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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 (TWD)
14,270.00
Online offer
Ends: 30-Jun-2025
16,700.00Save 2,430.00 (15%)
Each
-
Quantity:
5 mg
Price (TWD)
14,270.00
Online offer
Ends: 30-Jun-2025
16,700.00Save 2,430.00 (15%)
Each
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.
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
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Figures
Bovine pulmonary artery endothelial cells labeled with probes for mitochondria and the phosphorylated form of histone H3.
Madin-Darby canine kidney (MDCK) cells showing the distribution of the tight-junction protein ZO-3 and mitochondria.
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Lot #Certificate TypeDateCatalog Number(s)
3192379Certificate of AnalysisJun 20, 2025S888
2920645Certificate of AnalysisJul 11, 2024S888
2551350Certificate of AnalysisJan 25, 2023S888
2418504Certificate of AnalysisNov 03, 2021S888
2306804Certificate of AnalysisMar 31, 2021S888
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Safety Data Sheets
SDSProduct Information
Molecular Probes® Handbook
Frequently asked questions (FAQs)
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.
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)
Search citations by name, author, journal title or abstract text
Citations & References
Abstract
Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation.
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
Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes.
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
Cell-adhesive properties of streptavidin are mediated by the exposure of an RGD-like RYD site.
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
Cell adhesion to streptavidin via RGD-dependent integrins.
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
A fluorescence resonance energy transfer-based approach for investigating late endosome-lysosome retrograde fusion events.
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
18 total citations