|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for PPIA(NM_021130.4) Search again
Product ID:
HQP013694
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CYPA, CYPH, HEL-S-69p
Gene Description:
peptidylprolyl isomerase A
Target Gene Accession:
NM_021130.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Summary
This gene encodes 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. Multiple pseudogenes that map to different chromosomes have been reported. [provided by RefSeq].
Gene References into function
- novel mode of tyrosine kinase regulation for a Tec family member and provide a molecular basis for understanding a cellular function of the ubiquitous peptidyl prolyl isomerase, CypA
- NMR relaxation methods used to characterize conformational exchange during catalysis
- Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A.
- Active site residues of cyclophilin A are crucial for its signaling activity via CD147
- Effects of gag mutations on human immunodeficiency virus type 1 particle assembly, processing, and cyclophilin A incorporation.
- Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.
- functional CypA required for Vesicular Stomatis Virus-New Jersey replication and infection; interacts with the nucleocapsid (N) protein of VSV-NJ and VSV-IND in infected cells, but not obligatory for the latter serotype.
- Comparative molecular modeling of allergenic cyclophilin proteins, including cyclophilin A, was performed in order to investigate the structural basis of their cross-reactivity.
- Cyclophilin A interacts with HIV-1 Vpr and is required for its functional expression
- alternative splicing and role implicated in interaction with HIV-1
- CYPA and AIF cooperate in apoptosis-associated chromatinolysis.
- CyPA is a novel paracrine and autocrine modulator of EC functions in immune-mediated vascular disease
- Recombinant CyPA activated MAP kinases in cultured human umbilical vein EC & stimulated IkappaB-alpha phosphorylation, NF-kappaB activation, & adhesion molecule expression. It may play a role in the pathogenesis of inflammatory diseases.
- Results suggest that the N-terminal domain of the capsid domain of the HIV-1 Gag precursor polyprotein is the preferential site for cyclophilin A binding.
- Interaction energy and dynamical cross-correlation calculations are used for a detailed investigation of the protein-protein interactions in the cyclophilin A-HIV-1 capsid protein complex.
- identify a network of protein vibrations, extending from surface regions of the enzyme to the active site and coupled to substrate turnover. Crucial parts of this network are found to be conserved in 10 cyclophilin structures from six different species.
- Results describe the binding of severe acute respiratory syndrome coronavirus to human cyclophilin A.
- cyclophilin A binds CD99 and may be either a signaling mediator or a signaling regulator for CD99
- affects the fate of incoming HIV-1 capsid either directly or by modulating interactions with unidentified host cell factors.
- CypA substantially alters the mRNA levels of several key genes in human vascular cells, indicating potential multifunctional roles of CypA in vascular system.
- x-ray crystallographic analysis of human cyclophilin A in complex with the novel immunosuppressant sanglifehrin A
- The peptide FGPDLPAGD showed inhibition of the isomerase reaction and NMR chemical shift mapping experiments highlight the cyclophilin A interaction epitope
- analysis of HIV-1 Gag protein interactions with cyclophilin A
- protects HIV-1 from an unknown antiviral activity in human cells, completely independnet of TRIM5alpha
- results support that Pseudomonas aeruginosa exoenzyme S ADP-ribosylates and affects the function of the cytosolic protein, CpA, with the predominant functional effect relating to interference of CpA-cellular protein interactions
- PPIA, the c-myc-regulated gene is involved in genotype-C-HBV-related HCC, suggesting that c-myc is related to the hepatocarcinogenic activity of genotype-C HBV.
- Cyclophilin A is a downstream target in Fhit-mediated cessation of cell cycle progression at late G(1) phase.
- cyclophilin A and G2 cell cycle arrest appear to be two independent factors important for efficient lentiviral gene transfer
- Diverse lentiviruses, FIV and SIVagmTAN also bind to CypA.
- Results describe a novel vif-sensitive antiviral activity of human cyclophilin A that may limit zoonotic transmission of SIV and the first demonstration of CypA encapsidation into a virus other than human immunodeficiency virus type 1.
- the expression of CypA and its receptor CD147 in several kinds of lung cancer cells as well as a normal lung cell and found that in H446 cell, a kind of small cell lung cancer cell, the expression are the highest
- virus assembly and disassembly are attractive candidate processes for antiviral intervention; HIV-1 capsid (CA) protein and human cyclophilin A (CypA) play important roles in these processes
- CyPA acts as a potent monocyte chemoattractant and induces monocyte Il-6 release, implying a role for extracellular CyPA in the pathogenesis of atherosclerosis via activation of monocytes rather than endothelial cells
- most potent derivative binds CypA with a K(d) of 11.2+/-9.2 microM and an IC50 for activity against Caenorhabditis elegans (C. elegans) of 190 microM compared to 28 microM for cyclophilin A
- Data show that cyclophilin A is required for CXCR4-mediated nuclear export of heterogeneous nuclear ribonucleoprotein A2,activation and nuclear translocation of ERK1/2, and chemotactic cell migration.
- PPIA variation did not significantly contribute to the risk of suffering from myocardial infarction among patients with atherosclerotic diseased vessels.
- reveal the molecular mechanism of cyclosporine resistance and identify CyPA as a critical cellular cofactor for HCV replication and infection
- cyclophilin A gene was identified as the most suitable normaliser in gene expression studies involving human airway epithelial cells derived from normal, atopic and asthmatic children
- These data suggest that cyclophilin A may serve as a novel prognostic factor and possibly an attractive therapeutic target for endometrial carcinoma.
- The peptidyl-prolyl isomerase (PPI) cyclophilin A (CypA), which is implicated in the regulation of protein conformation, is necessary for the prolactin (PRL)-induced activation of Jak2 and the progression of human breast cancer.
- The data suggest a role for CypA in uncoating the core of HIV-1 to facilitate integration.
- The A1650G polymorphism in the regulatory region of the CypA gene may be associated with protection from HIV-1 infection.