C3805
Cyclophilin A human
≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution
Synonyme(s) :
CyP
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
human
Niveau de qualité
Produit recombinant
expressed in E. coli
Pureté
≥95% (SDS-PAGE)
Forme
buffered aqueous solution
Poids mol.
20 kDa
Concentration
≥0.3 mg/mL
Technique(s)
cell culture | mammalian: suitable
Numéro d'accès UniProt
Température de stockage
−20°C
Informations sur le gène
human ... PPIA(5478)
Description générale
Cyclophilins are a family of extremely conserved proteins, known as immunophilins. Cyclophilin A (CyPA) is present in all tissues in prokaryotes and eukaryotes. It is present in all organs of human. Cyclophilin A (CyPA), a 20 kDa chaperone protein, that is liberated from vascular smooth muscle cells (VSMCs).
Application
Cyclophilin A human has been used in the study to interpret the mechanisms by which extracellular CyPA initiates endothelial activation.
Actions biochimiques/physiologiques
Cyclophilin A (CyPA) participates in intracellular signalling and protein trafficking. It helps to control other proteins activity. CyPA plays a physiological and pathological role in cardiovascular diseases. Hence it acts as an important biomarker and mediator in several cardiovascular diseases, like vascular stenosis, atherosclerosis and abdominal aortic aneurysms. CyPA can induce the proliferation and inflammatory cell migration of vascular smooth muscle cells (VSMC) in vitro and in vivo.
Cyclophilins are peptidyl prolyl isomerases that catalyze the cis-trans isomerization of X-Pro peptide bonds. They are highly-conserved cytoplasmic enzymes that accelerate protein folding and facilitate HIV infectivity. Cyclosporin A binds to cyclophilin and inhibits its activity. The cyclosporin A-cyclophilin complex binds to calcineurin and inhibits T-cell activation. The structure of human, recombinant cyclophilin is given by Holzman, et al.
Forme physique
Composed of amino acids 1-165 plus an N-terminal 20 amino acid His-tag
Solution in 20mM Tris, pH 8.0, containing 20 mM NaCl, 0.5 mM DTT and 10% glycerol
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Atsushi Kumanogoh et al.
Nature reviews. Immunology, 13(11), 802-814 (2013-12-10)
Semaphorins were originally identified as axon-guidance molecules that function during neuronal development. However, cumulative evidence indicates that semaphorins also participate in immune responses, both physiological and pathological, and they are now considered to be potential diagnostic and/or therapeutic targets for
Nikhil Raghuram et al.
The Journal of cell biology, 203(1), 57-71 (2013-10-09)
Histone H1 plays a crucial role in stabilizing higher order chromatin structure. Transcriptional activation, DNA replication, and chromosome condensation all require changes in chromatin structure and are correlated with the phosphorylation of histone H1. In this study, we describe a
Cyclophilin A
Satoh K, et al.
Circulation Journal, 74(11), 2249-2256 (2010)
Roger van Kruchten et al.
Blood, 121(10), 1850-1857 (2013-01-11)
Scott syndrome, a bleeding disorder caused by defective phospholipid scrambling, has been associated with mutations in the TMEM16F gene. The role of TMEM16F in apoptosis- or agonist-induced phosphatidylserine (PS) exposure was studied in platelets from a Scott syndrome patient and
Päivi Pihlajamaa et al.
The EMBO journal, 33(4), 312-326 (2014-01-24)
Androgen receptor (AR) binds male sex steroids and mediates physiological androgen actions in target tissues. ChIP-seq analyses of AR-binding events in murine prostate, kidney and epididymis show that in vivo AR cistromes and their respective androgen-dependent transcription programs are highly
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