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I0408

Sigma-Aldrich

Invertase Glycoprotein Standard

BioReagent, from Saccharomyces cerevisiae, for proteomics

Synonym(s):

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

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About This Item

CAS Number:
9001-57-4
Enzyme Commission number:
3.2.1.26 (BRENDA, IUBMB)
EC Number:
232-615-7
MDL number:
MFCD00131410
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

Saccharomyces cerevisiae

Quality Level

200

grade

for proteomics

product line

BioReagent

form

lyophilized powder

mol wt

60 kDa

concentration

≥0.5 mg/vial protein (E1%/280)

storage temp.

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.

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.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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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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