Analytical Data
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基因名
Chymase/CMA1
- Application
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别名
CYH; CYM; Alpha-chymase; Mast cell protease I
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P23946
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表达区间
Ile22~Asn247
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分子量
29kDa
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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 an essential enzyme involved in the detoxification of methylglyoxal, a reactive dicarbonyl compound that can result from glycolysis and other metabolic processes. Elevated levels of methylglyoxal are linked to various pathophysiological conditions, including diabetes, neurodegenerative diseases, and cancer. As such, GLO1 plays a critical role in cellular defense against glycation and oxidative stress, thereby maintaining cellular homeostasis. The interest in GLO1 has surged, prompting researchers to focus on the recombinant production of this enzyme for both functional studies and therapeutic applications. By utilizing recombinant DNA technology, scientists can express GLO1 in suitable host systems, such as bacteria or yeast, allowing for the generation of large quantities of pure protein. This enables detailed biochemical characterization, kinetic studies, and investigation into the enzyme's mechanisms and regulation. Moreover, recombinant GLO1 can be used to explore its potential as a therapeutic target or biomarker in diseases associated with elevated methylglyoxal levels. Overall, the study of recombinant GLO1 not only enhances our understanding of its biological function but also opens avenues for novel strategies in treating glycation-related disorders.
