Recombinant Core Streptavidin

Mol. Wt.: Subunit 13.5 kDa; Tetramer 54kDa

Theoretical pI: 6.04

Theory Activity: 18.1 U/mg protein (r-cSA:Biotin = 1:4(mol:mol))

Resources: Escherichia coli (E. coli)

Purity: ≥95% by SDS-PAGE analysis

Test Activity: ≥15 U/mg protein (Determined by NUPTEC according to modified Green Method)

A280nm(1 mg/mL): 3.136

Storage Condition: -20 ℃

Storage Duration: 3 years

Description: 

Streptavidin is a homotetrameric protein found in the culture broth of Streptomyces avidinii. Similar to avidin, one mole of streptavidin can bind 4 moles of biotin with a high affinity virtually unmatched in nature. Streptavidin lacks carbohydrate side chains present on avidin and has an isoelectric point close to neutrality. Therefore it has a reducing nonspecific binding level as compared to avidin. Streptavidin has been extensively applied in various biological fields, such as ELISA, IHC, TRFIA, quantifying PCR, isolation of single-stranded nucleotide, purification of biomolecule, and monoclonal antibody production as well.

Compared to native streptavidin, r-cSA is improved in stability and solubility by the removal of activity-unrelated sequence. Also, one cysteine residue is inserted at the C-terminus of r-cSA for covalently conjugating to resin.

M:Protein Molecular Weight Marker

Lane 1:r-cSA subunit

Lane 2:r-cSA homotetramer

For research use only!