| First Author | Matesanz F | Year | 1998 |
| Journal | Cytokine | Volume | 10 |
| Issue | 4 | Pages | 249-53 |
| PubMed ID | 9617568 | Mgi Jnum | J:48212 |
| Mgi Id | MGI:1266978 | Doi | 10.1006/cyto.1997.9998 |
| Citation | Matesanz F, et al. (1998) High expression in bacteria and purification of polymorphic mouse interleukin 2 molecules. Cytokine 10(4):249-53 |
| abstractText | Recently, besides the known mouse interleukin 2 (IL-2) molecule, six other IL-2 alleles have been found in different mouse strains. In order to study their in vivo and in vitro biological activities large quantities are required. We cloned the corresponding IL-2 cDNAs into pET7- 7/BL21(DE3) bacterial system, a T7-RNA-polymerase- dependent expression vector, producing between 30 to 100 mg of IL-2 per litre of culture. The purification step is based on the resolution properties of the sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) technique and the capability of the IL-2 to regain its activity after SDS denaturation, These purified IL-2 molecules supported the growth of an IL-2-dependent cell line, CTL-L2, in a similar way to a commercial mouse IL-2 control. However, RF IL-2 allele, which is also expressed in NOD mice had a relatively lower growth activity in the CTL-L2 assay, These IL-2 molecules can be obtained in a purified form and totally recovered their activity after elimination of the SDS and 2-mercaptoethanol used in the extraction procedure. (C) 1998 Academic Press Limited. |
