Recombinant streptavidin (C-line)

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 carefully selects the active core regions of each functional fragment for recombination and expression. Compared with natural streptavidin, it significantly enhances the binding ability to NC membranes, and retains the affinity for biotin after binding to NC membranes. This product is typically used for C-line detection coated on NC membranes. Due to the strong affinity between streptavidin and biotin, it offers an excellent ability to capture trace biotin-labeled substances and can maintain stable color development.

Source: Escherichia coli

Buffer solution: 20mM PB, pH7.4

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