Integrin alpha 2b beta 3,ITGAIIb&ITGB3
Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free (IT3-H52W8) is expressed from human 293 cells (HEK293). It contains AA Leu 32 - Arg 993 (ITGAIIb) & Gly 27 - Asp 718 (ITGB3) (Accession # P08514-1 (R887L)~ITGAIIb) & P05106-1~ITGB3)).
Predicted N-terminus: Leu 32 (ITGAIIb) & Gly 27 (ITGB3)
Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free, produced by co-expression of ITGAIIb and ITGB3, has a calculated MW of 111.4 kDa (ITGAIIb) and 81.8 kDa (ITGB3). Subunit ITGAIIb is fused with an acidic tail at the C-terminus and followed by a polyhistidine tag and subunit ITGB3 contains no tag but a basic tail at the C-terminus. The non-reducing (NR) protein migrates as 115-130 kDa (ITGAIIb) and 85-92 kDa (ITGB3) respectively due to glycosylation.
Less than 1.0 EU per μg by the LAL method.
>90% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free on SDS-PAGE under non-reducing (NR) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
Immobilized Human Fibronectin at 2 μg/mL (100 μL/well) can bind Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free (Cat. No. IT3-H52W8) with a linear range of 2-78 ng/mL (QC tested).
Immobilized Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free (Cat. No. IT3-H52W8) at 1 μg/mL (100 μL/well) can bind Abciximab with a linear range of 0.8-6 ng/mL (Routinely tested).
Integrin alpha IIb beta 3 exist in a conformational equilibrium clustered around four main states. These conformations range from a compact bent nodule to two partially extended intermediate conformers and finally to a fully upright state. Activation of blood platelets by physiological stimuli at sites of vascular injury induces inside-out signaling, resulting in a conformational change of the prototype Integrin alpha IIb beta 3 from an inactive to an active state competent to bind soluble fibrinogen. Furthermore, ligand occupancy of Integrin alpha IIb beta 3 outside-in signaling and additional conformational changes of the receptor, leading to the exposure of extracellular neoepitopes termed ligand-induced binding sites (LIBS), which are recognized by anti-LIBS monoclonal antibodies.