Cloning, expression and purification of the C-terminal section of murine heat shock protein gp96 / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 619-622, 2004.
Artigo
em Chinês
| WPRIM
| ID: wpr-270075
ABSTRACT
Heat shock protein gp96 is a glycoprotein which was found several years ago. Besides its function as a molecular chaperone, it is also reported to play important roles both in innate immunity and adaptive immunity. Gp96 can stimulate the maturation of antigen presenting cells (especially dendritic cells) and the secretion of cytokines. Gp96 and its associated peptides could stimulate peptide specific cytotoxic T lymphocyte reaction (CTL), which was very promising in the designing of anti-virus and anti-tumor vaccines. However the expression level of whole length gp96 was relatively low in E. coli and the purity of gp96 are not very suitable for further study. We successfully cloned the carboxy terminal fragment (560aa-751aa) of murine gp96 into the pGEX-6p-1 vector and expressed in BL21 strain. This fragment contains the peptide binding domain and the dimerization domain. After purification, the recombinant fusion protein was cleaved with the PreScission Protease and analyzed by Gelfiltration. The results show that this fragment may be related to the dimerization of gp96 and make an foundation for further investigations of the protein.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fragmentos de Peptídeos
/
Proteínas Recombinantes de Fusão
/
Western Blotting
/
Cromatografia em Gel
/
Clonagem Molecular
/
Genética
/
Antígenos de Neoplasias
Limite:
Animais
Idioma:
Chinês
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2004
Tipo de documento:
Artigo
Similares
MEDLINE
...
LILACS
LIS