Integrin alpha 6 beta 1 Protein, Human, Recombinant (Flag & His Tag)

At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.

Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

The recombinant heterodimer of human ITGA6/ITGB1 comprises 1779 (1030 + 749) amino acids and has a calculated molecular mass of 198 (115 + 83) kDa. As a result of glycosylation, the apparent molecular mass of rh ITGA6/ITGB1 heterodimer is approximately 110 & 130 kDa in SDS-PAGE under reducing conditions

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.

A DNA sequence encoding the extracellular domain (Met 1-Ser 1011) of human ITGA6 isoform alpha-6X1B (P23229-3) was fused with a flag tag at the C-terminus, constructed the plasmid 1 ; A DNA sequence encoding the extracellular domain (Met 1-Asp 728) of human ITGB1 (P05556-1) was fused with a polyhistidine tag at the C-terminus, constructed the plasmid 2. The two plasmids were co-expressed and the heterodimer was purified