Garantee of highest activity
As Supplier, e-Proteins guarantees the best prices for the highest quality.
Neutralite Avidin is carbohydrate-free and neutral, with the double advantage of the presence of a large number of amino acids available for derivatization, and the absence of RYD sequences. Altogether, these molecular characteristics yield the lowest nonspecific binding among known biotin-binding proteins, yet a specific activity near the theoretical maximum of approximately 16 μg/mg of protein.
The e-Proteins’ Neutralite avidin presents an exceptional specific activity > 15,5 U/mg that competes successfully the steptavidin in many applications. Its process has been improved along the last 5 years R&D program in order to keep all its bio-performances although its process and to offer the best specific activity on the market (generally 14U/mg).
(% w :w)
|< 5.0 %|
|Isoelectric point||6.2 ± 0.2|
|Deglycosylation level||± 90%|
10mg/ml in PBS)
15mg/ml in water)
|Total Bacterial Count|
in 1 mg
|Appearance||White to off white free
powder, free of
any visible impurities
|One Unit activity binds
1 µg of biotin
|Origin||Egg proteins from hens|
Benefit of the neutral isoelectric point
With native avidin, basic proteins stick to negatively charged surfaces by virtue of electrostatic interactions. Although this property can be limited by the addition of salts, most biological tests are conducted under physiological conditions, which are not conducive to eliminating nonspecific absorption. In order to overcome this problem, the isoelectric point of the protein has been reduced to a neutral value under conditions whereby the number of surface lysine residues remains essentially unchanged; the neutral deglycosylated avidin (NeutraLite Avidin) can be used for subsequent derivatization and/or conjugation via lysine residues.
Avantage of Neutralite avidin Vs Streptavidin
No RYD fibronectin-like recognition sequence has been identified in avidin. The latter is responsible for an equivocal interaction between the bacterial Streptavidin and some macromolecular components in many experimental systems. The mechanism of this interaction remained a puzzle for many years, until Alon et al. (1990) showed that Streptavidin contains an Arg-Tyr-Asp (RYD) sequence highly reminiscent of the universal cell surface recognition sequence (Arg-Gly-Asp) present in a variety of adhesion molecules, e.g. fibronectin, vitronectin, fibrinogen, and collagen. Consequently, whereas streptavidin interacts strongly and in a biotin- independent manner with the integrins and related cell surface receptors, avidins do not.