Analytical Data
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Gene name
POMP
- Application
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Alternative Names
PNAS-110; UMP1; Proteassemblin; Protein UMP1 homolog; Voltage-gated K channel beta subunit 4.1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y244
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Expression Region
Met1~Leu141
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Molecular Weight
20kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
