Mouse Cyclophilin A / PPIA / CYPA Protein (His Tag)
2700098C05,Cphn,CyP-18,CypA
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Catalog Number | P50296-M08E |
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Organism Species | Mouse |
Host | E. coli |
Synonyms | 2700098C05,Cphn,CyP-18,CypA |
Molecular Weight | The recombinant human mouse PPIA consisting of 170 amino acids and has a calculated molecular mass of 18.8 kDa. It migrates as an approximately 17 kDa band in SDS-PAGE under reducing conditions. |
predicted N | Met |
SDS-PAGE | |
Purity | > 97 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the mouse PPIA (NP_032933.1) (Met 1-Leu 164) was expressed, with a polyhistide tag at the C-terminus. |
Bio-activity | |
Research Area | Microbiology |Pathogenic microorganism |viruses |animal virus |viral illness |Central nervous system diseases | |
Formulation | Lyophilized from sterile PBS, pH 7.4, 10% glycerol 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 | Mouse peptidyl-prolyl cis-trans isomerase A, also known as PPIase A, Rotamase A, Cyclophilin A, Cyclosporin A-binding protein, PPIA and CYPA, is a cytoplasm protein which belongs to the cyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins (CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. PPIA / Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIA / Cyclophilin A is secreted by vascular smooth muscle cells in response to inflammatory stimuli, and could thus contribute to atherosclerosis. It is not essential for mammalian cell viability. PPIA / Cyclophilin A can interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. |
Reference |