Analytical Data
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基因名
Arginase-2/ARG2
- Application
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别名
Kidney-type arginase; Non-hepatic arginase
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种属
Mouse
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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 90% as determined by SDS-PAGE.
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蛋白编号
O08691
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表达区间
Val23~Ile354
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分子量
37kDa
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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
Arginase-2 (ARG2) is a crucial enzyme that plays a significant role in the urea cycle, responsible for the conversion of arginine to ornithine and urea. This enzyme has gained attention due to its involvement in various physiological and pathological processes, including immune regulation, cancer progression, and cardiovascular diseases. While Arg 1, the other isoform of arginase, primarily operates in the liver, ARG2 is expressed in several tissues and exhibits unique regulatory mechanisms, particularly in immune cells and the tumor microenvironment. The overexpression of ARG2 has been linked to tumor growth and metastasis, as it can modulate the availability of arginine, an amino acid essential for T-cell function and proliferation. Consequently, ARG2 has emerged as a potential therapeutic target, leading to increasing interest in the development of recombinant ARG2 proteins for studying its molecular function, interactions, and potential as a biomarker or therapeutic agent. Characterizing recombinant ARG2 not only enhances the understanding of its enzymatic activity but also facilitates the exploration of its role in various diseases, paving the way for novel treatment strategies aimed at manipulating nitrogen metabolism in pathological conditions.












