Recombinant Human GLO1 Protein

重组人GLO1蛋白 | 重组人乙二醛酶Ⅰ蛋白

Aldoketomutase | glo1 | GLOD1 | Glx I | GLYI | glyoxalase domain containing 1 | Glyoxalase I | Ketone aldehyde mutase | Ketone-aldehyde mutase | Lactoyl glutathione lyase | Lactoylglutathione lyase | LGUL_HUMAN | Methylglyoxalase | S D lactoylglutathione

rp184954-10μg

10μg

无载体

≥95%(SDS-PAGE)

Glyoxalase I (also lactoylglutathione lyase, methylglyoxalase, and glx I) is a 21 kDa member of the Glyoxalase I family. The enzyme is an isomerase that catalyzes the formation of S-D-lactoylglutathione from the hemimercaptal adduct that forms spontaneously between methylglyoxal and reduced GSH. The monomeric subunit for human Glyoxalase I is 184 amino acids (aa) in length. In the mature protein, the methionine at the N-terminus is removed. Human Glyoxalase I exists in three separable isoforms as homo-and hetero-dimers of two allelic subunit variants, which differ in charge. The isoforms are formed when residue 19 is changed from cysteine to tyrosine and residue 111 is changed from glutamine to alanine. Each subunit binds one Zn2+ atom. The protein is made up of multiple beta strands and alpha helical regions. Human Glyoxalase I shares 91% and 90% aa sequence identity with rat and mouse Glyoxalase I, respectively. The enzyme is ubiquitously expressed and is also present in many tumor cell lines, in which its concentration is often upregulated. The biological role of the enzyme remains unclear, but the glyoxalase system detoxifies the precursors of advanced glycation end products, which take part in the pathogenesis of vascular, diabetic, and uremic complications. Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed:20454679, PubMed:23122816, PubMed:9705294). Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (PubMed:19199007). Required for normal osteoclastogenesis (By similarity). Post-translational: Glutathionylation at Cys-139 inhibits enzyme activity.Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B.Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B.

Measured by its ability to catalyze the formation of S-D-lactoylglutathione from the hemimercaptal adduct that forms spontaneously between methylglyoxal and reduced glutathione. The specific activity is >100 nmol/min/µg, as measured under the described conditions.​

重组表达

21.6 kDa

N-His

24.8 & 48.1 kDa, under reducing conditions; 24.8 & 48.1 kDa, under non-reducing conditions.

E. coli Accession #: Q04760 | E. coli

<1.0 EU/μg

人(Human)

2-184 aa

MHHHHHHAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM

No

Yes