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Dog (Canine) Polyclonal PPID Primary Antibody for ELISA, WB - ABIN547953
Forte, Gold, Marracci, Chaudhary, Basso, Johnsen, Yu, Fowlkes, Rahder, Stem, Bernardi, Bourdette: Cyclophilin D inactivation protects axons in experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis. in Proceedings of the National Academy of Sciences of the United States of America 2007
Human Polyclonal PPID Primary Antibody for ICC, IHC - ABIN1858597
Ojha, Nandi, Batra, Singhal, Annarapu, Bhattacharyya, Seth, Dar, Medigeshi, Vrati, Vikram, Guchhait: Platelet activation determines the severity of thrombocytopenia in dengue infection. in Scientific reports 2017
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.
Data show that cyclophilin 40 (CyP40) interacts with and dissolves amyloids forming proteins tau and alpha-synuclein aggregates.
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]
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.
The present study is to investigate the role of CypD in regulating the mitochondrial dynamics relevant to oxidative stress induced neuron dysfunctions.
CyPD regulates mitochondrial metabolism, and likely cell survival, by promoting more efficient electrons flow through the respiratory chain via increased supercomplex formation
cyclophilin D may modify mitochondrial features by inducing the translocation of molecules to the mitochondria through the mechanism associated with cellular energy metabolism
The thermodynamics of binding of Cyp-40 to Hsp90 shows remarkable temperature sensitivity in the physiological temperature range.
cyclophilin-D protein could increase oxidative stress and cause endothelial cell injury and apoptosis. cyclophilin-D protein is the key factor in reactive oxygen species-induced mitochondrial damage, leading to apoptosis of endothelial cells.
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.
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.
Cyp40 binds to C2I in vitro and in intact cells, it also interacts with the enzyme components of iota toxin and CDT, suggesting a common principle for this toxin family.
The Photorhabdus toxins TccC3 and TccC5 interacted with Hsp90, FKBP51, Cyp40 and CypA, suggesting a role of these host cell factors in translocation and/or refolding of the ADP-ribosyltransferases.
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.
cisplatin-induced non-apoptotic death requires mitochondria Cyp-D-p53 signaling in pancreatic cancer cells
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.
this is the first report establishing an important role for Cyp40 in lymphoma.
LKT-mediated cell death involve dynamin-2 and cyclophilin D.
stimulates mitochondrial permeability transition pore excessive opening, causing endoplasmic reticulum stress through p38 mitogen-activated protein kinase activation, resulting in enhanced sterol regulatory element-binding protein-1c transcription and hepatic steatosis
Data suggest that mitochondrial functions in osteoblasts during osteogenesis are regulated, in part, by CypD-mPTP axis; CypD appears to contribute to mitochondrial dysfunction in bone inflammation via excessive opening of mPTP. (CypD = cyclophilin D; mPTP = mitochondrial permeability transition pore)
Estrogen receptor beta modulates mitochondrial permeability transition by regulating CypD interaction with OSCP.
CypD regulates complex I-induced ROS production in heart mitochondria and modulates the cardioprotective effect of isoflurane, sevoflurane, and desflurane.
Murine eosinophil necrosis is regulated in vitro and in vivo by cyclophilin D.
Suggest that cyclosporin A-mediated CypD inhibition may provide a promising therapeutic potential for protecting retinal ganglion cells against ischemic injury-mediated mitochondrial dysfunction.
Loss of CypD results in changes in a number of mitochondrial proteins and metabolic pathways.
BAX/BAK-independent cell death did not require Cyclophilin D (CypD) expression, an important regulator of the mitochondrial permeability transition pore
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
These findings point to a possible role of immunophilin signal transduction pathways in astrocytic modulation of neuronal activity at the tripartite synapse.
Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury.
Complex contribution of cyclophilin D to Ca2+-induced permeability transition in brain mitochondria, with relation to the bioenergetic state.
these data suggest that CypD-dependent mitochondrial permeability transition does not play a major role in neurodegeneration in mnd2 mice.
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
suggest a novel CypD-dependent negative-feedback mechanism regulating arterial thrombosis
Cyclophilin D-dependent (CyD) mitochondrial permeability transition (CyD-mPT) plays an important role in glutamate-triggered delayed calcium deregulation (DCD) and excitotoxic neuronal death.
In the absence of Cyp-D, Col6a1(-/-) mice show negligible myofiber degeneration, rescue from mitochondrial dysfunction, and normalized incidence of apoptosis.
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 has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant cyclosporin A.
peptidylprolyl isomerase D
, peptidylprolyl isomerase D (cyclophilin D)
, 40 kDa peptidyl-prolyl cis-trans isomerase D
, PPIase D
, cyclophilin 40
, cyclophilin D
, cyclophilin-related protein
, peptidyl-prolyl cis-trans isomerase D
, rotamase D
, 40 kDa peptidyl-prolyl cis-trans isomerase
, Cyclophilin D
, estrogen receptor-binding cyclophilin
, cytoplasmic cyclophilin D