No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human PPIF Antibodies:
anti-Rat (Rattus) PPIF Antibodies:
anti-Mouse (Murine) PPIF Antibodies:
Go to our pre-filtered search.
Human Monoclonal PPIF Primary Antibody for ELISA, WB - ABIN534876
Bergsma, Eder, Gross, Kersten, Sylvester, Appelbaum, Cusimano, Livi, McLaughlin, Kasyan: The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms. in The Journal of biological chemistry 1992
Show all 2 Pubmed References
Human Polyclonal PPIF Primary Antibody for IF, IHC - ABIN5664246
Wang, Lin, Chen, Zhu, Jiang, Li, Wang et al.: Overexpression of mitochondrial Hsp75 protects neural stem cells against microglia-derived soluble factor-induced neurotoxicity by regulating mitochondrial permeability transition pore opening in ... in International journal of molecular medicine 2016
Human Polyclonal PPIF Primary Antibody for ICC, IF - ABIN4301695
Mulay, Honarpisheh, Foresto-Neto, Shi, Desai, Zhao, Marschner, Popper, Buhl, Boor, Linkermann, Liapis, Bilyy, Herrmann, Romagnani, Belevich, Jokitalo, Becker, Anders: Mitochondria Permeability Transition versus Necroptosis in Oxalate-Induced AKI. in Journal of the American Society of Nephrology : JASN 2019
the important yet enigmatic nature of CyPD (PPIF) somehow makes it a master regulator, yet a troublemaker, for mitochondrial function.
Data show that show that the molecular chaperone heat shock protein 60 (Hsp60) directly associates with cyclophilin D (CypD).
adult viable human brain and liver mitochondria possess an active CypD-sensitive mitochondrial permeability transition
Human coronavirus-induced neuronal programmed cell death required cyclophilin d but not caspase 3 caspase 9 activities.
CypD directs mitochondria-to-nuclei inflammatory gene expression in normal and tumor cells
These results suggest Cyp-D's critical role in UVB/oxidative stress-induced skin cell death.
cisplatin-induced non-apoptotic death requires mitochondria Cyp-D-p53 signaling in pancreatic cancer cells
The p53/Cyp-D mitochondrial complexation was prevented by CsA or Cyp-D silencing.
In summary, the results of the present study provide mechanistic evidence that both apoptosis and programmed necrosis attribute to berberine's cytotoxicity in prostate cancer cells.
molecular determinants necessary for Cyclophilin D activity regulation and binding to proposed pore constituents thereby regulating the mitochondrial permeability transition pore.
Cyp-D silencing down-regulated mitochondrial transcripts initiated from the heavy strand promoter 2 [i.e., NADH dehydrogenase 1 (ND1) by 11-fold; cytochrome oxidase 1 (COX1) by 4-fold; and ATP synthase subunit 6 (ATP6) by 6.5-fold.
Results show that CypD interacts with SPG7 and VDAC to form the mitochondrial permeability transition pore complex (PTP)and its CsA-binding region is necessary for PTP formation.
The influx of unfolded p53 into the mitochondrial matrix in response to oxidative stress indirectly activates the normally inhibited CypD by displacing it from Trap1 complexes. This activates CypD's isomerase activity. Liberated CypD then isomerizes multiple proteins including p53 (causing p53 aggregation) and the structural components of the mPTP pore, inducing pore opening.
cyclophilin D may modify mitochondrial features by inducing the translocation of molecules to the mitochondria through the mechanism associated with cellular energy metabolism
CyPD regulates mitochondrial metabolism, and likely cell survival, by promoting more efficient electrons flow through the respiratory chain via increased supercomplex formation
The present study is to investigate the role of CypD in regulating the mitochondrial dynamics relevant to oxidative stress induced neuron dysfunctions.
Binding of signal transducer and activator of transcription 3 (STAT3) to cyclophilin D (CypD) was important for reducing mitochondrial reactive oxygen species (ROS) production after oxidative stress.
This review discusses previous studies to provide comprehensive information on the physiological role of cyclophilin D as well as PTP opening in the cell that can be taken into consideration for the development of new PTP inhibitors. [review]
Crystal structure of human cyclophilin D in complex with its inhibitor, cyclosporin A at 0.96-A resolution, using a K133I mutant of human CypD
Cyclophilin D may play a role as a redox sensor in mitochondria of mammalian cells transmitting information on the redox environment to target proteins.
LKT-mediated cell death involve dynamin-2 and cyclophilin D.
Mannheimia haemolytica leukotoxin binds cyclophilin D on bovine neutrophil mitochondria.
mitochondrial CypD is involved in the regulation of inflammation in aorta.
Stimulation of oxidative phosphorylation (OXPHOS), inhibition of the mitochondrial permeability transition pore (PTP), or deletion of CypD increased high order synthasome assembly. OXPHOS inhibition or PTP opening increased synthasome disassembly in wild type, but not in CypD knockout heart mitochondria. CypD activity also correlated with synthasome assembly in other tissues, such as liver and brain.
This study has revealed the physiological function of CypD in dendritic plasticity by acting as a fine-tuner of mitochondrial calcium homeostasis.
deletion of CypD is associated with an increased mtHK activity.
This study identified a role for CypD in chronic tubular cell damage and in the development of renal interstitial fibrosis.
Loss of mitochondrial CypD (Ppif) results in a shift in bioenergetics and in activation of Akt/AMPK/p70S6 kinase pathways.
the permeability transition pore can form and open in the absence of CyP-D, which is the target for PTP inhibition by Cyclosporin A
implicate pathological activation of the mitochondrial permeability transition pore in the axonal damage occurring during multiple sclerosis and identify CyPD, as well as the permeability transition pore
Cyclophilin D-dependent (CyD) mitochondrial permeability transition (CyD-mPT) plays an important role in glutamate-triggered delayed calcium deregulation (DCD) and excitotoxic neuronal death.
suggest a novel CypD-dependent negative-feedback mechanism regulating arterial thrombosis
In the absence of Cyp-D, Col6a1(-/-) mice show negligible myofiber degeneration, rescue from mitochondrial dysfunction, and normalized incidence of apoptosis.
CyPD association to the lateral stalk of ATP synthase modulates the activity of the complex
these data suggest that CypD-dependent mitochondrial permeability transition does not play a major role in neurodegeneration in mnd2 mice.
Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury.
These findings point to a possible role of immunophilin signal transduction pathways in astrocytic modulation of neuronal activity at the tripartite synapse.
Complex contribution of cyclophilin D to Ca2+-induced permeability transition in brain mitochondria, with relation to the bioenergetic state.
At the whole muscle level, lack of cyclophilin-D does not protect against muscle atrophy, release of mitochondrial pro-apoptotic factors and activation of caspases following denervation.
mitochondrial permeability transition was increased by hypoxia-reoxygenation but was less in normoxic and hypoxia-reoxygenation Ppif(-/-) than wild type tubules
BAX/BAK-independent cell death did not require Cyclophilin D (CypD) expression, an important regulator of the mitochondrial permeability transition pore
Loss of CypD results in changes in a number of mitochondrial proteins and metabolic pathways.
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