Streptomyces Avidinii Streptavidin Protein

Streptomyces Avidinii The streptavidin protein, although its exact biological function is unknown, forms a strong non-covalent complex with biotin, binding one molecule to each subunit. Its specific affinity for biotin suggests its application in processes requiring specific binding to biotinylated molecules. Streptomyces Avidinii Streptavidin Protein is the recombinant Streptomyces Avidinii Streptavidin protein, expressed by E. coli , with tag free. The total length of Streptomyces Avidinii Streptavidin Protein is 128 a.a., with molecular weight of ~14.3 kDa.

The Streptomyces Avidinii Streptavidin protein, while the precise biological function remains elusive, exhibits a distinct capability to form a robust non-covalent specific complex with biotin, involving one molecule of biotin per subunit of streptavidin. This interaction highlights the protein's exceptional affinity for biotin, suggesting potential applications in various molecular and cellular processes where specific binding to biotinylated molecules is required. Structurally, streptavidin forms a homotetramer, further emphasizing its quaternary arrangement and potential functional relevance within this oligomeric configuration.

Others

E. coli

Tag Free

P22629 (A36-S163)

/

Approximately 14.3 kDa

Greater than 95% as determined by Tris-Bis PAGE.

<1 EU/μg, determined by LAL method.