Recombinant Human Cyclophilin A / CYPA Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1522

Recombinant Human Cyclophilin A / CYPA Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1522
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Product Overview

Tag His
Host Species Human
Accession P62937
Synonym CYPA, CYPH, HEL-S-69p
Background Peptidyl-prolyl cis-trans isomerase A, also known as PPIase A, Rotamase A, Cyclophilin A, Cyclosporin A-binding protein, PPIA and CYPA, is a cytoplasm protein which belongs to thecyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins (CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. PPIA / Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIA / Cyclophilin A is secreted by vascular smooth muscle cells in response to inflammatory stimuli, and could thus contribute to atherosclerosis. It is not essential for mammalian cell viability. PPIA / Cyclophilin A can 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.
Description A DNA sequence encoding the human PPIA (P62937) (Met 1-Glu 165) was expressed, with a His tag at the C-terminus.
Source E.coli
Predicted N Terminal Met 1
AA Sequence Met 1-Glu 165
Molecular Weight The recombinant human PPIA consisting of 175 a.a. and has a calculated molecular mass of 19.4 kDa as estimated in SDS-PAGE under reducing conditions.
Purity >97% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 50mM Tris, 150mM NaCl, 20% glycerol, pH 7.7.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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. Activates endothelial cells (ECs) in a proinflammatory 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. Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis. 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. Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1. 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. Plays an important role in platelet activation and aggregation. 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. Binds heparan sulfate glycosaminoglycans. Inhibits replication of influenza A virus (IAV). 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.; (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.; (Microbial infection) Stimulates RNA-binding ability of HCV NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent manner.
Subcellular Location Cytoplasm. Secreted. Nucleus.
Protein Families Cyclophilin-type PPIase family, PPIase A subfamily
Database References

Gene Functions References

  1. Molecular structure of cyclophilin A in complex with alispovir has been presented. PMID: 30198892
  2. Cyclophilin A is required for HIV-1 Tat palmitoylation . PMID: 29884859
  3. These results suggested that the CyPA located on SV-HUC-1 cell membranes may be the potential receptor of Mycoplasma genitalium adhesion protein (MgPa), which could provide an experimental basis for elucidating the function of MgPa and the possible pathogenic mechanism of M. genitalium. PMID: 29551599
  4. increased serum cyclophilin A concentrations could reflect trauma severity and unfavorable outcome after head trauma, substantializing cyclophilin A as a potential biomarker for prognostic prediction of TBI PMID: 29885319
  5. Here, the binding site of AIF(Delta1-121) and AIF(370-394) on CypA has been mapped by NMR spectroscopy and biochemical studies, and a molecular model of the complex has been proposed. The authors show that AIF(370-394) interacts with CypA on the same surface recognized by AIF(Delta1-121) protein and that the region is very close to the CypA catalytic pocket. PMID: 28442737
  6. CyPA was significantly increased in convalescent COPD patients and further elevated in COPD patients with acute exacerbation. PMID: 29403273
  7. CypA expression was not an independent prognostic factor, but correlated with poor prognosis of lung adenocarcinoma PMID: 29027312
  8. Extracellular cyclophilin A augments platelet-dependent thrombosis and thromboinflammation. PMID: 28981554
  9. the increased expression of CyPA in ectopic endometrial tissue is associated with endometrioma recurrences and vascularity. PMID: 29081463
  10. Taken together, these findings reveal an essential role of CypA in boosting RIG-I-mediated antiviral immune responses by controlling the ubiquitination of RIG-I and MAVS. PMID: 28594325
  11. Data show that cyclophilin A (CypA) is up-regulated in oral squamous cell carcinoma (OSCC) arising from oral submucous fibrosis (OSF). PMID: 27533088
  12. K308 of NS5A is indispensable for both RNA and NS5B binding, whereas W316 is essential for protein-protein interactions with CypA and NS5B. PMID: 27676132
  13. PPIA is differentially expressed in lesional biopsy specimens from patients with atopic eczema relative to normal skin PMID: 28479159
  14. inosine-5'-monophosphate dehydrogenase 2 (IMPDH2) is an intracellular target of the PPIA-Sanglifehrin A binary complex. PMID: 28076787
  15. these data suggest that CypA-NS4B interaction regulates Yellow fever virus (YFV )replication. Finally, we present the first evidence that YFV inhibition may depend on NS4B-CypA interaction. PMID: 28317380
  16. This report reviews the literature related to the mechanism of CypA-dependent cytokine secretion and discusses this factor as a possible therapeutic target in inflammatory diseases. PMID: 28729360
  17. Networks of dynamic allostery regulate cyclophilin A function. PMID: 28089447
  18. Results show that CypA is overexpressed in human hepatocellular carcinoma (HCC) and is associated with TNM stage and suggest that CypA may be involved in the development and progression of HCC. PMID: 28739738
  19. Plasma CyPA levels can be used to predict all-cause death, rehospitalization, and coronary revascularization in patients with coronary artery disease. PMID: 28153875
  20. data suggest that rs6850 G SNP enhances HIV-1 replication through upregulation of CypA expression following HIV-1 infection PMID: 27088296
  21. These results demonstrate that SUN2 is required for the optimal activation and proliferation of primary CD4 T cells and suggest that the disruption of these processes explains the contribution of endogenous SUN2 to HIV infection in primary lymphocytes and show that CypA is not required for the decreased infection observed in SUN2-silenced cells. PMID: 28077629
  22. The critical roles of Cyclophilin A in mediating or inhibiting viral infections. [review] PMID: 27033630
  23. Overexpression of CYPA is associated with colorectal cancer. PMID: 27468721
  24. PPIA may play a pivotal role in hepatocellular carcinoma (HCC) by regulating cell growth and could serve as a novel marker and therapeutic molecular target for HCC patients. PMID: 27397650
  25. found to be coupled and temporally dispersed, ranging over 4 to 5 orders of magnitude. Finally, using network centrality measures we demonstrate the changes in the communication network, connectivity, and influence of CypA residues upon substrate binding, mutation, and during catalysis. PMID: 27071107
  26. Enhanced platelet-bound CyPA is associated with hypertension and hypercholesterolemia in stable coronary artery disease patients. In patients with acute myocardial infarction platelet-bound CyPA is significantly decreased. PMID: 26084004
  27. results indicate that the PPIA SNP rs6850: A > G is associated with increased risk for elevated plasma levels of cyclophilin A and coronary artery disease in patients with and without type 2 diabetes PMID: 26702934
  28. the states of phosphorylation of Cyp A by Akt can influence the progress of the cell cycle in multiple myeloma. PMID: 26833980
  29. review of PPIA polymorphisms and what is known about their impact on the replication cycle and course of disease for different viral infections PMID: 26281011
  30. The present knowledge on the role of cyclophilin A during coronavirus replication is summarized (Review) PMID: 26318518
  31. CsA and FK506 might interfere with selected effector T cell functions via a CrkII-, but not CrkI-dependent mechanisms. PMID: 26792730
  32. Extracellular CyPA activates platelets via cluster of differentiation 147-mediated phosphoinositid-3-kinase/Akt-signaling, leading to enhanced adhesion and thrombus formation independently of intracellular CyPA. PMID: 25550208
  33. Overexpression of CypA/WT protected the cells against cisplatin or H2O2-induced oxidative damage, however, the CypA/P16S mutant had no effect. These findings suggested that CypA exhibits a protective antioxidant effect PMID: 25738284
  34. The poor prognosis of esophageal cancer patients was associated with high expression of CypA. PMID: 25420107
  35. These results indicate a special function mode for CypA of playing more important roles in the early stage of gastric tumorigenesis. PMID: 26008617
  36. Cyclophilin A regulates HIV-1 replication kinetics and infectivity, modulates sensitivity to host restriction factors, and cooperates in the transit of the pre-integration complex into the nucleus of infected cells. PMID: 25445708
  37. The frequency of immunihistochemistry detected cyclophilin A protein expression was found to be equal in tumor of both histotypes. PMID: 24272759
  38. Cyclophilin A regulates JNK/p38-MAPK signaling through its physical interaction with ASK1. PMID: 26095851
  39. Decrease in plasma cyclophilin A concentration at 1 month after myocardial infarction predicts better left ventricular performance and synchronicity at 6 months. PMID: 25552928
  40. review of the role of cyclophilin A and CD147 in kidney diseases and potential implications for treatment of kidney diseases PMID: 25580061
  41. These findings suggest that eCyPA-CD147 signaling promotes the bone marrow homing of B cell malignancies and offer a compelling rationale for exploring this axis as a therapeutic target for these malignancies. PMID: 26005854
  42. the results indicated that the combination of ENO1 and CYPA can serve as a potential molecular marker for the early detection of NPC. PMID: 24998431
  43. CypA is secreted from CCA cells and enhances cell proliferation in an autocrine/paracrine manner, at least via direct binding with CD147, which may activate the ERK1/2 and p38 MAPK signaling pathways. PMID: 25296734
  44. The extracellular portion of cyclophilin A probably plays an important role in human diseases associated with acute or chronic inflammation. PMID: 24713575
  45. The present data demonstrate that immunophilins regulate CrkII, but not CrkI activity in T cells and suggest that CsA and FK506 inhibit selected effector T cell functions via a CrkII-dependent mechanism. PMID: 25225668
  46. These results suggested that,CypA, a gene downstream of HIF-1alpha, could promote the development of PDAC. PMID: 24662981
  47. Cyclophilin A catalyzes proline isomerization by an electrostatic handle mechanism. PMID: 24982184
  48. These data demonstrate that, while CypA promotes reverse transcription under all conditions tested here, its effect on HIV-1 infectivity correlates more closely with effects on nuclear entry of the viral cDNA. PMID: 24479545
  49. Inhibition of the AIF/CypA complex protects against intrinsic death pathways induced by oxidative stress. PMID: 24434516
  50. Patients with type 2 diabetes have higher circulating levels of cyclophilin A than the normal population. PMID: 24502618


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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