추천 제품
분석
>99% (TLC)
형태
powder
포장
pkg of 1 × 50 μg (with stopper and crimp cap (810184P-50ug))
제조업체/상표
Avanti Polar Lipids 810184P
배송 상태
dry ice
저장 온도
−20°C
관련 카테고리
일반 설명
Although PI(4,5)P2 is a minor component of cell membranes, it plays a critical role as a substrate for a number of important signaling proteins. PI(4,5)P2 is an intermediate in the IP3/DAG pathway where it is hydrolyzed by phospholipase C to liberate the second messengers, inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). PI(4,5)P2 is also a substrate for PI 3-kinase where it is phosphorylated to PI(3,4,5)P3, an activator of downstream signaling components such as the protein kinase AKT.
애플리케이션
TopFluor® PI(4,5)P2 or 1-oleoyl-2-{6-[4-(dipyrrometheneboron difluoride)butanoyl]amino}hexanoyl-sn-glycero-3-phosphoinositol-4,5-bisphosphate (ammonium salt) has been used as a fluorescent lipid in living cells to analyse the cellular localization of phosphatidylinositol (PI) and in the preparation of giant unilamellar vesicles (GUVs) for the ezrin-membrane tethering assays.
포장
2 mL Amber Serum Vial with Stopper and Crimp Cap (810184P-50ug)
법적 정보
Avanti Research is a trademark of Avanti Polar Lipids, LLC
TopFluor is a trademark of Avanti Polar Lipids, LLC
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
No data available
Flash Point (°C)
No data available
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
Ezrin enrichment on curved membranes requires a specific conformation or interaction with a curvature-sensitive partner
eLife, 7, e37262-e37262 (2018)
Probing the subcellular distribution of phosphatidylinositol reveals a surprising lack at the plasma membrane.
The Journal of Cell Biology, 219(3), e201906127-e201906127 (2020)
Langmuir : the ACS journal of surfaces and colloids, 32(7), 1732-1741 (2016-02-02)
Phosphatidylinositol phosphate (PIP) lipids are critical to many cell signaling pathways, in part by acting as molecular beacons that recruit peripheral membrane proteins to specific locations within the plasma membrane. Understanding the biophysics of PIP-protein interactions is critical to developing
Langmuir : the ACS journal of surfaces and colloids, 33(43), 12463-12477 (2017-09-30)
Although the evidence for the presence of functionally important nanosized phosphorylated phosphoinositide (PIP)-rich domains within cellular membranes has accumulated, very limited information is available regarding the structural determinants for compartmentalization of these phospholipids. Here, we used a combination of fluorescence
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