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Overview
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Lectenz® are a novel class of lectin-like, enzyme-derived glycan-targeting affinity reagents engineered by computationally-guided directed evolution. The reagents are highly purified recombinant proteins, each designed to bind a specific glycan structure, and have advantages over naturally occurring lectins in rapid detection and enrichment of glycoconjugates.
SiaFind™ Pan-Specific Lectenz® 2.0 Kits contain a high-performance sialic acid affinity reagent engineered from the original SiaFind™ Pan-Specific Lectenz® for the robust detection, separation, or enrichment of sialoglycans terminating in Siaα2,3Gal, Siaα2,6Gal, and Siaα2,8Sia commonly found in glycoconjugates (glycoproteins, glycolipids, and oligo- or polysaccharides). It has high affinity and specificity towards sialoglycans in a linkage independent manner (pan-specific). Each kit also includes a 5X binding buffer to ensure maximum reagent specificity and ease of use.
SiaFind™ Pan-Specific Lectenz® 2.0 has a molecular mass of about 57 kD and works as a monomer without bivalent metal ions. It is 8xHis-tagged at its N-terminus, and an anti-polyhistidine antibody, or in the case of the biotinylated version, a streptavidin conjugate can be used for detection. The 8xHis tag may be removed by FasTEV™, a TEV protease with enhanced stability and catalytic activity.
The original SiaFind™ Pan-Specific Lectenz® has a molecular mass of about 77 kD and works as a monomer without bivalent metal ions. It is 6xHis-tagged at its N-terminus, and an anti-polyhistidine antibody, or in the case of the biotinylated version, a streptavidin conjugate can be used for detection.Please contact us at for specific academic pricing.
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- Properties
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Overview