Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.
Cyclophilin-D, a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, plays a crucial role in protein folding. PPIases, including Cyclophilin-D, catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides, accelerating the protein folding process. Notably, Cyclophilin-D exhibits PPIase activity and binds to the immunosuppressant cyclosporin-A. Its overexpression is known to suppress apoptosis in cancer cells. This suppression of apoptotic cell death is achieved through a mitochondrial hexokinase-2 dependent mechanism in cancer cells.
The antibody is supplied at a concentration of 1mg/ml in a buffer solution consisting of PBS at pH 7.4, 10% Glycerol, and 0.02% Sodium Azide.
The PPID antibody has undergone rigorous testing using ELISA and Western blot analysis to confirm its specificity and reactivity. However, due to variations in applications, it is essential to titrate the reagent for each specific experiment to achieve optimal results.
Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, CYP-40, Cyclophilin-related protein, CYP40, CYPD, PPID, Peptidylprolyl Isomerase D.
PPID antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT1B8AT.
Anti-human PPID mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PPID amino acids 1-370 purified from E. coli.
Mouse IgG2b heavy chain and κ light chain.
Peptidylprolyl isomerase D (PPID), also known as cyclophilin D, is an enzyme encoded by the PPID gene in humans. It belongs to the peptidyl-prolyl cis-trans isomerase (PPIase) family, which catalyzes the cis-trans isomerization of proline imidic peptide bonds. This activity facilitates the folding or repair of proteins .
PPID forms a β-barrel structure with a hydrophobic core, composed of eight anti-parallel β-strands capped by two α-helices at the top and bottom. The β-turns and loops in the strands contribute to the flexibility of the barrel . PPID is involved in various biological processes, including mitochondrial metabolism, apoptosis, redox regulation, and inflammation .
PPID participates in several critical biological processes:
Mouse anti-human PPID antibodies are used in research to study the expression and function of PPID in human cells. These antibodies are crucial for investigating the role of PPID in different biological processes and diseases.