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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Expression and purification of regulatory and catalytic domains of protein kinase C isoforms using maltose binding protein fusion expression system

등록일
2008년 8월 11일 17시 32분 43초
접수번호
0706
발표코드
33P198포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
김초롱, 소재원
인하대학교 화학과, Korea
Protein kinase C (PKC) isoforms are a family of at least 10 serine/threonine kinases divided into three subfamilies: classical, novel & atypical, and are important modifiers of several cardiovascular phenomena, carcinogenesis & apoptosis and also promising therapeutic target for cancer and other indications. In our present study, we expressed and purified regulatory domain and catalytic domain mutants of PKC isoforms. Bacterial protein expression plasmids were constructed by using pMBPN3 vector. These expression vectors were transformed into BL21(DE3) E.coli strain and expressed by IPTG induction. Proteins were expressed as MBP fusion protein and purified by amylose resin. We checked the protein expression levels by SDS-PAGE analysis. We will use these proteins to characterize isoform-specific protein-protein interactions between PKC and other PKC-interacting proteins.

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