85878
Streptavidin from Streptomyces avidinii
affinity purified, lyophilized from 10 mM potassium phosphate, ≥13 U/mg protein
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About This Item
form
powder
Quality Level
quality
affinity purified
lyophilized from 10 mM potassium phosphate
specific activity
≥13 U/mg protein
mol wt
Mr ~60000
solubility
H2O: 1 mg/mL, clear to hazy, colorless to faintly yellow
storage temp.
−20°C
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General description
Streptavidin is a crystalline protein synthesized by Streptomycetes.
Application
Streptavidin from Streptomyces avidinii has been used:
- in the pre-functionalization of self-propelled catalytic micromotors
- in the fabrication and modification of hydroxyapatite-chitosan (HA-CTS) nanofilm-coated substrates
- as an analyte to bind biomolecules to the gold-inverted polymer solar cells (Au-IPSC)
Biochem/physiol Actions
Streptavidin is a biotin binding protein and has the ability to bind four molecules of biotin. The biotin binding pocket of streptavidin helps to interact with biotin. It can be used to enhance protein binding and multimerization.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
The sales quantitites 1 mg and 5 mg
Unit Definition
1 U corresponds to the amount of protein which binds 1μg (+)-biotin at pH 7.5
Analysis Note
Binding capability: Streptavidin binds one molecule of biotin per subunit. Comparison of biotin binding and absorbance measurements indicates that ≤5% binding sites are occupied.
Other Notes
Review: Application of the avidin-biotin technique in microbiology; Protein isolated from the bacterium Streptomyces avidinii, having a high affinity for biotin; Avidin-Biotin technology
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Soon Gang Choi et al.
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Chen Y Y, et al.
Journal of Cancer, 7(1), 69-69 (2016)
M. Wilchek and E.A. Bayer, eds.
Methods of Enzymatic Analysis, 184 (1990)
D.A. Fuccillo
Biotechniques, 3, 494-494 (1985)
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