Description

 Streptavidin, Flamma® 496 is a fluorescence labeled biotin binding protein that Flamma® 496 dye is covalently attached to streptavidin. Homotetrameric protein streptavidin (53 KDa) displays high binding affinity (Kd ~ 1014 M) for biotin, and each streptavidin can bind with four biotins by a non-covalent interaction. Streptavidin has a little lower affinity than avidin but displays less non-specific binding due to near-neutral pI value and lack of carbohydrates. Flamma® 496 is a bright green fluorescent dye. Flamma® 496 might be excited using 488 nm laser line. Fluorescent streptavidin–biotin conjugation has been utilized in a wide range of applications such as cell surface labeling, ELISA, immunohistochemistry, affinity purification, FACS, EMSA, etc. The bond formation between biotin and streptavidin is rapid, and the binding is stable at high temperature, in a wide range of pH and denaturing agents. BioActs offers Streptavidin, Flamma® 496 as an effective detecting and analytic probe for diverse applications in medical diagnostics and in vitro analysis.

Specifications

Fluorophore label: Flamma® 496

Reactive group: Streptavidin 

Reacting toward: Biotin

Excitation/Emission Max.(nm): 496/516

Storage conditions: -20 ℃, protect from light

Citation & Reference

1. Ting-Wei Wu. Fluorescent Probe Encapsulated in Avidin Protein to Eliminate Nonspecific Fluorescence and Increase Detection Sensitivity in Blood Serum. Anal Chem 88.16 (2016): 7873-7. 


2. Qian Sun. Discrimination between streptavidin and avidin with fluorescent affinity-based probes. Analyst 140 (2015): 4648-4653.


3. Yung-Peng Wu. Target-activated streptavidin–biotin controlled binding probe. Chem. Sci 9 (2018): 770-776.


4. Akshay Jain. The principles and applications of avidin-based nanoparticles in drug delivery and diagnosis. Journal of Controlled Release 245.10 (2017): 27-40.


5. MEIR WILCHEK. Introduction to Avidin-Biotin Technology. Methods Enzymol 184 (1990): 5-13.


6. JEANNE BENTLEY LAWRENCE. Interphase and Metaphase Resolution of Different Distances Within the Human Dystrophin Gene. Science New Series 249.4971 (1990): 928-932.

OPTION

Added cart

장바구니 아이콘

We put the items
in the shopping cart.