Neutralite avidin
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 Neutralite avidin (NLA), currently sold through large global distributors’ platforms, presents a polymerization ratio variable from one lot to the other. Therefore, when neutralite avidin is used in specific diagnostic applications, this variability can impact test results.
Having received several customer requests for both more polymerized and less polymerized lots, e-Proteins has launched a R&D project to master the Neutralite avidin polymerization and therefore better respond to its customers’ expectations.
After more than five years of research, e-Proteins has implemented a new approach that separates the production of neutralite avidin from its polymerization. By separating both processes, e-Proteins manages to develop two new products with distinct specifications.
For its neutralite avidin , e-proteins focuses its efforts on the deglycolisation level in order to reduce as much as possible the non-specific binding and on the activity of the proteins. So the e-Proteins’ Neutralite avidin presents an exceptional specific activity > 15,5 U/mg that competes successfully the steptavidin in many applications with a deglycolisation level around 95% . 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 comparing the neutralite avidin available on the market (generally 14U/mg for the specific activity and 90% of deglycolisation).
Product competitor : streptavidin (from the bacterium Streptomyces avidinii)
Prices
Specifications
| Physicochemistry | NAX100 |
|---|---|
| Purity | 100% |
| Activity (U/mg solid) | > 15,5 |
| Moisture content (% w :w) | < 5.0 % |
| Isoelectric point | 6.2 ± 0.2 |
| Deglycosylation level | ± 90% |
| Dimer | < 10% |
| Solubility (transmittance @650nm 10mg/ml in PBS) | >95% |
| Solubility (transmittance @650nm 15mg/ml in water) | >95% |
| Microbiology | NAX100 |
|---|---|
| Total Bacterial Count in 1 mg | < 1 |
| Other | NAX100 |
|---|---|
| Appearance | White to off white free flowing lyophilised powder, free of any visible impurities |
| Definition of activity | One Unit activity binds 1 µg of biotin |
| Country of Manufacturing | Belgium |
| 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.