Analytical Data
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Gene name
PPIL4
- Application
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Alternative Names
PPIL4;Peptidyl-prolyl cis-trans isomerase-like 4
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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
Q8WUA2
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Expression Region
1-512aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAVLLETTLGDVVIDLYTEERPRACLNFLK LCKIKYYNYCLIHNVQRDFIIQTGDPTGTGRGGESIFGQLYGDQASFFEA EKVPRIKHKKKGTVSMVNNGSDQHGSQFLITTGENLDYLDGVHTVFGEVT EGMDIIKKINETFVDKDFVPYQDIRINHTVILDDPFDDPPDLLIPDRSPE PTREQLDSGRIGADEEIDDFKGRSAEEVEEIKAEKEAKTQAILLEMVGDL PDADIKPPENVLFVCKLNPVTTDEDLEIIFSRFGPIRSCEVIRDWKTGES LCYAFIEFEKEEDCEKAFFKMDNVLIDDRRIHVDFSQSVAKVKWKGKGGK YTKSDFKEYEKEQDKPPNLVLKDKVKPKQDTKYDLILDEQAEDSKSSHSH TSKKHKKKTHHCSEEKEDEDYMPIKNTNQDIYREMGFGHYEEEESCWEKQ KSEKRDRTQNRSRSRSRERDGHYSNSHKSKYQTDLYERERSKKRDRSRSP KKSKDKEKSKYR
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Molecular Weight
59 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
PPIL4, or Peptidylprolyl Isomerase Like 4, belongs to a family of peptidylprolyl isomerases (PPIases), which are critical for protein folding and regulation. These enzymes catalyze the cis-trans isomerization of proline residues in polypeptides, influencing protein structure and function. Emerging studies have highlighted the role of PPIL4 in various biological processes, including cell cycle progression, signal transduction, and immune responses. Its expression has been linked to several diseases, including cancer and neurodegenerative disorders, suggesting that PPIL4 may have potential as a therapeutic target. Research has increasingly focused on the molecular mechanisms underlying PPIL4's activity and its interactions with other proteins, revealing insights into its role in post-translational modifications and cellular homeostasis. Given the complexity of cellular signaling networks, understanding PPIL4's function could provide valuable information for developing novel strategies in disease treatment and gene therapy. The ongoing exploration of PPIL4 as a reconstituted protein aims to elucidate its biochemical properties and therapeutic potential, contributing to the broader field of protein engineering and targeted drug design.
