Analytical Data
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Gene name
PPIC
- Application
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Alternative Names
PPIC；CYPC；Peptidyl-prolyl cis-trans isomerase C
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P45877
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Expression Region
31-182aa
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AA Sequence
MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEY QGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQL KEFLDANLAGSGSGHMHHHHHHSSGLVPRGSGMKETAAAKFERQHMDSPD LGTDDDDKAMAKRGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVEN FVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPD ENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDG MTVVHSIELQATD
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Molecular Weight
34 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
PPIC, or Peptidylprolyl isomerase C, is an essential enzyme that plays a crucial role in protein folding and chaperone activity in various biological processes. Its function is particularly important in the context of post-translational modifications, where it catalyzes the isomerization of proline residues in polypeptide chains, facilitating proper protein conformation and stability. Recent research highlights the significance of PPIC in cellular stress responses, protein quality control, and disease mechanisms, including cancer and neurodegenerative disorders. The study of recombinant PPIC proteins not only enhances our understanding of their biochemical properties but also provides insights into their potential therapeutic applications. Recombinant protein expression systems have advanced significantly, allowing for the high-yield production and purification of PPIC variants, which can be utilized for structural and functional analyses. By exploring the specific interactions and pathways involving PPIC, researchers aim to elucidate its role in cell biology and disease, paving the way for novel therapeutic strategies targeting protein misfolding and aggregation-related disorders. The ongoing exploration of PPIC's functionality underscores its promise as a pivotal component in the quest for understanding complex biological mechanisms and developing innovative treatments.
