Analytical Data
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基因名
GLO1
- Application
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别名
GLO1;Lactoylglutathione lyase
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q04760
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表达区间
1-184aa
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氨基酸序列
MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYT RVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLE LTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFV KKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM
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分子量
21 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Glyoxalase I (GLO1) is a key enzyme in the detoxification of methylglyoxal (MG), a reactive dicarbonyl compound generated as a byproduct of glycolysis. Elevated levels of MG are associated with various diseases, including diabetes, neurodegenerative disorders, and cancer, due to its ability to induce protein glycation and oxidative stress. GLO1 catalyzes the conversion of MG and reduced glutathione into S-D-lactoylglutathione, thereby protecting cells from MG-induced damage. The study of recombinant GLO1 has gained significant interest as it offers insights into the enzyme's structure-function relationship, catalytic mechanisms, and potential as a therapeutic target. Advances in molecular biology and protein expression systems have facilitated the production of recombinant GLO1, enabling detailed kinetic and biochemical analyses. Researchers aim to elucidate the role of GLO1 in human health and disease, explore its potential as a biomarker, and develop novel therapeutic strategies that enhance its activity or mimic its function to mitigate MG-related pathologies. Understanding the regulation of GLO1 and its interplay with other cellular pathways may pave the way for innovative treatments in conditions where MG accumulation is detrimental.
