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The protein encoded by PPIF is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. Additionally we are shipping PPIF Proteins (21) and PPIF Kits (3) and many more products for this protein.
Showing 10 out of 100 products:
Human Polyclonal PPIF Primary Antibody for EIA, WB - ABIN951771
Lin, Lechleiter: Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. in The Journal of biological chemistry 2002
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Chicken Polyclonal PPIF Primary Antibody for WB - ABIN2782510
Clark, Edwards, Peterson, Clifton, Thompson, Sasaki, Suzuki, Kikuchi, Watabe, Kawakami, Sugano, Elgar, Johnson: Fugu ESTs: new resources for transcription analysis and genome annotation. in Genome research 2003
Show all 2 references for ABIN2782510
Human Monoclonal PPIF Primary Antibody for EIA, IHC (p) - ABIN356236
Bowles, Abraham, Brugada, Zintz, Comeaux, Sorajja, Tsubata, Li, Brandon, Gibbs, Scherer, Bowles, Towbin: Construction of a high-resolution physical map of the chromosome 10q22-q23 dilated cardiomyopathy locus and analysis of candidate genes. in Genomics 2000
Show all 2 references for ABIN356236
Human Polyclonal PPIF Primary Antibody for IHC, ELISA - ABIN1533690
Deloukas, Earthrowl, Grafham, Rubenfield, French, Steward, Sims, Jones, Searle, Scott, Howe, Hunt, Andrews, Gilbert, Swarbreck, Ashurst, Taylor, Battles, Bird, Ainscough, Almeida, Ashwell, Ambrose et al.: The DNA sequence and comparative analysis of human chromosome 10. ... in Nature 2004
Cyclophilin D protects cell from cell death.
There was increased [Ca(2 (show CA2 Antibodies)+)](c), [Ca(2 (show CA2 Antibodies)+)](m), mCICR, MPTP (show PTPN2 Antibodies) opening, and expression of cyclophilin D and decreased DeltaPsim in POAG TM cells compared with control cells.
Mannheimia haemolytica leukotoxin binds cyclophilin D on bovine neutrophil mitochondria.
Ischemic postconditioning might prevent lethal reperfusion injury through an increased SIRT3 (show SIRT3 Antibodies) activity and subsequent attenuation of CyPD (show CYPD Antibodies) acetylation at reperfusion.
These findings reveal the role of HAX-1 (show HAX1 Antibodies) in regulating cyclophilin-D levels via an Hsp90 (show HSP90 Antibodies)-dependent mechanism, resulting in protection against activation of mPTP (show PTPN2 Antibodies) and subsequent cell death responses
study identifies a novel signaling pathway composed of E2F1 (show E2F1 Antibodies), miR (show MLXIP Antibodies)-30b and CypD (show CYPD Antibodies) that regulates myocardial necrosis.
It is concluded that CypD (show CYPD Antibodies) sensitizes the brain mitochondria to PT, and its inhibition by CsA (show HSPA9 Antibodies) or CypD (show CYPD Antibodies) absence improves the complex I-related mitochondrial function and increases mitochondria stability against Ca(2 (show CA2 Antibodies)+) stress.
Data indicate that Ppif (show PPID Antibodies) protein cyclophilin D (CypD (show CYPD Antibodies))-dependent protein kinase A (PKA)/cAMP regulatory-element-binding (CREB (show CREB1 Antibodies)) signaling is responsible for amyloid beta (Abeta (show APP Antibodies))-induced synaptic injury.
Ablation of CypD (show CYPD Antibodies) leads to changes in the mitochondrial acetylome which may contribute to altered mitochondrial metabolism in CypD (show CYPD Antibodies)-deficient mice.
These results suggest a physiologic function for CypD (show CYPD Antibodies) and the mitochondrial permeability transition in the regulation of starvation-induced autophagy.
new insights into CypD (show CYPD Antibodies)-dependent mitochondrial mPTP (show PTPN2 Antibodies) and signaling on mitochondrial trafficking in axons and synaptic degeneration in an environment enriched for Abeta (show APP Antibodies)
Cys (show DNAJC5 Antibodies)-203 residue of CypD (show CYPD Antibodies) is necessary for redox stress-induced activation of mPTP (show PTPN2 Antibodies).
Data suggest that, in mitochondria exhibiting intact inner membranes, the absence of cyclophilin D or the inhibition of its binding to F(0)F(1)-ATP synthase by cyclosporin A will affect only matrix adenine nucleotides levels.
The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
peptidyl-prolyl cis-trans isomerase A
, peptidylprolyl isomerase F (cyclophilin F)
, peptidyl-prolyl cis-trans isomerase F, mitochondrial
, cyclophilin D
, cyclophilin F
, ppiase F
, rotamase F
, peptidylprolyl isomerase F
, PPIase F
, cyclophilin 3
, mitochondrial cyclophilin
, peptidyl-prolyl cis-trans isomerase, mitochondrial
, mitochondrial Cyclophilin D