N-Glycopeptide Binding Protein, also known as Fbs1-GYR lectin, is engineered to selectively bind and enrich a wide variety of N-glycopeptides in a complex proteomic sample to assist N-glycoprotein identification and discovery, without requiring the use of traditional lectin affinity chromatography (LAC) techniques, HILIC columns, or cartridges.

• Engineered lectin, a glycan-binding protein that recognizes a wide variety of N-glycoforms
• For enrichment and identification of glycopeptides and glycoproteins
• Selectively binds and enriches N-glycopeptides in a complex proteomics sample
• Does not require lectin affinity chromatography (LAC), HILIC
• Significantly increased glycopeptide spectrum match and glycoprotein ID and discovery

This engineered lectin, originating from human Fbs1 protein, exhibits improved specificity towards high mannose, complex, and hybrid N-glycans, as well as towards fucosylated and non-fucosylated, sialylated and non-sialylated, with bi-, tri- and tetra-antennary structures. N-Glycopeptide Binding Protein includes a SNAP tag for immobilizing to create versatile workflows. 1ml of protein at 1 mg/ml Source: An E. coli strain that carries human Fbs1 mutant gene.

Storage buffer: 20 mM Tris-HCl, 50 mM NaCl, 0.2 mM TCEP
pH: 8.0
Heat inactivation: No