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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

Antibody: Streptavidin Dye: Europium Chelate W-1024 Excitation max. λ: 340 nm Emission max. λ: 615 nm Uses: TR-FRET high throughput screening (HTS) applications (LANCE®, HTRF®)

HOOK™-NHS-SS-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35 are…

HOOK™-Biotin-PEG₃-Amine reacts with protein carboxyl groups in the presence of the heterobifunctional cross-linker EDC. HOOK™-Biotin-Pentylamine, HOOK™-Biotin-PEG₂-Amine and HOOK™-Biotin-PEG₃-Amine are water soluble, due to its polyethylene…

HOOK™-Sulfo-NHS-LC-LC-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

HOOK™-Iodoacetyl-LC-Biotin reacts with protein free sulhydryl groups. Sulfhydryl reactive reagents are more specific and react only with free sulfhydryl residues (-SH or thiol groups). The side chain of the amino acid cysteine is the most common source of free sulfhydryl groups. If free…

HOOK™-NHS-dPEG™₄-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of…

HOOK™-Biotin-PEG₂-Amine reacts with protein carboxyl groups in the presence of the heterobifunctional cross-linker EDC. HOOK™-Biotin-Pentylamine, HOOK™-Biotin-PEG₂-Amine and HOOK™-Biotin-PEG₃-Amine are water soluble, due to its polyethylene…

HOOK™-Biotin-Hydrazide reacts with oxidized carbohydrate side chains. Some biotin reagents do not bind directly to the protein itself but conjugate to the carbohydrate residues of glycoproteins. Carbodhydrate reactive biotin reagents contain hydrazides (-NH-NH₂) as a reactive…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

HOOK™-PFP-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35 are…

HOOK™-Sulfo-NHS-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35…

HOOK™-Sulfo-NHS-LC-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35…

Streptavidin conjugated to SureLight® APC Binding Moiety: Streptavidin Dye: SureLight® Allophycocyanin (APC) Excitation max. λ: 652 nm Emission max. λ: 657.5 nm Uses: High throughput screening (HTS) and fluorescence resonance energy transfer (FRET) assays, flow cytometry

HOOK™-Biotin-BMMCC reacts with protein free sulhydryl groups. Sulfhydryl reactive reagents are more specific and react only with free sulfhydryl residues (-SH or thiol groups). The side chain of the amino acid cysteine is the most common source of free sulfhydryl groups. If free sulfhydryl…

HOOK™-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). The side chain of the amino acid cysteine is the most common source of free sulfhydryl groups.…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

HOOK™ NHS-Biotin reacts with protein primary amines. Amines, lysine ε-amines and N-terminal α-amines, are the most abundant group in protein molecules and represent the most common target for biotinylation. For example, BSA contains 59 primary amines, of which up to 35 are…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

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 of streptavidin are recommended for use with…

Streptavidin: Streptavidin is a tetrameric protein composed of four identical subunits. Each subunit binds one biotin molecule with a KD of ~1 x 10-15 M. The preparation contains an N- and C-terminal shortened variant (core streptavidin) with improved properties concerning homogeneity,…

This is a purified product supplied in 0.05% sodium azide. The typical working dilution is 1:50-1:150.

Biotin, a 244Da vitamin (Vitamin H) molecule, exhibits an extraordinary binding affinity for avidin (Ka=10¹â�µM-¹) and streptavidin (Ka=10¹â�µM-¹). Biotin and (strept)avidin interaction is rapid. Once the bond is established, it can survive up to 3M…