Streptavidin

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.

Applications

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)

Activity

Specific activity 15U/mg

Formulation

Lyophilized carrier free

Purity

≥95% Purity by SDS Page

Storage

Store at 4°C to -20°C. After reconstitution use within 2 weeks, store at 4°C.