protein

GLO1/Glyoxalase I Protein, Mouse (His)

HY-P75162

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

52;88;247;420;1176;1880 USD

GLO1/Glyoxalase I Protein, Mouse (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg;500 μg;1 mg

52;88;247;420;1176;1880 USD

GLO1 is an important enzyme responsible for catalyzing the conversion of hemithiol (the product of methylglyoxal and glutathione) to S-lactoylglutathione. This enzyme activity plays a crucial role in cellular detoxification by mitigating the effects of methylglyoxal, a reactive carbonyl species. GLO1/Glyoxalase I Protein, Mouse (His) is the recombinant mouse-derived GLO1/Glyoxalase I protein, expressed by E. coli , with N-His, N-6*His labeled tag. The total length of GLO1/Glyoxalase I Protein, Mouse (His) is 183 a.a., with molecular weight of ~25 & 48 kDa, respectively.

Mouse

Glyoxalase I (GLO1), also known as lactoylglutathione lyase, is a critical enzyme involved in cellular detoxification processes. GLO1 catalyzes the conversion of hemimercaptal, a compound formed from the reaction between methylglyoxal and glutathione, into S-lactoylglutathione. This enzymatic activity is essential for clearing toxic methylglyoxal, a reactive dicarbonyl compound, and preventing its harmful effects on cellular components. Moreover, GLO1 plays a role in regulating the transcriptional activity of NF-kappa-B, potentially influencing cellular responses to inflammation. Additionally, GLO1 is required for normal osteoclastogenesis, implicating its significance in bone development and remodeling. The multifaceted functions of GLO1 underscore its importance in cellular homeostasis and its potential involvement in various physiological processes.

Lactoylglutathione lyase; Glyoxalase I; Glx I

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.4.

Room temperature in continental US; may vary elsewhere.