Streptavidin is a biotin-binding protein found in culture broth of the bacterium Streptomyces avidin. Streptavidin binds 4 moles of biotin per mole of protein with a remarkably high affinity. Streptavidin has isoelectric point near to neutrality where most useful biological interaction occur. Accordingly, streptavidin exhibits lower levels of non-specific interaction than does avidin molecule when the streptavidin protein used in applications relying upon the formation of avidin/biotin complexes.
MicroProtein’s recombinant Streptavidin lacks carbohydrate side chains or other associated cofactors. Streptavidin is a 52 K Dalton, is a tetramer complex composed of 4 identical polypeptide chains. Recombinant Streptavidin protein contain no cysteine residues, sugar side chains or other cofactors. Streptavidin protein is stable over wide pH range and heat stable, heating up to 100°C for 20 minutes in 0.2% SDS to dissociate the subunits.
MicroProtein’s high quality recombinant Streptavidin is a suitable tool for allowing universal test systems in molecular diagnostics, reagents, kits, and immunology. This recombinant Streptavidin is appropriate for coating solid phases such as microarrays, beads, and microplates etc.
Animal component free (ACF) & Animal origin free (AOF)
Specific activity 15U/mg
Lyophilized carrier free
≥95% Purity by SDS Page
Store at 4°C to -20°C. After reconstitution use within 2 weeks, store at 4°C.
G7: SDS-PAGE Analysis of recombinant streptavidin: Lane 1: MW marker; Lane 2: 4ug of tetramer without heating; Lane 3: 4ug of monomer after heating.