Integrin alpha 11 beta 1,ITGA11&ITGB1
Human ITGA11&ITGB1 Heterodimer Protein, His Tag&Tag Free (IT1-H52W3) is expressed from human 293 cells (HEK293). It contains AA Phe 23 - Pro 1141 (ITGA11) & Gln 21-Asp 728 (ITGB1) (Accession # Q9UKX5-1(L524R) (ITGA11) & P05556-1(ITGB1)).
Predicted N-terminus: Phe 23 (ITGA11) & Gln 21 (ITGB1)
Human ITGA11&ITGB1 Heterodimer Protein, His Tag&Tag Free, produced by co-expression of ITGA11 and ITGB1, has a calculated MW of 131.6 kDa (ITGA11) and 82.7 kDa (ITGB1). Subunit ITGA11 is fused with an acidic tail at the C-terminus and followed by a polyhistidine tag and subunit ITGB1 contains no tag but a basic tail at the C-terminus. The reducing (R) protein migrates as 150-165 kDa (ITGA11) and 90-120 kDa (ITGB1) 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 ITGA11&ITGB1 Heterodimer Protein, His Tag&Tag Free on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 90%.
Immobilized Human Collagen I protein at 2 μg/mL (100 μL/well) can bind Human ITGA11&ITGB1 Heterodimer Protein, His Tag&Tag Free (Cat. No. IT1-H52W3) with a linear range of 0.078-1.25 μg/mL (QC tested).
Integrin alpha 11 beta 1 is a receptor for collagen. The alpha11 cDNA encodes a mature protein with a large 1120-residue extracellular domain that contains an I-domain of 207 residues and is linked by a transmembrane domain to a short cytoplasmic domain of 24 amino acids. The deduced alpha11 protein shows the typical structural features of integrin alpha-subunits and is similar to a distinct group of alpha-subunits from collagen-binding integrins.