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Principaux documents

I0408

Sigma-Aldrich

Invertase Glycoprotein Standard

BioReagent, from Saccharomyces cerevisiae

Synonyme(s) :

Invertase from baker’s yeast (S. cerevisiae), β-D-Fructofuranosidase, β-D-Fructofuranoside fructohydrolase, Saccharase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

Saccharomyces cerevisiae

Niveau de qualité

Gamme de produits

BioReagent

Forme

lyophilized powder

Poids mol.

60 kDa

Concentration

≥0.5 mg/vial protein (E1%/280)

Température de stockage

2-8°C

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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.

Actions biochimiques/physiologiques

Invertase hydrolyzes sucrose into glucose and fructose yielding a colorless product, unlike acid hydrolysis which produces colored products.

Autres remarques

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.

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

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)
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)
Rachel Morissette et al.
Bioscience reports, 32(6), 577-586 (2012-09-04)
In eukaryotes, GPI (glycosylphosphatidylinositol) lipid anchoring of proteins is an abundant post-translational modification. The attachment of the GPI anchor is mediated by GPI-T (GPI transamidase), a multimeric, membrane-bound enzyme located in the ER (endoplasmic reticulum). Upon modification, GPI-anchored proteins enter
Nayan J Sarma et al.
Nucleus (Austin, Tex.), 3(6), 508-515 (2012-10-11)
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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