Neutralite Avidin is a chemically & enzymatically modified avidin characterized by a neutral isoelectric point and the absence of surface glycans. Without RYD segment, Neutralite avidin increases drastically the quality of the IVD’s.

Native – glycosylated & basic – avidin is treated with an endoglycosidase F (Endo-F1) to release the glycans located on each monomer asparagine 17 (Asn-17), leaving a surfacial GlcNAc-Asn residue (see caption under). A chemical mutation transforms a precise number of surfacial arginine (Arg) to nor-lysine (Nor-Lys) residues, and the isoelectric point (pI) is standardized to a neutral – slightly acidic - value. The end product is a highly standardized deglycosylated acetylated avidin, ie Neutralite avidin, characterized by an excellent solubility, absence of non-specific binding properties (lectin affinity, electrostatical interaction, RYD aminoacid sequence) and similar-to-native-avidin number of free surfacial primary amino group for derivatization.

Advantage Neutralite Vs Avidin

- The deglycosylation reduces the affinity of avidin for lecitins to undetectable levels (Hilles at al., 1987). read more

- The neutral isoelectric point of the neutralite avidin enables to conduct tests under physiological condition with the same binding property of native avidin. read more

Advantage Neutralite vs Streptavidin

The benefit of the absence of the RYD segment with Neutralite avidin is an increase of the IVD’s quality by a drastic reduction of false positive results. read more

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 14 μg/mg of protein.