| Product Name | ppiA, 1-164aa, Mouse His tag |
|---|---|
| Description | ppiA also known as Peptidyl-prolyl cis-trans isomerase A. This is an enzyme 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 proline's unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Recombinant mouse ppiA, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Peptidyl-prolyl cis-trans isomerase A, 2700098C05 Cphn, CyP-18, CypA |
| Host | E. coli |
| Molecular Weight | 57.1kDa (493aa) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 10% glycerol |
| Concentration | 0.5mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Haendler B., et al. (1987) EMBO J. 6:947-950 |
| Background | ppiA also known as Peptidyl-prolyl cis-trans isomerase A. This is an enzyme 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 proline's unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Recombinant mouse ppiA, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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