Product nameRecombinant human PPIL1 protein
See all PPIL1 proteins and peptides
Protein lengthFull length protein
Amino Acid Sequence
SequenceMAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNG TKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAM ANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQ DRPVDDVKIIKAYPSGLEHHHHHH
Our Abpromise guarantee covers the use of ab79247 in the following tested applications.
Biological activitySpecific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 µmole of suc-AAFP-pNA per minute at 25°C in Tris-Hcl pH8.0 using chymotrypsin.
- Prepare 170 µl assay buffer into a suitable container and pre-chill on ice before use: The final concentrations are 200 mM Tris-Hcl, pH 8.0, and 20nM chymotrypsin.
- Add 10 µl of recombinant PPIL1 protein with 1 µg in assay buffer.
- Mix by inversion and equilibrate to 1deg;C and monitor the A405nm until the value is constant using a spectrophotometer.
- Add 20 µl pre-chilled 5mM suc-AAFP-pNA. (Substrate was dissolved in TFE that contained 460mM LiCl to a concentration of 3 mM)
- Record the increase in A405 nm for 30 minutes at 25°C.
Purity> 95 % SDS-PAGE.
ab79247 is purified using conventional chromatography techniques.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Constituents: 0.316% Tris HCl, 20% Glycerol
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- CGI 124
FunctionPPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.
Tissue specificityUbiquitous, with the most abundant expression in heart and skeletal muscle.
Sequence similaritiesBelongs to the cyclophilin-type PPIase family. PPIL1 subfamily.
Contains 1 PPIase cyclophilin-type domain.
- Information by UniProt
ab79247 has not yet been referenced specifically in any publications.