United States set
Menu Shopping cart $0 Search
Manufactured by BioVendor

Cyclophilin B Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Rotamase B, S-cyclophilin, SCYLP, PPIB, CYPB
  • Species:Human
Cat. No. Size Price
1 - 4 pcs / 5 - 9 pcs / 10+ pcs

RD172360100 0.1 mg $421 / $370 / On request
PubMed Product Details
Technical Data


Recombinant protein


Total 193 AA. MW: 22 kDa (calculated). UniProtKB acc.no. P23284 (Asp34-Glu216). N-terminal His-tag (10 extra AA). Protein identity confirmed by MS.

Amino Acid Sequence



E. coli


˃ 90 % by SDS-PAGE


14 % SDS-PAGE separation of Human Cyclophilin B:
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and boiled sample, 2.5 μg/lane
3. non-reduced and non-boiled sample, 2.5 μg/lane


< 1.0 EU/µg


Filtered (0.4 μm) and lyophilized from 0.5 mg/mL solution in 20 mM Tris buffer, 50 mM NaCl, pH 7.5.


Add 200 µl of deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely.


Western blotting, ELISA


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80 °C for long term storage. Reconstituted protein can be stored at 4 °C for three days.

Quality Control Test

BCA to determine quantity of the protein.
SDS PAGE to determine purity of the protein. Endotoxin level determination.


This product is intended for research use only.


Research topic

Immunology, Oncology


Cyclophilin B (CypB, Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, rotamerase B, S-cyclophilin, SCYLP, PPIB) is a 21-kDa protein belonging to the cyclophilin family. Cyclophilins are ubiquitous cellular proteins with peptidyl-prolyl cis-trans isomerase enzymatic activity, which are involved in a variety of functions related to cell metabolism, energy homeostasis, and exhibit enhanced expression in inflammation or malignancy. CypB has been identified in the endoplasmic reticulum and nucleus of all cell types and is also secreted in notable levels in the serum and breast milk. Structurally, CypB shows a high degree of homology with other members of the cyclophilin family in its core β-barrel/isomerase region, which contains a surface hydrophobic pocket that constitutes the proline binding motif. Both N- and C- termini of CypB differ significantly from other cyclophilin family members. Within the N-terminus, CypB contains a nuclear translocation motif (DEKKKGPKV), while the endoplasmic reticulum retention sequence (AIAKE) resides in its C-terminus. This ER-retention motif is proteolytically clipped in the ER, enabling secretion of CypB into the extracellular milieu. The larger biological function of CypB has remained enigmatic. Within the nucleus, ongoing research has demonstrated that CypB functions as a transcriptional inducer of Stat5-mediated gene expression. Given the association of CypB with other intracellular transcription factors, these findings suggest that CypB could serve to coordinate global networks of gene expression. At the cell surface, CypB also serves as a ligand for CD147 receptor that in turn regulates mitogen-activated protein kinase activation, motility, calcium transport and expression of the pro-apoptotic protein Bim. The extracellular fractions of CypB are involved in cell-cell communication and inflammatory signaling however on its own, CypB seems to be unable to induce pro-inflammatory cytokines. CypB acts in progression of inflammatory diseases such as rheumatoid arthritis and psoriasis, but is equally involved in the first steps of certain viral infections. Its inflammatory activity is conditioned by its interaction with heparan sulfate proteoglycans and the membrane receptor CD147, two binding partners at the cell surface of T cell lymphocytes, granulocytes and macrophages. CypB is able to induce chemotaxis and triggers T lymphocyte adhesion to fibronectin in the extracellular matrix. Cyclophilin B is closely associated with the occurrence and progression of tumors. This protein has been shown to be highly expressed in breast, liver, colon, stomach and pancreatic cancer.

Summary References (10)

References to Cyclophilin B

  • Meng DQ, Li PL, Xie M: Expression and role of cyclophilin B in stomach cancer. J of Genetics and Molecular Research. May; 14 (2): 5346-5354 (2015)
  • Naoumov N: Cyclophilin inhibition as potential therapy for liver diseases. J of Hepatology. July; 61 (5): 1166-1174 (2014)
  • Ray P, Rialon-Guevara KL, Veras E, Sullenger BA, White RR: Comparing human pancreatic cell secretomes by in vitro aptamer selection identifies cyclophilin B as a candidate pancreatic cancer biomarker. J of Clinical Investigation. May; 122 (5): 1734-1741 (2012)
  • Suñé G, Sarró E, Puigmulé M, López-Hellín J, Zufferey M, Pertel T, Luban J, Meseguer A: Cyclophilin B Interacts with Sodium-Potassium ATPase and Is Required for Pump Activity in Proximal Tubule Cells of the Kidney. PlosOne. Nov.; 5 (11): e13930 (2010)
  • Fang F, Zheng J, Galbaugh TL, Fiorillo AA, Hjort EE, Zeng X, Clevenger CHV: Cyclophilin B as a co-regulator of prolactin-induced gene expression and function in breast cancer cells. J of Molecular Endocrinology. June; 44 (6): 319-329 (2010)
  • Choi JW, Sutor SL, Lindquist L, Evans GL, Madden BJ, Bergen HR, Hefferan TE, Yaszemski MJ, Bram RJ: Severe Osteogenesis Imperfecta in Cyclophilin B-Deficient Mice. Plos Genetics. Dec.; 5 (12): e1000750 (2009)
  • Fang F, Flegler AJ, Du P, Lin S, Clevenger CHV: Expression of Cyclophilin B is Associated with Malignant Pogression and Regulation of Genes Implicated in the Pathogenesis of Breast Cancer. J of Pathology. Jan.; 174 (1): 297-308 (2009)
  • Kim J, Choi TG, Ding Y, Kim Y, Ha KS, Lee KH, Kang I, Ha J, Kaufamn RJ, Lee J, Choe W, Kim SS: Overexpressed cyclophilin B suppresses apoptosis associated with ROS and Ca2+ homeostasis after ER stress. J of Cell Science. Nov.; 121 (21): 3636-3648 (2008)
  • Hanoulle X, Melchior A, Sibille N, Parent B, Denys A, Wieruszeski JM, Horvath D, Allain F, Lippens G, Landrieu I: Structural and Functional Characterization of the Interaction between Cyclophilin B and a Heparin-derived Oligosaccharide. J of Biological Chemistry. Nov.; 282 (47): 34148-34158 (2007)
  • Vanpouille CH, Deligny A, Delehedde M, Denys A, Melchior A, Liénard X, Lyon M, Mazurier J, Fernig DG, Allain F: The Heparin/Heparan Sulfate Sequence That Interacts with Cyclophilin B Contains a 3-O-Sulfated N-Unsubstituted Glucosamine Residue. J of Biological Chemistry. Aug.; 282 (33): 24416-24429 (2007)
Related Products Docs