PPID _ CyP_40
- Known as:
- PPID _ CyP_40
- Catalog number:
- Y213700
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- PPID _ CyP_40
Related genes to: PPID _ CyP_40
- Gene:
- PPID NIH gene
- Name:
- peptidylprolyl isomerase D
- Previous symbol:
- -
- Synonyms:
- CYP-40
- Chromosome:
- 4q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-08-23
- Date modifiied:
- 2016-10-05
Related products to: PPID _ CyP_40
1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial,24-OHase,Cyp24,Cyp-24,Cyp24a1,Cytochrome P450 24A1,Cytochrome P450-CC24,Mouse,Mus musculus,Vitamin D(3) 24-hydroxylase40 kDa peptidyl-prolyl cis-trans isomerase,Bos taurus,Bovine,Cyclophilin-40,Cyclophilin-related protein,CYP-40,CYPD,Estrogen receptor-binding cyclophilin,Peptidyl-prolyl cis-trans isomerase D,PPIase D40 kDa peptidyl-prolyl cis-trans isomerase,Cyclophilin-40,Cyclophilin-related protein,CYP40,CYP-40,CYPD,Homo sapiens,Human,Peptidyl-prolyl cis-trans isomerase D,PPIase D,PPID,Rotamase D40 kDa peptidyl-prolyl cis-trans isomerase,Cyclophilin-40,CYP-40,Mouse,Mus musculus,Peptidyl-prolyl cis-trans isomerase D,PPIase D,Ppid,Rotamase D40 kDa peptidyl-prolyl cis-trans isomerase,Cyclophilin-40,CYP-40,Peptidyl-prolyl cis-trans isomerase D,PPIase D,Ppid,Rat,Rattus norvegicus,Rotamase DAnti- PPID CyP-40 Antibodyanti-Cyclophilin D，PPIDanti-PPID (4C7)Anti-PPID Antibodyanti-PPID(4C7)Anti-recombinant CYP-33E1 Monoclonal AntibodyAntibodies: PPID _ CyP-40 HOST: Goat Clonality: pAbAntigens Cyclophilin D(PPID), 1- 370aa, Human, His-tagged, Recombinant, E.coliBovine Peptidyl-prolyl cis-trans isomerase D(PPID) ELISA kitBovine Peptidyl-prolyl cis-trans isomerase D(PPID) ELISA kit SpeciesBovine Related articles to: PPID _ CyP_40
- Limited published data exist regarding the diagnostic utility of beta-endorphin (β-END) for pituitary pars intermedia dysfunction (PPID), either compared with or in combination with adrenocorticotropic hormone (ACTH). - Source: PubMed
Billmann PaulaDurham Andy EChristen GaranceGerber VinzenzGross JosefFouché Nathalie - Variables associated with hormonal, clinical, and survival outcomes of equids with pituitary pars intermedia dysfunction (PPID) are incompletely investigated. - Source: PubMed
Stapley EmmaLowndes CaitrinInanc EceGillespie-Harmon CarolineWaxman SarahFarr Amandavan Eps AndrewBertin François-René - Pituitary pars intermedia dysfunction (PPID) is a prevalent endocrine disease in older horses sharing pathogenetic features with Parkinson disease, including dopaminergic neurodegeneration and α-synuclein aggregation. This study was conducted to determine whether horses with PPID exhibit changes in short-chain fatty acid (SCFA) profiles as described in Parkinson disease, providing further evidence for involvement of a microbiota-gut-brain axis in the pathogenesis of PPID. - Source: PubMed
Publication date: 2026/08/18
Wang WenqingNitert Marloes DekkerGobius SaharaGonzalez-Astudillo VivianaBertin François-René - Kawasaki disease (KD) is a systemic vasculitis of childhood driven by aberrant immune activation. Natural killer (NK) cell dysregulation plays a critical role, but its upstream molecular mechanisms remain unclear. Isonicotinylation (Kinic), a novel lysine acylation acting as a metabolic sensor, represents an unexplored regulatory layer in KD. - Source: PubMed
Publication date: 2026/07/22
Yang YanliHu Pengjuan - Protein translocation across the bacterial SecYEG channel involves mechanical constraints arising from ATP-driven SecA activity, geometric confinement within the translocon, and folding of the emerging polypeptide on the periplasmic side. Periplasmic chaperones assist substrate maturation during this process, but how they influence protein folding under force remains poorly understood. Using protein L as a model two-state substrate, we applied physiologically relevant force pulses using custom-built single-molecule magnetic tweezers to examine how bacterial periplasmic chaperones modulate folding under tension. To isolate the direct effects of individual chaperones, these experiments were performed in the absence of SecA and the SecYEG translocon. We show that the periplasmic chaperones PpiD and DsbC increase folding probability and accelerate refolding under force, while having minimal effect on unfolding kinetics. In contrast, Spy and Skp reduce folding probability and suppress refolding, consistent with holdase-like behaviour. These observations show that distinct classes of periplasmic chaperones differentially modulate folding probability and refolding kinetics under mechanical force. Increased folding probability correspondingly enhances the expected mechanical work output of substrate folding under force. Together, our findings establish a quantitative framework for investigating how bacterial periplasmic chaperones modulate protein folding under controlled mechanical conditions. - Source: PubMed
Publication date: 2026/08/01
Chaudhuri DeepBhatt MadhuHaldar Shubhasis