추천 제품
재조합
expressed in baculovirus infected Sf9 cells
Quality Level
제품 라인
PRECISIO® Kinase
분석
≥70% (SDS-PAGE)
양식
buffered aqueous glycerol solution
특이 활성도
17-23 nmol/min·mg
분자량
~59 kDa
UniProt 수납 번호
배송 상태
dry ice
저장 온도
−70°C
유전자 정보
human ... RIPK2(8767)
일반 설명
Receptor interacting serine/threonine kinase 2 (RIPK2) or RICK is a serine/threonine kinase. It contains a kinase domain at the amino-terminal, an intermediate domain and a caspase activation and recruitment domain (CARD) at the carboxy-terminal. The gene encoding RIPK2 is localized on human chromosome 8q21.3.
생화학적/생리학적 작용
Receptor interacting serine/threonine kinase 2 (RIPK2) or RICK is activated during innate immune responses and acts as a scaffold for downstream effectors. It functions in nuclear factor-κB (NFκB) activation pathways. The protein also has roles in toll-like receptor (TLR)-signaling pathways and in the production of inflammatory cytokines.
물리적 형태
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
법적 정보
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Knockdown of receptor-interacting serine/threonine protein kinase-2 (RIPK2) affects EMT-associated gene expression in human hepatoma cells.
Anticancer Research, 3775-3783 (2012)
Current biology : CB, 8(15), 885-888 (1998-08-26)
Members of the tumor necrosis factor receptor (TNFR) superfamily have an important role in the induction of cellular signals resulting in cell growth, differentiation and death. TNFR-1 recruits and assembles a signaling complex containing a number of death domain (DD)-containing
Receptor-interacting protein 2 (RIP2) gene polymorphisms are associated with increased risk of subclinical atherosclerosis and clinical and metabolic parameters. The Genetics of Atherosclerotic Disease (GEA) Mexican study.
Experimental and Molecular Pathology (2017)
Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation.
PLoS ONE (2017)
RIP2, a checkpoint in myogenic differentiation.
Molecular and Cellular Biology (2002)
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