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Human Cyclophilin C Recombinant Protein N-Trx, 6 His Tag

Human Cyclophilin C Recombinant Protein N-Trx, 6 His Tag

SKU:IHUCYPNCRNTRX6HIS50UG

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Key facts

    Human Cyclophilin C Recombinant Protein N-Trx, 6 His Tag from Innovative Research has been recombinantly produced in E. coli. This is a Liquid protein buffered in Supplied as a 0.2 um filtered solution of 20mM PB, 150mM NaCl, 10% Glycerol, pH 7.4. It is not recommended to reconstitute to a concentration less than 100UG/ml. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Human Target: PPIC Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: E. coli Storage Conditions: Store at -20░C, stable for 6 months after receipt.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.



    Additional Information:

    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.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

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Human Cyclophilin C Recombinant Protein N-Trx, 6 His Tag from Innovative Research has been recombinantly produced in E. coli. This is a Liquid protein buffered in Supplied as a 0.2 um filtered solution of 20mM PB, 150mM NaCl, 10% Glycerol, pH 7.4. It is not recommended to reconstitute to a concentration less than 100UG/ml. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Human Target: PPIC Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: E. coli Storage Conditions: Store at -20░C, stable for 6 months after receipt.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.



Additional Information:

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.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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