Abstract: Objective　To obtain the myofibrillogenesis regulator 1S (MR-1S)-His recombinant protein through the expression of MR-1S gene and prepare anti-MR-1S antiserum after purification. To identify the stable system to preserve the recombinant protein，and to provid the reference for the investigation of MR-1S protein characteristics and biological function.  Methods　The recombinant plasmid pET21a-MR-1S was constructed with pronucleus expression vector pET 21a(+) and transferred into Escherichia coli BL21 (DE3)，and the expression of MR-1S recombinant protein was induced by isopropyl-beta-D-thiogalactopyranoside (IPTG). The MR-1S recombinant protein was purified by affinity chromatography and identified by Western blot. The anti-MR-1S polyclonal antibodies were prepared by the rabbit-immunized technique. With comparison of the protein activities of 4 stable systems under different temperatures，the most suitable stable preservation system and condition were picked out.  Results　Recombinant plasmid pET21a-MR-1S was established，and the MR-1S-His recombinant protein was expressed solubly in Escherichia coli BL21(DE3) by the identification of Western blot. The anti-MR-1S antisera were obtained by immunization rabbit，and the satabilization system and preservation condition were definited.  Conclusions　Under undenatured conditions，the soluble MR-1S recombinant protein is expressed and can be preserved stably，and it lays the foundation for MR-1S characteristices and biological function studies.

Key words: Myofibrillogenesis regulator 1, Molecular cloning, Antibody