Recombinant Human Lactoylglutathione Lyase (GLO1) Protein (GST)

Name: Recombinant Human Lactoylglutathione Lyase (GLO1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03503P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Lactoylglutathione Lyase (GLO1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q04760
Target Symbol	GLO1
Synonyms	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 methylglyoxal lyase ; S-D-lactoylglutathione methylglyoxal lyase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM
Expression Range	1-184aa
Protein Length	Full Length
Mol. Weight	47.8kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis.
Protein Families	Glyoxalase I family
Database References	HGNC: 4323 OMIM: 138750 KEGG: hsa:2739 STRING: 9606.ENSP00000362463 UniGene: Hs.268849

Gene Functions References

GLO1 SNPs, rs1130534 (c.372A>T, p.G124G), rs2736654 (c.A332C, p.E111A) and rs1049346 (c.-7C>T, 5'-UTR) were genotyped. While c.A332C polymorphism was not associated with retinitis pigmentosa (RP), c.372A>T showed an allelic association. Conversely, c.-7C>T showed both genotypic and allelic associations. RP susceptibility may be associated with two of the analyzed GLO1 polymorphisms (rs1130534 and rs1049346). PMID: 30099685
The active sites of human and staphylococcus glyoxalases I are also different: the former contains one Zn-ion per chain; the latter incorporates two of these ions.. We suggest that only single Zn1-ion plays the role of catalytic center. The newly found differences between the two subfamilies could guide the design of new drugs against S. aureus, an important pathogenic micro-organism. PMID: 28034013
This study shows that only the GLO1 C-7T polymorphism, and not the GLO1 A419C and ALR C-106T polymorphisms, is associated with carotid atherosclerosis in Chinese patients with type 2 diabetes. PMID: 21294693
The expression of glyoxalase system member glyoxalase 1 (GLO1) in melanoma cells is downregulated by miR-137. siRNA targeting of GLO1 mimicks inhibition of melanoma cell proliferation caused by miR-137 overexpression. Re-expression of GLO1 restores miR-137-mediated suppression of melanoma cell proliferation. PMID: 29307109
The critical role of glyoxalases as regulators of tumorigenesis in the prostate through modulation of various critical signaling pathways, and an overview of the current knowledge on glyoxalases in bladder, kidney and testis cancers is reviewed.(GLO1, GLO2) PMID: 29385039
Inhibition of GLO1 in Glioblastoma Multiforme Increases DNA-AGEs, Stimulates RAGE Expression, and Inhibits Brain Tumor Growth in Orthotopic Mouse Models PMID: 29385725
current research highlighted the Glo-I/AGE/RAGE system as an interesting therapeutic target in chronic liver diseases. These findings need further elucidation in preclinical and clinical studies. PMID: 29156655
GLO1-knockdown provoked collagen expression, endothelial inflammation and dysfunction and apoptosis which might contribute to vascular damage PMID: 27898103
expressed in basal epidermis; significantly higher expression in older individuals PMID: 26914966
Interdependence of GLO I and PKM2 in the Metabolic shift to escape apoptosis in GLO I-dependent cancer cells. PMID: 29225125
Induced Glyoxalase 1 expression is a common feature in the pathogenesis of oropharyngeal squamous cell carcinoma PMID: 28549423
The lowering of glycative stress via modulation of RAGE-AGE axis or glyoxalase 1 activity is beneficial for tubular homeostasis and the subsequent prevention and treatment of kidney disease, suggesting the possibility of novel therapeutic approaches which target glycative stress. PMID: 27270765
Glo-1 responds to dicarbonyl stress to enhance cytoprotection at the transcriptional level through stress-responsive increase of Glo-1 expression. PMID: 27406712
Glo1, together with Glo2, represents a novel mechanism in prostate cancer progression driven by a PTEN/PI3K/AKT/mTOR signaling pathway. PMID: 27696457
Gly82Ser and 2184 A/G RAGE polymorphisms were related to the mortality due to the breast cancer and -419 A/C glyoxalase I polymorphism was related to the overall mortality of the patients suggesting their role not only in the risk of breast cancer but also in the outcome of patients with breast cancer. PMID: 28695773
Reduction of GLO1 activity in atherosclerotic lesions of nondiabetic patients with increased HbA1c is associated with a functional involvement of this protective enzyme in atherogenesis. PMID: 27478003
Studies suggest that the enhancement of glyoxalase I (GLO-1) is a promising strategy aimed at halting the vicious cycle between chronic kidney disease and increases in glycative stress. PMID: 28106734
GLO1 on one hand is crucial to maintaining tumor characteristics of malignant cells, and, on the other hand, supports malignant transformation of cells in a hypoxic environment when overexpressed. PMID: 27999356
GLO1 SNPs are significantly associated with late-onset and drug-resistant epilepsy. PMID: 27000251
MS5 induced hydrogen peroxide-mediated c-Jun-dependent Glo1 up-regulation which resulted in a decrease in the Argpyrimidine-modified Hsp70 protein level which triggered EMT in a novel mechanism involving miR-21 and SMAD signalling PMID: 26784015
MMP-9 and Bcl-2 expression levels were dramatically decreased by addition of methylglyoxal or inhibition of GLOI. These findings may provide a new approach for the treatment of breast cancer. PMID: 26618552
Data suggest Glo1's effects on anxiety-like behavior are centrally mediated as overexpression of Glo1 in neurons was sufficient to increase anxiety-like behavior PMID: 26711908
Studies indicate that the most extensively investigated The most extensively investigated glyoxalase enzymes are glyoxalase I and glyoxalase II (Glo1 and Glo2). PMID: 26552067
The GLO1 variations were not the source of association of the BTBD9 locus with restless legs syndrome. PMID: 26298793
Glo1 is involved in the Min-U-Sil 5 crystalline silica-induced BEAS-2B cell mitochondrial apoptotic pathway. PMID: 25841781
Two classes of the metalloenzyme GlxI exist and vary in their metal dependencies PMID: 25557363
GLO1 activity affects the overall burden of carotid artery atherosclerosis. PMID: 24767709
individuals with the GLO1 A /E genotype, PON192/QR-RR genotypes and PON55/LM-MM genotypes had a significantly higher risk of cerebral cavernous malformations compared with the other genotypes. PMID: 26122242
This study demonstrated that the GLO1 C332 (Ala111) allele confers autism vulnerability by reducing brain glyoxalase activity and enhancing advanced glycation end-products. formation PMID: 25201284
This review describes the role of GLO1 in tumor cell proliferation and survival, and the potential of GLO1 as a biomarker for tumor diagnosis and as a target for anticancer drug development. [review] PMID: 25342507
Significant differences in the allelic and genotype frequencies of GLO1. PMID: 25407489
In ApoE(-/-) mice with or without diabetes, GLO1 overexpression did not lead to decreased atherosclerotic lesion size or systemic inflammation. PMID: 25139743
Data show that GlxI is a novel substrate of TG2 and TG2 catalyzes either polyamine conjugation or deamidation depending the presence of polyamines. PMID: 24494193
results suggested involvement of accumulated dicarbonyls and/or pentosidine in the pathophysiology of schizophrenia patients carrying Glyoxalase-1 mutations. PMID: 24995521
Study demonstrates that GLO1 is a novel metabolic oncogene of the 6p21 amplicon, which promotes tumor growth and aberrant transcriptional signals via regulating cellular metabolic activities for energy production. PMID: 24662817
GLO1 lessened inhibitory phosphorylation of eNOS (Thr495) by reducing glycative stress. Study demonstrates that blunting glycative stress prevents the long-term impact of endothelial dysfunction on vascular aging. PMID: 24612481
GLO1 is prevailingly expressed in cutaneous neoplasms of higher malignancy and contributes to the progression of squamous cell carcinoma PMID: 25184957
Weak association of glyoxalase 1 (GLO1) variants with autism spectrum disorder PMID: 24671236
Suggest Glo1 pathway activation is required for cell proliferation and cell survival of hepatocellular carcinoma cells carrying Glo1 genetic amplification. PMID: 24966916
Report association of GLO1 (rs4746) polymorphism with markers of endothelial activation in diabetes mellitus. PMID: 24908234
Overexpression of GLO1 in bone marrow cells is sufficient to overcome the defective neovascularization that is characteristic of diabetes. PMID: 24259499
Overall, thus Glo1 might be essential for hepatocellular carcinoma progression and can be designated as a potential therapeutic target for hepatocellular carcinoma in the future. PMID: 24158671
level by differently inhibiting GI via NF-kappaB.Superoxide anion and hydrogen peroxide induced a diverse apoptosis. PMID: 24002659
we provided evidence of the biological plausibility of Glyoxalase 1 polymorphism, either alone or in combination with other ones, all related to oxidative stress control that represents a key event in PCa development and progression. PMID: 24040147
GLO1 was the only protein which consistently varied according to the metastatic potentials of SN12C clones. GLO1 was increased in high metastatic cell lines by western blot analysis. PMID: 23982595
data suggest a possible association of C332C-genotype of the glyoxalase 1 gene with diabetic neuropathy in type 2 diabetes, supporting the hypothesis that methylglyoxal might be an important mediator of diabetic neuropathy in type 2 diabetes. PMID: 23775136
GLO1 expression level in prostate cancer tissues correlates with pathological grade and proliferation rate. PMID: 24105621
Data suggest that GLO1 activity is lower in blood (in whole blood assay) in type 1 or type 2 diabetes with painful peripheral diabetic neuropathy as compared to control subjects; Glo1 activity negatively correlates with duration of type 1 diabetes. PMID: 23351995
The Ala111Glu glyoxalase gene polymorphism did not have an effect on glyoxalase 1 activity in either the type 1 diabetes mellitus or healthy control group. PMID: 23360186
No evidence of an association of RAGE or glyoxalase I single nucleotide polymorphisms with pathological pregnancy. PMID: 22771726

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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