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P0872S, N-Glycopeptide Binding Protein - 1 mg
2.463,30 RON
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.
SKU
NEB_P0872S
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. 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.
Product Source
An E. coli strain that carries human Fbs1 mutant gene.
Properties & Usage
Storage Buffer
20 mM Tris-HCl
50 mM NaCl
0.2 mM TCEP
pH 8
Heat Inactivation: No
Molecular Weight: Theoretical- 45 kDa
Unit Assay Conditions
Functional Testing (N-Glycan Enrichment) - A 200 μL reaction in 20 mM Tris-HCl, 50 mM NaCl, 0.2 mM TCEP, 10% acetonitrile, pH 8.0 containing 1 nmol of fluorescently labeled sialylglycopeptide and 100 μg N-Glycopeptide Binding Protein incubated for 30 minutes at 4°C results in ≥40% enrichment as determined by UV-Vis Spectroscopy at 520 nm.
Advantages and Features
Features
- 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, unlike other lectin affinity chromatography (LAC) techniques, HILIC, or other lectin-based enrichment methods
- Significantly increased glycopeptide spectrum match and glycoprotein ID and discovery
- Versatile workflow
Mai multe informatii
| Price | 2.070,00 RON (preturile sunt fara TVA) |
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| Description |
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. 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. Product Source An E. coli strain that carries human Fbs1 mutant gene. Properties & Usage Storage Buffer 20 mM Tris-HCl Heat Inactivation: No Molecular Weight: Theoretical- 45 kDa Unit Assay Conditions Functional Testing (N-Glycan Enrichment) - A 200 μL reaction in 20 mM Tris-HCl, 50 mM NaCl, 0.2 mM TCEP, 10% acetonitrile, pH 8.0 containing 1 nmol of fluorescently labeled sialylglycopeptide and 100 μg N-Glycopeptide Binding Protein incubated for 30 minutes at 4°C results in ≥40% enrichment as determined by UV-Vis Spectroscopy at 520 nm. Advantages and Features Features
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