链霉素亲和素,固体
链霉素亲和素,固体
Invitrogen™

链霉素亲和素,固体

链霉亲和素是一种细菌来源的生物素结合蛋白,据报告非特异性结合比例低于亲和素。链霉亲和素以未标记、未偶联的冻干粉末形式提供了解更多信息
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货号数量
S8885 mg
货号 S888
价格(CNY)
5,543.00
Each
添加至购物车
数量:
5 mg
价格(CNY)
5,543.00
Each
添加至购物车
链霉亲和素是一种细菌来源的生物素结合蛋白,据报告非特异性结合比例低于亲和素。

链霉亲和素以未标记、未偶联的冻干粉末形式提供。
仅供科研使用。不可用于诊断程序。
规格
产品类型链霉素亲和素偶联物(荧光)
数量5 mg
运输条件室温
偶联物未偶联
形式实心
Unit SizeEach
内容与储存
收货储存条件:≤-20°C,干燥

常见问题解答 (FAQ)

How many biotin binding-sites are there per streptavidin molecule?

Streptavidin is a protein composed of four identical subunits, each containing a high affinity binding site for biotin (K-D = 10 -15 M) . Streptavidin has the same biotin binding properties as avidin, but it has a low isoelectric point (pI=5) and no carbohydrate groups, resulting in low non-specific binding.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Is Streptavidin (Cat. No. S888, 434302, and 434301) RNAse-free?

Although we utilize manufacturing methods that minimize the introduction of any contaminants such as RNases, we do not process this product to specifically remove or inactivate RNases and do not test for RNase activity.

Find additional tips, troubleshooting help, and resources within our Cell Analysis Support Center.

引用和文献 (18)

引用和文献
Abstract
Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation.
Authors:Hirsch JD, Eslamizar L, Filanoski BJ, Malekzadeh N, Haugland RP, Beechem JM, Haugland RP
Journal:Anal Biochem
PubMed ID:12419349
'The high-affinity binding of biotin to avidin, streptavidin, and related proteins has been exploited for decades. However, a disadvantage of the biotin/biotin-binding protein interaction is that it is essentially irreversible under physiological conditions. Desthiobiotin is a biotin analogue that binds less tightly to biotin-binding proteins and is easily displaced by ... More
Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes.
Authors:Tortorella D, Sesardic D, Dawes CS, London E
Journal:J Biol Chem
PubMed ID:7499201
'Diphtheria toxin undergoes membrane insertion and translocation across membranes when exposed to low pH. In this study, the translocation of the toxin has been investigated by the binding of antibodies to two preparations of model membrane-inserted toxin. In one preparation, toxin was added externally to model membrane vesicles and then ... More
Cell-adhesive properties of streptavidin are mediated by the exposure of an RGD-like RYD site.
Authors:Alon R, Bayer EA, Wilchek M
Journal:Eur J Cell Biol
PubMed ID:1425765
'The interaction of streptavidin with various cell systems was studied using fluorescent derivatives of the protein. The native unprocessed form of streptavidin bound to cells at low levels and in a nonspecific manner. In contrast, both the truncated "core" streptavidin (the commercially available form) and the biotin-blocked unprocessed protein bound ... More
Cell adhesion to streptavidin via RGD-dependent integrins.
Authors:Alon R, Bayer EA, Wilchek M
Journal:Eur J Cell Biol
PubMed ID:8462588
'Biotin-blocked streptavidin binds specifically (Kd approximately 3 x 10(-8) M) to cell surfaces, presumably via an RYD-containing sequence. This site is distinct from the biotin-binding cleft of the protein and bears high homology to the RGD-containing cell-binding domain of fibronectin. We show here that various cell types adhere to immobilized ... More
A fluorescence resonance energy transfer-based approach for investigating late endosome-lysosome retrograde fusion events.
Authors:Kaufmann AM, Goldman SD, Krise JP,
Journal:Anal Biochem
PubMed ID:19109922
'Traditionally, lysosomes have been considered to be a terminal endocytic compartment. Recent studies suggest that lysosomes are quite dynamic, being able to fuse with other late endocytic compartments as well as with the plasma membrane. Here we describe a quantitative fluorescence energy transfer (FRET)-based method for assessing rates of retrograde ... More