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Recombinant BTX (Light Chain) Protein
Botulinum neurotoxin type A is one of the seven serotypes of Botulinum Neurotoxins (BoNTs) produced by various strains of Clostridium botulinum.
Streptavidin
Streptavidin is a non-glycosylated, 52.8 kDa, tetrameric bacterial protein isolated from Streptomyces avidinii with a very high affinity for biotin. Streptavidin-biotin bond is the strongest known non-covalent interaction with Kd ~10-15 M. Because streptavidin lacks any carbohydrate modification and has a near-neutral pI, it has the advantage of much lower nonspecific binding than avidin.
Description
Streptavidin is a non-glycosylated, 52.8 kDa, tetrameric bacterial protein isolated from Streptomyces avidinii with a very high affinity for biotin. Streptavidin-biotin bond is the strongest known non-covalent interaction with Kd ~10-15 M. Because streptavidin lacks any carbohydrate modification and has a near-neutral pI, it has the advantage of much lower nonspecific binding than avidin. The binding of streptavidin to biotin provides several further advantages in addition to the strength of the interaction:
Highly specific
Rapid on-rate
Resistant to changes in temperature or pH
Can withstand the presence of organic solvents and denaturing agents
Streptavidin is used extensively in a wide range of laboratory applications, and there are many ways in which their strong biological interaction can be exploited.
Applications
Immunoassays
Histochemistry
FISH (Fluorescence In Situ Hybridization)
Flow cytometry
Microarrays and blot analysis
Source
E. coli
Purity
> 95 % as determined by SDS-PAGE
Unit Definition
One unit is defined as the amount of streptavidin required to bind 1.0 µg of D-Biotin at pH 7.0.
Specific Activity
15.5 U/mg by biotin titration method
Storage
Store vial at 4° C prior to restoration. For extended storage aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing.
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Streptavidin is a non-glycosylated, 52.8 kDa, tetrameric bacterial protein isolated from Streptomyces avidinii with a very high affinity for biotin. Streptavidin-biotin bond is the strongest known non-covalent interaction with Kd ~10-15 M. Because streptavidin lacks any carbohydrate modification and has a near-neutral pI, it has the advantage of much lower nonspecific binding than avidin.