Cyclophilin A Antibody [H11E16] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:100 IF1:1000 FCM1:2000

Application
WB, IP, IHC, FCM

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
18 kDa

Positive Control	Jurkat cells; HeLa cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Cyclophilin A Antibody [H11E16] detects endogenous levels of total Cyclophilin A protein.

Clone
H11E16

Synonym(s)
CYPA; PPIA; Peptidyl-prolyl cis-trans isomerase A; PPIase A; Cyclophilin A; Cyclosporin A-binding protein; Rotamase A

Background
Cyclophilin A (CypA) is a member of the immunophilin family of peptidyl-prolyl cis-trans isomerases (PPIases) that catalyze the interconversion of proline peptide bonds, accelerating protein folding and conformational dynamics. The 165-amino-acid protein adopts an eight-stranded antiparallel β-barrel structure flanked by two α-helices, with a hydrophobic active site pocket (comprising Arg55, Phe60, Gln63, and Lys82) that coordinates substrate proline residues for efficient isomerization. CypA is highly abundant in the cytosol, where it chaperones client proteins such as HIV-1 Gag p55 during viral uncoating and nuclear import, facilitating replication. Inhibition of its PPIase activity by cyclosporin A blocks calcineurin-NFAT signaling, suppressing T-cell cytokine production. Under oxidative stress or inflammatory conditions, CypA is secreted, binding the CD147 receptor on endothelial cells to activate ERK1/2 and NF-κB pathways. This upregulates adhesion molecules (VCAM-1, ICAM-1), chemokines (CXCL8, IL-1), and reactive oxygen species (ROS), amplifying leukocyte recruitment during inflammation. In the vascular endothelium, extracellular CypA inhibits eNOS via KLF2 repression, promotes LDL oxidation and uptake by scavenger receptors, and induces matrix metalloproteinases (MMPs), contributing to atherosclerotic plaque instability. CypA also modulates infection outcomes: it restricts some viruses by isomerizing capsid loops or influencing innate immunity, but is exploited by HIV for capsid maturation and by HCV to evade apoptosis. Mitochondrial CypA regulates mtDNA stability and respiratory chain assembly, while nuclear pools affect pre-mRNA splicing and telomere maintenance. CypA overexpression drives proliferation, migration, and metastasis via CD147/FAK signalling, promotes angiogenesis (via VEGF), and confers chemoresistance by stabilising mutant p53 or XIAP. Rheumatoid arthritis synovial fibroblasts secrete CypA to fuel IL-6/TNF inflammatory storms, and plasma CypA levels rise after myocardial infarction, correlating with injury severity.

Background

Cyclophilin A (CypA) is a member of the immunophilin family of peptidyl-prolyl cis-trans isomerases (PPIases) that catalyze the interconversion of proline peptide bonds, accelerating protein folding and conformational dynamics. The 165-amino-acid protein adopts an eight-stranded antiparallel β-barrel structure flanked by two α-helices, with a hydrophobic active site pocket (comprising Arg55, Phe60, Gln63, and Lys82) that coordinates substrate proline residues for efficient isomerization. CypA is highly abundant in the cytosol, where it chaperones client proteins such as HIV-1 Gag p55 during viral uncoating and nuclear import, facilitating replication. Inhibition of its PPIase activity by cyclosporin A blocks calcineurin-NFAT signaling, suppressing T-cell cytokine production. Under oxidative stress or inflammatory conditions, CypA is secreted, binding the CD147 receptor on endothelial cells to activate ERK1/2 and NF-κB pathways. This upregulates adhesion molecules (VCAM-1, ICAM-1), chemokines (CXCL8, IL-1), and reactive oxygen species (ROS), amplifying leukocyte recruitment during inflammation. In the vascular endothelium, extracellular CypA inhibits eNOS via KLF2 repression, promotes LDL oxidation and uptake by scavenger receptors, and induces matrix metalloproteinases (MMPs), contributing to atherosclerotic plaque instability. CypA also modulates infection outcomes: it restricts some viruses by isomerizing capsid loops or influencing innate immunity, but is exploited by HIV for capsid maturation and by HCV to evade apoptosis. Mitochondrial CypA regulates mtDNA stability and respiratory chain assembly, while nuclear pools affect pre-mRNA splicing and telomere maintenance. CypA overexpression drives proliferation, migration, and metastasis via CD147/FAK signalling, promotes angiogenesis (via VEGF), and confers chemoresistance by stabilising mutant p53 or XIAP. Rheumatoid arthritis synovial fibroblasts secrete CypA to fuel IL-6/TNF inflammatory storms, and plasma CypA levels rise after myocardial infarction, correlating with injury severity.

References
https://pubmed.ncbi.nlm.nih.gov/39513594/ https://pubmed.ncbi.nlm.nih.gov/24982184/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%