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G4252

Sigma-Aldrich

Glyoxalase I from Saccharomyces cerevisiae

Grade IV, buffered aqueous glycerol solution, ≥400 units/mg protein

Synonym(s):

S-Lactoyl-glutathione methylglyoxal-lyase (isomerizing)

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About This Item

CAS Number:
9033-12-9
Enzyme Commission number:
4.4.1.5 (BRENDA, IUBMB)
MDL number:
MFCD00131225
UNSPSC Code:
12352204
NACRES:
NA.54

type

Grade IV

form

buffered aqueous glycerol solution

specific activity

≥400 units/mg protein

foreign activity

glyoxalase II ≤1%

storage temp.

2-8°C

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General description

Glyoxalase detoxification system consists of glyoxalase (GLO)-I and GLO-II. GLO-I is a cytosolic, 42 kDa, dimeric Zn2+ metalloenzyme.

Application

Glyoxalase I from Saccharomyces cerevisiae has been used as a standard in Glyoxalase I assay for C. dilatata females and brooded encapsulated embryos. It has also been used as a standard for calibration curve generation for quantifying glyoxalase I from brain tissues and cerebral microvessels.

Biochem/physiol Actions

Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner.

Unit Definition

One unit will form 1.0 μmole of S-lactoylglutathione from methylglyoxal and reduced glutathione per min at pH 6.6 at 25 °C.

Physical form

Solution in 50% glycerol, 0.4 M (NH4)2SO4 and 0.002 M KH2PO4 pH 6.5

Analysis Note

Protein determined by biuret.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

G4252-200UN:
G4252-VAR:
G4252-500UN:
G4252-2.5KU:
G4252-5KU:
G4252-1KU:
G4252-BULK:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Hiroya Taniguchi et al.
Molecular cancer therapeutics, 11(10), 2294-2300 (2012-07-13)
Methylglyoxal is an essential component in glycolysis and is known to be an inducer of apoptosis. Glyoxalase I (GLO1) metabolizes and inactivates methylglyoxal. GLO1 is known to be overexpressed in cancer cells and causes resistance to anticancer agents. We show
Lingling Dong et al.
The journal of obstetrics and gynaecology research, 38(8), 1077-1085 (2012-05-01)
Metformin plays an important role in the inhibition of cancer cell growth and prolongs remission durations. It reverses progestin-resistance in endometrial cancer cells by downregulating glyoxalase I (GloI) expression. This study aimed to investigate the effect of metformin on endometrial
Yufeng Wang et al.
Anticancer research, 32(8), 3219-3222 (2012-07-31)
Glyoxalase I (GLO1), an enzyme involved in the detoxification of methylglyoxal in the glycolysis pathway, has been found to be frequently overexpressed in various types of cancer. Recent studies showed that GLO1 is related to proliferation and apoptosis in human
Ravi Gupta et al.
Journal of proteome research, 11(5), 2684-2696 (2012-04-11)
Plants' distribution and productivity are adversely affected by low temperature (LT) stress. LT induced proteins were analyzed by 2-DE-nano-LC-MS/MS in shoot secretome of Hippophae rhamnoides (seabuckthorn), a Himalayan wonder shrub. Seedlings were subjected to direct freezing stress (-5 °C), cold
Miriam Urscher et al.
The FEBS journal, 279(14), 2568-2578 (2012-05-23)
Glucose consumption and therefore methylglyoxal production of human erythrocytes increase significantly upon infection with malaria parasites. The glyoxalase systems of the host-parasite unit cope with this metabolic challenge by catalyzing the removal of harmful methylglyoxal. Thus, glyoxalase 1 from the
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