C3805
Cyclophilin A human
≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution
Synonym(s):
CyP
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Assay:
≥95% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Concentration:
≥0.3 mg/mL
biological source
human
recombinant
expressed in E. coli
assay
≥95% (SDS-PAGE)
form
buffered aqueous solution
mol wt
20 kDa
concentration
≥0.3 mg/mL
technique(s)
cell culture | mammalian: suitable
UniProt accession no.
storage temp.
−20°C
Quality Level
Gene Information
human ... PPIA(5478)
General description
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.
Biochem/physiol Actions
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.
Physical form
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
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Julien Pottecher et al.
Journal of vascular surgery, 57(4), 1100-1108 (2013-01-22)
By binding to cyclophilin D, cyclosporine A (CsA) inhibits mitochondrial permeability transition pore (mPTP) opening and prevents mitochondrial dysfunction and ultimately cell death after ischemia-reperfusion (IR) injury in cardiac muscle. This study tested whether CsA would decrease skeletal muscle oxidative
Cyclophilin A
Satoh K, et al.
Circulation Journal, 74(11), 2249-2256 (2010)
G Fischer et al.
Nature, 337(6206), 476-478 (1989-02-02)
The enzyme peptidyl-prolyl cis-trans isomerase (PPIase) was recently discovered in mammalian tissues and purified from porcine kidney. It catalyses the slow cis-trans isomerization of proline peptide (Xaa-Pro) bonds in oligopeptides and accelerates slow, rate-limiting steps in the folding of several
Francisco J Roca et al.
Cell, 153(3), 521-534 (2013-04-16)
Tumor necrosis factor (TNF) constitutes a critical host defense against tuberculosis, but its excess is also implicated in tuberculosis pathogenesis in zebrafish and humans. Using the zebrafish, we elucidate the pathways by which TNF mediates tuberculosis pathogenesis. TNF excess induces
Haruhiro Toko et al.
Circulation research, 112(9), 1244-1252 (2013-03-15)
Cardiac hypertrophy results from the complex interplay of differentially regulated cascades based on the phosphorylation status of involved signaling molecules. Although numerous critical regulatory kinases and phosphatases have been identified in the myocardium, the intracellular mechanism for temporal regulation of
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