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Key Documents

C3805

Sigma-Aldrich

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 de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

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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Cyclophilin A
Satoh K, et al.
Circulation Journal, 74(11), 2249-2256 (2010)
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
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
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
Elan Zohar Eisenmesser et al.
Science (New York, N.Y.), 295(5559), 1520-1523 (2002-02-23)
Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action

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