Ugrás a tartalomra
Merck

C3805

Sigma-Aldrich

Cyclophilin A human

≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution

Szinonimák:

CyP

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54

biológiai forrás

human

Minőségi szint

rekombináns

expressed in E. coli

Teszt

≥95% (SDS-PAGE)

form

buffered aqueous solution

molekulatömeg

20 kDa

koncentráció

≥0.3 mg/mL

technika/technikák

cell culture | mammalian: suitable

UniProt elérési szám

tárolási hőmérséklet

−20°C

Géninformáció

human ... PPIA(5478)

Általános leírás

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).

Alkalmazás

Cyclophilin A human has been used in the study to interpret the mechanisms by which extracellular CyPA initiates endothelial activation.

Biokémiai/fiziológiai hatások

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.

Fizikai forma

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

Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
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
Cyclophilin A
Satoh K, et al.
Circulation Journal, 74(11), 2249-2256 (2010)
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
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

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