Recombinant Streptavidin (Core, High Purity & Activity)

Recombinant Streptavidin is a homo-tetrameric protein produced in E. coli as an N- and C-terminal shortened variant (core streptavidin, amino acids 13–139). It is purified using proprietary chromatographic techniques to ensure maximum purity and excellent activity.

Because it lacks carbohydrate modifications and has a near-neutral isoelectric point (pI), our recombinant streptavidin offers significantly lower non-specific binding compared to native avidin, making it ideal for sensitive molecular biology applications.

Key Features & Specifications

• High Affinity: Binds D-biotin with a dissociation constant (Kd) of ~1.0 x 10^-14 mol/L, one of the strongest non-covalent interactions in nature.
• Exceptional Stability: The streptavidin-biotin complex remains stable across a wide range of temperatures and pH levels.
• High Activity: Greater than 16 U/mg (1 unit binds 1 µg of D-biotin).
• Formulation: Supplied as a 5 mg/mL solution in 0.5X PBS buffer (pH 7.4) and 50% glycerol.
• Molecular Weight: 13.4 kDa per monomer (single, non-glycosylated polypeptide chain of 128 amino acids); approximately 53.6 kDa per functional tetramer.

Applications

Optimized for use in high-performance downstream research applications, including:

• Enzyme-Linked Immunosorbent Assays (ELISA detection)
• Flow Cytometry and Immunohistochemistry
• Western Blotting and Protein Purification
• FISH (Fluorescence In Situ Hybridization) and Microarrays

Catalog # ST-302-5 (5 mg), ST-302-25 (25 mg).
This product is for research use only (RUO).