Product Description
Size: 100µg
Recombinant human PPIL1 protein is a Human Full Length protein, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB, FuncS.
Key facts
Purity:>95% SDS-PAGE,
Expression system:Escherichia coli,
Tags:Tag free,
Applications:SDS-PAGE, WB, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific activity is > 700 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 nmole of suc-AAPF-pNA per minute at 37°C in Tris-Hcl pH8.0 using chymotrypsin.,
Accession:Q9Y3C6,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 20% Glycerol (glycerin, glycerine), 0.316% Tris HCl
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
PPIL1 known as Peptidylprolyl Isomerase Like 1 is an enzyme that functions as a peptidyl-prolyl cis-trans isomerase. It facilitates protein folding by catalyzing the isomerization of proline residues in polypeptide chains. PPIL1 carries a mass of approximately 18 kDa. This protein is expressed in various tissues including the brain and immune system indicating its role in diverse cellular processes.
Biological function summary
PPIL1 contributes significantly to cellular activities by facilitating protein conformational modifications. It often operates as part of larger complexes interacting with other proteins to maintain cellular homeostasis. PPIL1 plays a vital role in response to different cellular stress conditions and its activity affects basic cellular functions especially those involving protein assembly and signaling.
Pathways
PPIL1 interacts with several critical signaling pathways influencing protein folding and cellular stress responses. It is notably involved in the protein processing pathway where it modulates the action of related proteins like Cyclophilin A (CYPA). These interactions are essential for maintaining protein homeostasis affecting processes such as cell cycle progression and apoptosis.
Abnormalities in PPIL1 expression or function have been linked to various pathological conditions such as cancer and neurodegenerative diseases. In these diseases PPIL1 may affect tumor growth or neuronal survival by interacting with proteins like p53 which is important in cancer cell apoptosis regulation. These interactions highlight PPIL1's potential as a therapeutic target for drug development and disease treatment strategies.
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Collaboration
Tony Tang
Email: Tony.Tang@iright.com
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