Recombinant streptavidin (Core type)

Streptavidin is composed of a tetramer of four identical subunits, each of which can bind to biotin. That is, one molecule of streptavidin can bind to four molecules of biotin, and the binding force is very high (Kd~10-15). Compared with avidin, streptavidin has a lower isoelectric point and contains no sugar groups. Therefore, when used in antigen-antibody detection systems, its non-specific binding is much lower than that of avidin.

Streptavidin has good thermal stability and certain tolerance to some protein denaturants such as acids, urea, and SDS, which endows the biotin-streptavidin system with advantages such as high affinity, high sensitivity, good specificity, good stability, and signal amplification. It can be widely applied in fields such as immunology, molecular biology, and histochemistry.

This product selects the core sequence of streptavidin that maintains its activity for cloning and expression. Compared with natural streptavidin, the protein of the same mass has higher activity.

Features: High affinity, high purity, stable performance

Source: Escherichia coli

Molecular weight: ~53.6kDa (13.4kDa/ subunit)

Purity: ≥95% (SDS-PAGE)

Activity: ≥16.0U/mg (1U represents binding 1μg of biotin)

Isoelectric point: 6.04