Mouse Anti-PPIA Recombinant Antibody (CBYC-P542) (CBMAB-P2512-YC)

Mouse

Human

CBYC-P542

IgG

WB, ICC, IHC-P, IHC-Fr, ELISA

Cyclophilin A

Human

IgG

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

PBS, pH 7.4, 0.02% sodium azide, 50% glycerol

Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

peptidylprolyl isomerase A (cyclophilin A)

PPIA is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.

CYPA; CYPH; HEL-S-69p

Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:25678563, PubMed:21593166).
Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143).
Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913).
Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815).
In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369).
Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851).
Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563).
Plays an important role in platelet activation and aggregation (By similarity).
Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity).
Binds heparan sulfate glycosaminoglycans (PubMed:11943775).
Inhibits replication of influenza A virus (IAV) (PubMed:19207730).
Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:30328013, PubMed:22347431).
(Microbial infection) May act as a mediator between human SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion of host cells by the virus (PubMed:15688292).
(Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner.

Activation of protein kinase B activityManual Assertion Based On ExperimentIDA:UniProtKB
Apoptotic processManual Assertion Based On ExperimentIDA:UniProtKB
Cell adhesion molecule productionManual Assertion Based On ExperimentIDA:UniProtKB
Cellular response to oxidative stressManual Assertion Based On ExperimentIDA:UniProtKB
Endothelial cell activationManual Assertion Based On ExperimentIDA:UniProtKB
Leukocyte chemotaxisManual Assertion Based On ExperimentIMP:UniProtKB
Lipid droplet organizationManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of protein K48-linked ubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of protein kinase activityManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of stress-activated MAPK cascadeManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of viral life cycleManual Assertion Based On ExperimentIMP:UniProtKB
Neuron differentiationIEA:Ensembl
Neutrophil chemotaxisManual Assertion Based On ExperimentIDA:UniProtKB
Platelet activationISS:UniProtKB
Platelet aggregationISS:UniProtKB
Positive regulation of MAPK cascadeManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of NF-kappaB transcription factor activityManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of protein dephosphorylationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of protein secretionManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of viral genome replicationManual Assertion Based On ExperimentIMP:UniProtKB
Protein foldingManual Assertion Based On ExperimentIBA:GO_Central
Protein peptidyl-prolyl isomerizationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of apoptotic signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of viral genome replicationManual Assertion Based On ExperimentIMP:UniProtKB
Viral release from host cellManual Assertion Based On ExperimentTAS:UniProtKB

Cytoplasm
Secreted
Nucleus
Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that includes Rho GTPase signaling, actin remodeling, and myosin II activation.

Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition (PubMed:20364129, Ref.12). Acetylation at Lys-125 favors its interaction with TARDBP (PubMed:25678563).