Name :
PPIC Protein
Description :
Cyclophilin C is an enzyme (EC 5.2.1.8) found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but prolines unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.
Species :
Human
Uniprotkb :
E. coli
Tag :
N-Trx-6His
Synonyms :
PPIase C, Peptidyl-Prolyl Cis-Trans Isomerase C, PPIC, Cyclophilin C, CYPC, Rotamase C
Construction :
Recombinant Human Peptidyl-Prolyl Cis-trans Isomerase C is produced by our E.coli expression system and the target gene encoding Lys31-Asp182 is expressed with a Trx, 6His tag at the N-terminus.
Protein Purity :
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight :
34 KDa, reducing conditions
Endotoxin :
Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulatione :
Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 10% Glycerol, pH 7.4.
Reconstitution :
Stability & Storage :
Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping :
The product is shipped on dry ice/polar packs.Upon receipt, store it immediately at the temperature listed below.
Research Background :
Cyclophilin C is an enzyme (EC 5.2.1.8) found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but prolines unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.
References and Literature :
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
CALD1 Antibody Protocol Adenosylhomocysteinase medchemexpress PMID:35238915 MedChemExpress (MCE) offers a wide range of high-quality research chemicals and biochemicals (novel life-science reagents, reference compounds and natural compounds) for scientific use. We have professionally experienced and friendly staff to meet your needs. We are a competent and trustworthy partner for your research and scientific projects.Related websites: https://www.medchemexpress.com