Recombinant Strep-Tactin with Cysteine (r-STc)

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Lyophilized from 5mM PB (2.5mM Na2HPO4, 2.5mM NaH2PO4, pH 6.8)
Mol. Weight:
13.4 kDa subunit; Tetramer 53.6 kDa
Theory pI:
Theoretical activity:
18.2 U / mg protein (r-STc: Biotin = 1: 4 (mol: mol))
≥ 15 U / mg protein (Improved green method)
≥95% (SDS-PAGE)
Concentration determination:
absorption method at 280nm, the molar absorption coefficient is 1.68 × 105 (mol / L) -1cm-1, c (g / L) = A280nm / 3.13
≤5EU / mg
Storage condition:
-20 °C
Storage period:
3 years
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Streptavidin is a streptavidin mutant, which can bind specifically to streptavidin. The Strep II tag is a small 8 amino acid tag (wshpqfek). Since the tag is small, it is only about 1 kDa, which generally does not affect the structure and function of the fusion protein. It is commonly used in the detection and purification of fusion protein. Compared to streptactin, streptactin has a 10 times stronger affinity for streptavidin. It can bind and dissociate with streptavidin under mild conditions and can play a good role in separation and purification. In order to be able to bind to the medium, a cysteine ​​has been added to the C-terminus of the amino acid sequence, which can be covalently linked to the medium through a sulfhydryl group.

M : protein molecular weight marker

Lane 1 : r-STc subunit Lane 2 : r-STc Tetramer

For research only!

Recombinant Strep-Tactin with Cysteine (r-STc) DataSheet

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