Recombinant Core Streptavidin (r-cSA)

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lyophilized from 5 mM of PB (4 mM of Na2HPO4, 1 mM of NaH2PO4, pH 7.4)
Mol. Weight:
13.5 kDa subunit; Tetramer 54kDa
Theory pI:
Theoretical activity:
18.1 U / mg protein (rc-SA: Biotin = 1: 4 (mol: mol))
Escherichia coli (E. coli)
≥95% by SDS-PAGE analysis
Test activity:
≥ 15 U / mg protein (determined by NUPTEC according to the modified green method)
Storage condition:
-20 °C
Storage period:
3 years
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Streptavidin is a homotetrameric protein found in the culture broth of Streptomyces avidinii. Similar to avidin, one mole of streptavidin can bind to 4 moles of biotin with high affinity virtually unmatched in nature. Streptavidin lacks the carbohydrate side chains present on avidin and has an isoelectric point close to neutrality. Therefore, it has a reducing nonspecific binding level compared to avidin. Streptavidin has been widely applied in various biological fields, such as ELISA, IHC, TRFIA, PCR quantification, single-stranded nucleotide isolation, biomolecule purification, and monoclonal antibody production.

Compared to native streptavidin, rc-SA is improved in stability and solubility by removing the sequence unrelated to activity. In addition, a cysteine ​​residue is inserted at the C-terminus of rc-SA for covalent conjugation to the resin.

M : Protein molecular weight marker

Channel 1 : rc-SA subunit

Lane 2 : rc-SA homotetramer

For research only!

Recombinant Core Streptavidin (r-cSA) DataSheet

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