PPIase is a member of the immunophilin protein family. It also belongs to the cyclophilin-type PPIase family; PPIL3 subfamily. PPIase contains 1 PPIase cyclophilin-type domain. Members of the immunophilin protein family play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. It has a very high substrate specificity for the four-residue peptide Ala-Ala-Pro-Phe only when the proline peptide bond is in the trans state. It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels; and coordinates multi-protein complex formation of the tetrameric skeletal muscle ryanodine receptor. In mouse; deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium.
<1.0 EU per µg of the protein as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the human FKBP7 (Q9Y680-2) (Met1-Gln218) was expressed with a polyhistidine tag at the C-terminus.
Purity:
(84.2+12.5) % as determined by reducing SDS-PAGE.
Mol Mass:
23.8 kDa
AP Mol Mass:
27-30 kDa
Formulation:
Lyophilized from sterile PBS; pH 7.4
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
