Human Cyclophilin A / PPIA / CYPA Protein (His Tag)
CYPA,CYPH,HEL-S-69p
- 100ug (NPP3787) Please inquiry
Catalog Number | P10436-H08E |
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Organism Species | Human |
Host | E. coli |
Synonyms | CYPA,CYPH,HEL-S-69p |
Molecular Weight | The recombinant human PPIA consisting of 175 amino acids and has a calculated molecular mass of 19.4 kDa as estimated in SDS-PAGE under reducing conditions. |
predicted N | Met 1 |
SDS-PAGE | |
Purity | > 97 % as determined by SDS-PAGE |
Protein Construction | A DNA sequence encoding the human PPIA (P62937) (Met 1-Glu 165) 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 50mM Tris, 150mM NaCl, 20% glycerol, pH 7.7 1. Normally 5 % - 8 % trehalose and mannitol 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 |