Expression and purification of GST-CML28 fusion protein and preparation of its polyclonal antibody / 中国实验血液学杂志
Journal of Experimental Hematology
;
(6): 1302-1306, 2012.
Artículo
en Chino
| WPRIM
| ID: wpr-278385
ABSTRACT
This study was aimed to investigate the expression of GST-CML28 in Escherichia Coli and to prepare its antibody. The constructed recombinant expression vectors CML28-pGEX-3X were transformed into Escherichia Coli BL21 under IPTG induction. The protein was abstracted from the transformers, and purified by a GSTrap FF column. The rabbits were immunized by the purified fusion protein to produce serum with anti-CML28 antibody. The serum was purified by chromatographic column stuffed with glutathione Sephamse 4B to get the antibody. The specific antibody against CML28 was further identified by ELISA, Western blot, immunohistochemistry and quantum dot luminescence. The results indicated that GST-CML28 fusion protein was expressed in Escherichia coli and its specific polyclonal antibody was obtained. It is concluded that the anti-CML28 polyclonal antibodies with high titer and specificity are successfully prepared. These antibodies provide an useful experimental tool to profoundly research the physiological significance and biological function of the CML28 gene.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Proteínas Recombinantes de Fusión
/
Células Cultivadas
/
Proteínas de Unión al ARN
/
Biología Celular
/
Alergia e Inmunología
/
Escherichia coli
/
Células Endoteliales de la Vena Umbilical Humana
/
Complejo Multienzimático de Ribonucleasas del Exosoma
/
Vectores Genéticos
/
Glutatión Transferasa
Límite:
Animales
/
Humanos
Idioma:
Chino
Revista:
Journal of Experimental Hematology
Año:
2012
Tipo del documento:
Artículo
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