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.
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.
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