About this item
Streptavidin is a nonglycosylated, tetrameric protein, with each subunit able to bind a single molecule of the vitamin biotin. Streptavidin-biotin bond is the strongest known non-covalent interaction with Kd ~10-15 M. Because streptavidin lacks any carbohydrate modification and has a near-neutral pI, it has the advantage of much lower nonspecific binding than avidin. Streptavidin is broadly used in various applications such as immunoassays, histochemistry, FISH (Fluorescence In Situ Hybridization), flow cytometry, microarrays and blot analysis.
The recombinant streptavidin was expressed in E. coli. It shows one major band about 56 kDa on SDS-PAGE. The activity of recombinant streptavidin is ~17 units/mg, where one unit is defined as the amount of protein required to bind 1.0 g of D-biotin. The extinction coefficient of streptavidin is E1% 280=32; 1 mg/mL A280 = 3.2.
The recombinant streptavidin was expressed in E. coli. It shows one major band about 56 kDa on SDS-PAGE. The activity of recombinant streptavidin is
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Specifications
- Conjugation:Unconjugated
- Protein/Peptide Type:Recombinant
- Source:E. coli
- Species:Bacteria
- Storage Conditions:4 °C
- Gene ID:P02701
- Protein Synonyms:Avidin|Recombinant avidin
- Protein/Peptide Name:Streptavidin
- Molecular Weight:56 kDa