Recombinant Core Streptavidin 2

Mol. Wt.: Subunit 13.3 kDa; Tetramer 53.2kDa

Theoretical pI: 6.09

Theory Activity: 18.3 U/mg protein (r-cSA2:Biotin = 1:4(mol:mol))

Resources: Escherichia coli (E. coli)

Purity: ≥95% by SDS-PAGE analysis

Test Activity: ≥16 U/mg protein (Determined by NUPTEC according to modified Green Method)

A280nm(1 mg/mL): 3.16

Endotoxin: ≤5 EU/mg

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-cSA2 is improved in stability and solubility by the removal of activity-unrelated sequence. Compared with r-csa (NRPA09), the amino acid sequence of this product does not contain cysteine, so it does not need reduction treatment.

M：Protein Molecular Weight Marker

Lane 1：r-cSA2 subunit

Lane 2：r-cSA2 homotetramer

For research use only!