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Citations & References (17)
Invitrogen™
Avidin, Egg White
Avidin from egg white is a glycosylated biotin-binding protein that has a basic isoelectric point and is widely used toRead more
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| Catalog Number | Quantity |
|---|---|
| A887 | 100 mg |
| A2667 | 5 mg |
Catalog number A887
Price (EUR)
870,00
Each
Quantity:
100 mg
Price (EUR)
870,00
Each
Avidin from egg white is a glycosylated biotin-binding protein that has a basic isoelectric point and is widely used to detect biotinylated probes.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Quantity100 mg
Shipping ConditionRoom Temperature
ConjugateUnconjugated
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C).
Citations & References (17)
Citations & References
Abstract
Biotin binding to avidin. Oligosaccharide side chain not required for ligand association.
Journal:Biochem J
PubMed ID:3435435
A commercially available, purified preparation of avidin was found to comprise two polypeptide bands (Mr 18,000 and Mr 15,500 respectively). Both bands bound biotin as assessed by biotin overlays of protein blots. The Mr 15,500 polypeptide was found to differ from the Mr 18,000 polypeptide only in its sugar content.
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
Chemical imaging of tissue in vivo with video-rate coherent anti-Stokes Raman scattering microscopy.
Journal:Proc Natl Acad Sci U S A
PubMed ID:16263923
'Imaging living organisms with molecular selectivity typically requires the introduction of specific labels. Many applications in biology and medicine, however, would significantly benefit from a noninvasive imaging technique that circumvents such exogenous probes. In vivo microscopy based on vibrational spectroscopic contrast offers a unique approach for visualizing tissue architecture with
The structure of the complex between avidin and the dye, 2-(4'-hydroxyazobenzene) benzoic acid (HABA).
Journal:FEBS Lett
PubMed ID:8344421
'The crystal structure of the complex formed between the egg-white biotin-binding protein, avidin, and the dye, 2-(4''-hydroxyazobenzene) benzoic acid (HABA), was determined to a resolution of 2.5 A. The interaction of avidin with the benzoate ring of HABA is essentially identical to that of the complex formed between HABA and
Three-dimensional structures of avidin and the avidin-biotin complex.
Journal:Proc Natl Acad Sci U S A
PubMed ID:8506353
'The crystal structures of a deglycosylated form of the egg-white glycoprotein avidin and of its complex with biotin have been determined to 2.6 and 3.0 A, respectively. The structures reveal the amino acid residues critical for stabilization of the tetrameric assembly and for the exceptionally tight binding of biotin. Each