Human PPIL1 Protein (His Tag)
CGI-124,CYPL1,hCyPX,PPIase
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| Catalog Number | P14163-H08E |
|---|---|
| Organism Species | Human |
| Host | E. coli |
| Synonyms | CGI-124,CYPL1,hCyPX,PPIase |
| Molecular Weight | The recombinant human PPIL1 consists of 172 amino acids and predicts a molecular mass of 19.1 KDa. It migrates as an approximately 17 - 20 KDa band in SDS-PAGE under reducing conditions. |
| predicted N | Met |
| SDS-PAGE |  |
| Purity | > 90 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the human PPIL1 (Q9Y3C6) (Met1-Gly166) was expressed with a polyhistidine tag at the C-terminus. |
| Bio-activity | |
| Research Area | Epigenetics |DNA / RNA |RNA Processing |RNA splicing |
| Formulation | Lyophilized from sterile 50mM Tris, 10% glycerol, pH 8.0 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | PPIL1 is a member of the cyclophilin family. Cyclophilins are well conserved and ubiquitous. Members of cyclophilin family take an significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 is a peptidylprolyl isomerase(PPIase). It increases the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is a novel molecular target for colon-cancer therapy. |
| Reference |