Analytical Data
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基因名
AKR1CL1
- Application
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别名
AKR1C8P; AKR1CL1Putative aldo-keto reductase family 1 member C8; Aldo-keto reductase family 1 member C-like Protein 1; EC 1.1.1
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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
Q5T2L2
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表达区间
1-129aa
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氨基酸序列
MMTDLKQSHS VRLNDGPFMP VLGFGTYAPD HTPKSQAAEA TKVAIDVGFR HIDSAYLYQN EEEVGQAIWE KIADGTVKRE EIFYTIKLWA TFFRAELVHP ALERSLKKLG PDYVDLFIIH VPFAMKGSS
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分子量
14 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
AKR1CL1 (Aldo-keto reductase family 1 member C1) is a significant enzyme belonging to the aldo-keto reductase superfamily, which plays a crucial role in the metabolism of various endogenous and exogenous compounds. This enzyme is involved in the reduction of aldehydes and ketones, contributing to the detoxification processes within cells and influencing steroid hormone metabolism. Recent studies have highlighted AKR1CL1's potential role in cancer biology, particularly in tumor progression and resistance to chemotherapy, making it a target for research within oncology. The recombinant expression and purification of AKR1CL1 allow researchers to investigate its enzymatic properties, substrate specificity, and structural characteristics. Understanding the biochemical functions and regulatory mechanisms of AKR1CL1 can lead to insights into its physiological roles and potential implications in drug development. Additionally, elucidating the structural basis of its interactions with various ligands could provide critical information for designing specific inhibitors, which could enhance therapeutic strategies against diseases associated with dysregulated AKR1CL1 activity. Given the increasing interest in the enzyme's involvement in diverse biological contexts, the study of AKR1CL1 as a recombinant protein is essential for advancing our understanding of its function and therapeutic potential.
