Streptavidin

HOOK&trade-NHS-SS-Biotin reacts with protein primary amines. Amines, lysine &epsilon-amines and N-terminal &alpha-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation.

HOOK&trade-PEG₂-Iodoacetyl-Biotin reacts with protein free sulhydryl groups. Sulfhydryl reactive reagents are more specific and react only with free sulfhydryl residues (-SH or thiol groups).

HOOK&trade-PFP-Biotin reacts with protein primary amines. Amines, lysine &epsilon-amines and N-terminal &alpha-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation.

HOOK&trade-Sulfo-NHS-Biotin reacts with protein primary amines. Amines, lysine &epsilon-amines and N-terminal &alpha-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation.

HOOK&trade-Sulfo-NHS-LC-Biotin reacts with protein primary amines. Amines, lysine &epsilon-amines and N-terminal &alpha-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation.

HOOK&trade-Sulfo-NHS-LC-LC-Biotin reacts with protein primary amines. Amines, lysine &epsilon-amines and N-terminal &alpha-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation.

HOOK&trade-Sulfo-NHS-SS-Biotin reacts with protein primary amines. Amines, lysine &epsilon-amines and N-terminal &alpha-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation.

Steptavidin, a bacterial protein isolated from Streptomyces avidinii, is similar to egg-white avidin in its ability to bind biotin, and has been used as a replacement for egg-white avidin because of its more favorable chemical properties. Conjugates

Steptavidin, a bacterial protein isolated from Streptomyces avidinii, is similar to egg-white avidin in its ability to bind biotin, and has been used as a replacement for egg-white avidin because of its more favorable chemical properties. Conjugates

Biotin, a 244Da vitamin (Vitamin H) molecule, exhibits an extraordinary binding affinity for avidin (Ka=10&sup1&acirc&microM-&sup1) and streptavidin (Ka=10&sup1&acirc&microM-&sup1). Biotin and (strept)avidin interaction is rapid.

Steptavidin, a bacterial protein isolated from Streptomyces avidinii, is similar to egg-white avidin in its ability to bind biotin, and has been used as a replacement for egg-white avidin because of its more favorable chemical properties. Conjugates

Steptavidin, a bacterial protein isolated from Streptomyces avidinii, is similar to egg-white avidin in its ability to bind biotin, and has been used as a replacement for egg-white avidin because of its more favorable chemical properties. Conjugates