Analytical Data
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Gene name
PPIAL4G
- Application
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Alternative Names
PPIAL4G
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A2BFH1
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Expression Region
1-164 aa
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AA Sequence
MVNSVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGEKGFRYKGSCFHRIIPGFMCQGGDFTRPNGTGDKSIYGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITIADCGQF
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Molecular Weight
18.1 kDa
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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
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Protein Description
PPIAL4G (Peptidylprolyl Isomerase A-Like 4G) is a member of the peptidylprolyl isomerase (PPIase) family, which plays a vital role in protein folding and post-translational modification. This protein is characterized by its ability to catalyze the isomerization of proline residues in peptide bonds, influencing protein conformation and stability. Research has indicated that PPIAL4G may be involved in various cellular processes, including signal transduction, cell proliferation, and apoptosis. Studies have also suggested potential links between PPIAL4G expression levels and several diseases, including cancers, where altered protein folding may contribute to tumorigenesis. The interest in PPIAL4G is further heightened by its implications in neurodegenerative disorders, as proper protein folding is crucial for neuronal function. By studying PPIAL4G's structure and function, researchers aim to elucidate its role within the cellular environment and its potential as a therapeutic target. Understanding the mechanisms by which PPIAL4G operates and its involvement in disease pathways could pave the way for novel interventions in conditions where protein misfolding is a critical factor. The study of recombinant PPIAL4G proteins can provide insights into their enzymatic properties and interactions with other molecules, enhancing our comprehension of their biological significance and potential roles in health and disease management.
