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C3805

Sigma-Aldrich

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:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

human

Quality Level

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

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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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