Analytical Data
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基因名
HRSP12
- Application
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别名
RIDA;HRSP12;2-iminobutanoate/2-iminopropanoate deaminase
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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
P52758
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表达区间
2-137aa
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氨基酸序列
SSLIRRVISTAKAPGAIGPYSQAVLVDRTIYISGQIGMDPSSGQLVSGGVAEEAKQALKNMGEILKAAGCDFTNVVKTTVLLADINDFNTVNEIYKQYFKSNFPARAAYQVAALPKGSRIEIEAVAIQGPLTTASL
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分子量
41.4kDa
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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
HRSP12 (HRSP12 protein) is a protein that plays a crucial role in the cellular response to stress and is particularly involved in the regulation of protein synthesis during stress conditions. Understanding its structure and function is important for elucidating the underlying mechanisms of cellular stress responses, which are relevant in various biological contexts, including development, aging, and disease. Recent studies have suggested that HRSP12 may be implicated in diverse cellular processes, such as apoptosis, cell proliferation, and inflammation. Its association with various diseases, including cancer and neurodegenerative disorders, highlights the necessity of investigating its molecular interactions and signaling pathways. Research into the recombinant expression of HRSP12 protein has gained momentum, as it provides a platform for detailed biochemical analysis and functional studies. This protein's recombinant form can be utilized to dissect its roles in stress granule formation, translational regulation, and overall cellular homeostasis. By employing advanced techniques in molecular biology and biochemistry, scientists aim to characterize HRSP12's properties, interactions with other proteins, and the effects of post-translational modifications. Such studies not only deepen our understanding of the protein's biological functions but may also pave the way for therapeutic innovations targeting HRSP12-related pathways in various diseases. Overall, the exploration of HRSP12 is an emerging field that holds promise for advancing our knowledge of cellular responses to stress and for the development of novel treatment strategies in health and disease contexts.












