as a negative control to study the binding of lectins to high mannose structures[2]
for sample pre-treatment in proteomic analyses to study drug-induced toxic epidermal necrolysis[3]
The Invertase Glycoprotein Standard can be used to demonstrate N-glycosylation using PNGase F with both in-solution and in-gel procedures. The extent of deglycosylation can be assessed by mobility shift on SDS-PAGE gels.
Used in the production of confectionary foods and artificial honey.
Biochem/physiol Actions
Invertase hydrolyzes sucrose into glucose and fructose yielding a colorless product, unlike acid hydrolysis which produces colored products.
Other Notes
Invertase is an enzyme that catalyses the hydrolysis of sucrose into fructose and glucose. Invertase Glycoprotein Standard is the periplasmic (glycosylated form, external invertase) with 50% of its mass as polymannan. Since yeast can provide an alternative system for protein glycosylation that is similar to mammalian systems, periplasmic invertase is often used as a model for the study of the function of oligosaccharides in glycoproteins and for studies on glycoprotein biosynthesis.
Proteomic kinetic analysis of blister fluid and serum in a patient with drug-induced toxic epidermal necrolysis. A comparison with skin immunohistochemistry
Paquet P, et al.
Current Drug Safety (2012)
Glycan characterization of the NIST RM monoclonal antibody using a total analytical solution: From sample preparation to data analysis
Hilliard M, et al.
MAbs (2017)
A lectin affinity workflow targeting glycosite-specific, cancer-related carbohydrate structures in trypsin-digested human plasma
Journal of biosciences, 37(6), 1079-1088 (2012-11-16)
We correlated root growth inhibition with aluminium (Al(3+)) localization and toxicity symptoms in rice roots using seedlings of two genotypes (tolerant and sensitive) that were exposed to different AlCl(3) concentrations. Al(3+) localization was evaluated by hematoxylin in primary roots and
Transcriptional regulation is a complex process that requires the integrated action of many multi-protein complexes. The way in which a living cell coordinates the action of these complexes in time and space is still poorly understood. Recent work has shown
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