Analytical Data
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Gene name
PPIL6
- Application
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Alternative Names
PPIL6; Probable inactive peptidyl-prolyl cis-trans isomerase-like 6; PPIase; Cyclophilin-like protein PPIL6; Rotamase PPIL6
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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
Q8IXY8
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Expression Region
1-311 aa
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AA Sequence
MARPQPCGPP HARCGSPSLP ERPLQVKVVG LFSCPNFQIA KSAAENLKNN HPSKFEDPIL VPLQEFAWHQ YLQEKKRELK NETWEYSSSV ISFVNGQFLG DALDLQKWAH EVWDIVDIKP SALYDALTED FSAKFLRDTK HDFVFLDICI DSSPIGRLIF ELYCDVCPKT CKNFQVLCTG KAGFSQRGIR LHYKNSIFHR IVQNGWIQGG DIVYGKGDNG ESIYGPTFED ENFSVPHNKR GVLGMANKGR HSNGSQFYIT LQATPYLDRK FVAFGQLIEG TEVLKQLELV PTQNERPIHM CRITDSGDPY A
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Molecular Weight
35.2 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
Related Products
Protein Description
PPIL6, or Peptidylprolyl Isomerase Like 6, is a member of the cyclophilin family of proteins that play crucial roles in various biological processes, including protein folding, cell signaling, and immune response modulation. Its involvement in these critical cellular functions has attracted significant research interest, particularly due to its potential implications in diseases such as cancer and autoimmune disorders. Recent studies have suggested that PPIL6 may serve as a regulatory factor in the T-cell response and in the progression of certain cancers, highlighting its promise as a therapeutic target. Additionally, PPIL6's enzymatic activity in catalyzing the cis-trans isomerization of proline residues may influence protein structure and function, further underscoring its importance in cellular biology. The recombinant production of PPIL6 protein has been a focus of recent investigations, facilitating in-depth studies of its biochemical properties, interactions, and therapeutic potential. These advances have paved the way for exploring PPIL6 as a viable candidate for drug development and other biotechnological applications, making it a significant subject in the fields of molecular biology and pharmacology.
