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PPIC Protein, Human, Recombinant (Trx & His)
Catalog No. TMPJ-00971
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.
PPIC Protein, Human, Recombinant (Trx & His)
Catalog No. TMPJ-00971
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.
| Pack Size | Price | Availability | Quantity |
|---|---|---|---|
| 10 μg | $184 | 7-10 days | |
| 50 μg | $545 | 7-10 days | |
| 500 μg | $1,900 | 7-10 days | |
| 1 mg | $2,730 | 7-10 days |
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| Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
| 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 |
| Expression System | E. coli |
| Tag | N-Trx-6xHis |
| Accession Number | P45877 |
| Synonyms | Rotamase C,PPIC,PPIase C,Peptidyl-Prolyl Cis-Trans Isomerase C,CYPC,Cyclophilin C |
| Amino Acid | Lys31-Asp182 |
| Construction | Lys31-Asp182 |
| Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
| Molecular Weight | 34 KDa (reducing condition) |
| Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
| Formulation | Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 10% Glycerol, pH 7.4. |
| Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
| Shipping | Shipping with blue ice. |
| 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. |
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