Streptavidin / ˌstrɛpˈtævɪdɪn / is a 52 kDa protein (tetramer) purified from the bacterium Streptomyces avidinii. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin (also known as vitamin B7 or vitamin H).
Streptavidin is a tetrameric protein isolated from the bacterium Streptomyces avidinii. It’s highly known for its lesser non-specific binding with the biotin (or Vitamin H) molecule. The protein has a molecular weight of 60 kDa.
Learn about streptavidin, a protein whose remarkably specific interaction with biotin is harnessed by scientists as a core tool for molecular detection.
Streptavidin is a bacterially derived biotin-binding protein that reportedly exhibits less nonspecific binding than avidin. Capacity: Binding activity of streptavidin is determined to be >11 units per mg protein.
Streptavidin is a biotin-binding protein found in the culture broth of the bacterium Streptomyces avidinii. Like its namesake, avidin, streptavidin binds 4 moles of biotin per mole of protein with a high affinity virtually unmatched in nature (K d 10 -15 M).
Streptavidin is a 60-kDa protein that was purified from the well-known bacterium Streptomyces avidinii. It is a homotetrameric protein with dihedral D 2 symmetry (Fig. 8 A; PDB: 1STP). It has four sites with an extraordinarily high affinity for the nutrient termed biotin (also known as vitamin B7).
In this study, streptavidin was expressed in Escherichia coli (E. coli) BL21 (DE3) pLysS cells and purified by affinity chromatography. Various dialysis methods were employed to enable the protein to refold to its natural form and create a strong bond with biotin.
Streptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites (Figure 1). Each monomer is roughly 13kDa, forming an approximately 52 to 55 kDa homo tetramer in its native state.