Technical Data
C8850-03A
Cyclophilin A (Cyclosporin A Binding Protein, Peptidyl Prolyl Cis Trans Isomerase A, PPIASE)
Description:
Cyclophilins are a highly conserved family of peptidylprolyl cis-trans-isomerases (PPIA) that are targets of the immunosuppressant drug cyclosporin A (CsA). The complex of cyclophilin and CsA can bind to and inhibit calcineurin which leads to inhibition of the transcription factor NFAT and decreased production of cytokines. As isomerases, cyclophilins have been proposed to aid in protein folding. Cyclophilin A can bind to the p55 Gag protein of HIV and appears necessary for HIV infection. There is also some evidence that cyclophilins can have nuclease activity and play a role in apoptosis.

Applications:
Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabAffinity Purified
SizeStorageShippingSourceHost
100ul-20CBlue IceRabbit
Concentration:
Not Determined
Immunogen:
Synthetic peptide corresponding to residues near the carboxy terminus of Cyclophilin A.
Purity:
Purified by Protein A and peptide affinity chromatography.
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Specificity:
Recognizes endogenous levels of total Cyclophilin A at ~18kD. Species Crossreactivity: human, mouse, rat and monkey. Species Sequence Homology: bovine and canine
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Takahashi, N. et al. (1989) Nature 337, 473475. 2. Wang, P. and Heitman, J. (2005) Genome Biol. 6, 226. 3. Jain, J. et al. (1993) Nature 365, 352355. 4. McCaffrey, P.G. et al. (1993) J. Biol. Chem. 268, 37473752. 5. Thali, M. et al. (1994) Nature 372, 363365. 6. Streblow, D.N. et al. (1998) Virology 245, 197202. 7. Montague, J.W. et al. (1994) J. Biol. Chem. 269, 1887718880.