Streptavidin is a bacterially derived biotin-binding protein that reportedly exhibits less nonspecific binding than avidin.Capacity: Binding activity of streptavidin isRead more
Streptavidin is a bacterially derived biotin-binding protein that reportedly exhibits less nonspecific binding than avidin.
Capacity: Binding activity of streptavidin is determined to be >11 units per mg protein. One unit of binding activity is defined as that amount of protein which binds 1 μg of biotin (Green, N.M., Biochem. J., 89:599,1963)
Form: Streptavidin is provided in lyophilized form in 10 mM phosphate buffered saline, pH 7.4. Reconstitute with 1 ml of distilled or deionized water.
Storage: Store at 4°C.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Product TypeStreptavidin Conjugate (fluorescent)
Quantity5 mg
Shipping ConditionWet Ice
ConjugateUnconjugated
FormLyophilized
Unit SizeEach
Contents & Storage
Streptavidin is provided in lyophilized form in 10 mM phosphate buffered saline, pH 7.4. Reconstitute with 1 ml of distilled or deionized water. Store at 4°C.
Frequently asked questions (FAQs)
Are there any His-tags on Streptavidin (Cat. No. 434302)?
This Streptavidin is a native protein from Streptomyces avidinii, therefore there are no His-tags on it.
How many biotin binding-sites are there per streptavidin molecule?
Streptavidin is a protein composed of four identical subunits, each containing a high affinity binding site for biotin (K-D = 10 -15 M) . Streptavidin has the same biotin binding properties as avidin, but it has a low isoelectric point (pI=5) and no carbohydrate groups, resulting in low non-specific binding.
Is Streptavidin (Cat. No. S888, 434302, and 434301) RNAse-free?
Although we utilize manufacturing methods that minimize the introduction of any contaminants such as RNases, we do not process this product to specifically remove or inactivate RNases and do not test for RNase activity.