Analytical Data
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基因名
PPIL1
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简介
The PPIL1 protein is a spliceosome component that coordinates pre-mRNA splicing and controls RNA processing. As a peptidylprolyl cis-trans isomerase (PPIase), PPIL1 accelerates protein folding by catalyzing the cis-trans isomerization of proline imide peptide bonds. PPIL1 Protein, Human (His) is the recombinant human-derived PPIL1 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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别名
Peptidyl-Prolyl Cis-Trans Isomerase-Like 1; PPIase; Rotamase PPIL1; PPIL1; CYPL1
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种属
Human
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表达系统
E. coli
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标签
N-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y3C6
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表达区间
M1-G166
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蛋白长度
Full Length
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分子量
19-24 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
PPIL1, or peptidylprolyl isomerase-like 1, is a member of the cyclophilin protein family known for its role in protein folding and chaperone activity. Recent studies have highlighted PPIL1's involvement in various cellular processes, including cell proliferation, apoptosis, and response to stress. Its unique isomerase activity, which catalyzes the cis-trans isomerization of proline residues in polypeptides, is crucial for proper protein conformation and function. Dysregulation of PPIL1 has been linked to several diseases, including cancer, where it may influence tumor progression and metastasis. This has attracted interest in developing PPIL1 as a potential therapeutic target. Moreover, the expression patterns of PPIL1 in different tissues and its interactions with other proteins suggest that it may play a significant role in cellular signaling pathways. Recent advances in recombinant protein technology have enabled the production of PPIL1 in laboratory settings, facilitating detailed studies on its structure and function. Understanding the biochemical properties and physiological roles of PPIL1 through its recombinant form could provide insights into its mechanisms of action and contribute to broader applications in biotechnology and medicine. Research into PPIL1 is expanding our knowledge of essential cellular processes and may pave the way for new strategies in treating diseases associated with protein misfolding and dysfunction.
