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
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
1 U corresponds to the amount of protein which binds 1μg (+)-biotin at pH 7.5
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
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
D.A. Fuccillo
Biotechniques, 3, 494-494 (1985)
Soon Gang Choi et al.
Nature communications, 10(1), 3907-3907 (2019-08-31)
Complementary assays are required to comprehensively map complex biological entities such as genomes, proteomes and interactome networks. However, how various assays can be optimally combined to approach completeness while maintaining high precision often remains unclear. Here, we propose a framework
Scientific and Clinical Applications of Magnetic Carriers (2013)
Capture and identification of heterogeneous circulating tumor cells using transparent nanomaterials and quantum dots-based multiplexed imaging
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)
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