIIa, is a crucial receptor found on the surface of platelets, playing a vital role in hemostasis and thrombosis. This heterodimeric protein is responsible for binding fibrinogen and other adhesive proteins, facilitating platelet aggregation during clot formation. The study of recombinant integrin alpha 2B beta 3 has garnered significant interest due to its implications in cardiovascular diseases, particularly in the development of antithrombotic therapies. Understanding the structure and function of this integrin can lead to the design of novel inhibitors that target its active sites, which are essential for platelet aggregation. Research has highlighted the significance of different conformational states of alpha 2B beta 3 in regulating its activity and interaction with ligands. Additionally, recombinant production of this integrin enables detailed biochemical and biophysical characterization, providing insights into its signaling mechanisms and the molecular basis of integrin-mediated cell adhesion. With the increasing prevalence of cardiovascular disorders, the development of integrin-targeting therapeutics based on recombinant alpha 2B beta 3 offers a promising approach to mitigating the risks associated with thrombotic events. Therefore, ongoing studies focused on the isolation, purification, and functional analysis of recombinant alpha 2B beta 3 are critical for advancing our understanding of platelet biology and improving clinical strategies for thromboembolic diseases.
