Analytical Data
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基因名
POMP
- Application
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别名
PNAS-110; UMP1; Proteassemblin; Protein UMP1 homolog; Voltage-gated K channel beta subunit 4.1
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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 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y244
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表达区间
Met1~Leu141
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分子量
20kDa
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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
POMP (Prolyl Oligopeptidase-Targeted Peptide) is a newly identified protein that plays a crucial role in the cellular protein quality control system. Its significance has surged in recent years as research has shown that it is involved in the proper folding and degradation of misfolded proteins, contributing to cellular homeostasis. Abnormalities in protein folding are implicated in various diseases, including neurodegenerative disorders like Alzheimer's and Parkinson's disease. The study of POMP is particularly relevant in understanding these pathologies, as perturbations in its function may lead to the accumulation of toxic protein aggregates. Researchers are investigating the molecular mechanisms by which POMP interacts with other cellular chaperones and proteasomal machinery to enhance the degradation of unwanted proteins. Additionally, the potential therapeutic applications of modulating POMP activity are being explored, which could offer new strategies for treating diseases linked to protein misfolding. Overall, the ongoing research into POMP not only sheds light on fundamental cellular processes but also opens up exciting avenues for therapeutic interventions in protein misfolding diseases.
