Amid Biosciences| Competent Cells and Protein Expression Vectors
Streptavidin is a homo-tetrameric protein secreted by Streptomyces avidinii. Streptavidin is used extensively in molecular biology for its extraordinarily high affinity for biotin. The binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature with a dissociation constant (Kd) of the biotin-streptavidin complex on the order ~10-14 mol/L. The streptavidin/biotin complex is extremely stable over a wide range of temperature and pH. Because streptavidin lacks any carbohydrate modification and has a near-neutral pI, it has the advantage of much lower nonspecific binding than avidin.
Recombinant Streptavidin is produced in E. coli as an N- and C-terminal shortened variant (core streptavidin, amino acids 13-139) and purified by proprietary chromatographic techniques. A single, non-glycosylated polypeptide chain contains a total of 128 amino acids with a molecular mass of 13.4 kDa. The molecular weight per tetramer is approximately 53.6 kDa.
The Streptavidin solution (5 mg/ml) contains 0.5XPBS buffer, pH 7.4 and 50% glycerol.
SKU: ST-302-5 (5 mg), ST-302-25 (25 mg)
Activity: Greater than 16 U/mg, 1 unit binds 1 µg of d-biotin.
Storage is recommended at -20°C for longer periods of time.
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This product is for laboratory research use only.