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About This Item
CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.32
EC Number:
232-615-7
MDL number:
Biological source:
Saccharomyces cerevisiae
Concentration:
≥0.5 mg/vial protein (E1%/280)
biological source
Saccharomyces cerevisiae
Quality Level
product line
BioReagent
form
lyophilized powder
mol wt
60 kDa
concentration
≥0.5 mg/vial protein (E1%/280)
storage temp.
2-8°C
Application
Invertase Glycoprotein Standard has been used:
- to generate N-linked glycan library
- as a negative control to study the binding of lectins to high mannose structures
- for sample pre-treatment in proteomic analyses to study drug-induced toxic epidermal necrolysis
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
ppe
Eyeshields, Gloves, type N95 (US)
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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)
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)
A lectin affinity workflow targeting glycosite-specific, cancer-related carbohydrate structures in trypsin-digested human plasma
Analytical biochemistry (2011)
Sheila G Valerio et al.
Carbohydrate polymers, 92(1), 462-468 (2012-12-12)
Invertase (E.C.3.2.1.26) from Saccharomyces cerevisiae was covalently immobilized on chitosan nanoparticles prepared by the ionotropic gelation method and activated with glutaraldehyde. The support was characterized and it was studied its load capacity, the influence of the presence of substrate during
Lu Wang et al.
Plant physiology, 160(2), 777-787 (2012-08-07)
Despite substantial evidence on the essential roles of cell wall invertase (CWIN) in seed filling, it remains largely unknown how CWIN exerts its regulation early in seed development, a critical stage that sets yield potential. To fill this knowledge gap
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