Streptavidin, solid

Citations & References (18)

Invitrogen™

Streptavidin, solid

Streptavidin is a bacterially derived biotin-binding protein that reportedly exhibits less nonspecific binding than avidin.Streptavidin is unlabeled, unconjugated, and providedRead more

Catalog Number	Quantity
S888	5 mg

Catalog number S888

Price (MXN)

Quantity:

Streptavidin is a bacterially derived biotin-binding protein that reportedly exhibits less nonspecific binding than avidin.

Streptavidin is unlabeled, unconjugated, and provided as a lyophilized powder.

For Research Use Only. Not for use in diagnostic procedures.

Specifications

Product TypeStreptavidin Conjugate (fluorescent)

Quantity5 mg

Shipping ConditionRoom Temperature

ConjugateUnconjugated

FormSolid

Unit SizeEach

Contents & Storage

Storage Upon Receipt:≤-20°C, desiccate

Frequently asked questions (FAQs)

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.

Citations & References (18)

Citations & References

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

View all Streptavidin, solid citations