Generation and Characterization of Novel Human IRAS Monoclonal Antibodies. (10th August 2009)

• Record Type: Journal Article
• Authors: Wang, Bo; Liu, Ying; Shan, Yajun; Yao, Zhenyu; Liu, Xiaolan; Su, Ruibin; Sun, Qihong; Cong, Yuwen; Li, Jin
• Other Names: Watts Val J. Academic Editor.
• Is Part Of: Journal of biomedicine and biotechnology. Volume 2009(2009)
• Publication Date: 2009-08-10
• Subjects: Medicine -- Periodicals; Biology -- Periodicals; Biotechnology -- Periodicals; Medicine; Biology; Biotechnology; Médecine; Biologie; Biotechnologie; Biology; Biotechnology; Medicine; Biotechnology; Biomedicine; Electronic journals; Periodical; Periodicals; Electronic journals; 610
• DOI: 10.1155/2009/973754
• Languages: English
• ISSNs: 1110-7243

Abstract

Abstract : Imidazoline receptors were first proposed by Bousquet et al., when they studied antihypertensive effect of clonidine. A strong candidate for I1R, known as imidazoline receptor antisera-selected protein (IRAS), has been cloned from human hippocampus. We reported that IRAS mediated agmatine-induced inhibition of opioid dependence in morphine-dependent cells. To elucidate the functional and structure properties of I1R, we developed the newly monoclonal antibody against the N-terminal hIRAS region including the PX domain (10–120aa) through immunization of BALB/c mice with the NusA-IRAS fusion protein containing an IRAS N-terminal (10–120aa). Stable hybridoma cell lines were established and monoclonal antibodies specifically recognized full-length IRAS proteins in their native state by immunoblotting and immunoprecipitation. Monoclonal antibodies stained in a predominantly punctate cytoplasmic pattern when applied to IRAS-transfected HEK293 cells by indirect immunofluorescence assays and demonstrated excellent reactivity in flow immunocytometry. These monoclonal antibodies will provide powerful reagents for the further investigation of hIRAS protein functions.