Streptavidin [FITC] (DAG4456)

Streptavidin, FITC-conjugated, synthetic

Product Overview
Streptavidin, FITC-conjugated
Target
Streptavidin
Specificity
Ficoll prepared human peripheral blood lymphocytes, CEM, HPB-MLT, Nalm-6, Jurkat, U-937, Molt-4, Raji, Daudi and KG-1 (cells expressing Fc receptors were pre-blocked with human IgG).
Nature
Synthetic
Tag/Conjugate
FITC
Recommended Usage
Streptavidin can be used in conjunction with biotinylated antibodies as an avidin/biotin labeling system for flow cytometry.
Procedure
None
Purity
Purified streptavidin was covalently conjugated to FITC and the conjugate isolated by size exclusion chromatography. with a FITC to protein molar ratio of 9.0.
Format
Liquid
Concentration
100 μg/mL
Size
120 tests
Buffer
50 mM Sodium Phosphate pH 7.5, 100 mM Potassium Chloride, 150 mM NaCl, 5% Glycerol, 0.2% BSA, 0.04% NaN3 (as a preservative).
Preservative
0.04% Sodium Azide
Storage
Store at 2 - 5°C. Do not freeze! Protect from light. Product should retain activity for at least 12 months after shipping date when stored as recommended.
Warnings
PLEASE note that this product is intended for research use only; not for diagnostic or clinical use.
Introduction
Streptavidin is a 52.8 kDa protein purified from the bacterium Streptomyces avidinii. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin (also known as vitamin B7 or vitamin H). With a dissociation constant (Kd) on the order of ≈10?14 mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Streptavidin is used extensively in molecular biology and bionanotechnology due to the streptavidin-biotin complex's resistance to organic solvents, denaturants (e.g. guanidinium chloride), detergents (e.g. SDS, Triton), proteolytic enzymes, and extremes of temperature and pH.
Keywords
Streptavidin

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References


Lin, JH; Li, M; et al. A high gradient and strength bioseparator with nano-sized immunomagnetic particles for specific separation and efficient concentration of E-coli O157:H7. JOURNAL OF MAGNETISM AND MAGNETIC MATERIALS 378:206-213(2015).
Kim, D; Sahin, O; et al. Imaging and three-dimensional reconstruction of chemical groups inside a protein complex using atomic force microscopy. NATURE NANOTECHNOLOGY 10:264-269(2015).

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