Analytical Data
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Gene name
PPID
- Application
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Alternative Names
PPID; CYPD; CyP-D; PPIase D; Peptidylprolyl Isomerase D; Cyclophilin 40; 40 kDa peptidyl-prolyl cis-trans isomerase; Cyclophilin-related protein; Rotamase D
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Species
Mouse
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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
Q9CR16
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Expression Region
Lys9~Asp189
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Molecular Weight
23kDa
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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
PPID (Peptidyl-prolyl isomerase D) is a type of protein that plays a crucial role in protein folding and isomerization, influencing various cellular processes. Research on PPID is particularly significant due to its involvement in the regulation of stress responses and cellular signaling, as well as its potential link to various diseases, including cancer and neurodegenerative disorders. Recent studies have highlighted the importance of PPID in assisting the proper folding of proteins within the endoplasmic reticulum, thereby contributing to the overall protein quality control within cells. The ability to produce recombinant PPID has opened new avenues for in-depth investigation, enabling researchers to explore its structural properties, enzymatic functions, and interaction with other cellular components. Understanding PPID’s mechanisms may lead to the development of therapeutic strategies targeting diseases where protein misfolding is implicated. As such, ongoing studies focus on the molecular characterization of PPID, its role in cellular homeostasis, and its application in biotechnology, showcasing the relevance of this protein in both basic research and clinical implications.
