추천 제품
제품 라인
BioReagent
Quality Level
분석
≥97.0% (HPLC)
적합성
suitable for fluorescence
SMILES string
CCN(CC)c1ccc2C=C(C(=O)NCCN3C(=O)C=CC3=O)C(=O)Oc2c1
InChI
1S/C20H21N3O5/c1-3-22(4-2)14-6-5-13-11-15(20(27)28-16(13)12-14)19(26)21-9-10-23-17(24)7-8-18(23)25/h5-8,11-12H,3-4,9-10H2,1-2H3,(H,21,26)
InChI key
IXQPRUQVJIJUEB-UHFFFAOYSA-N
애플리케이션
7-Diethylamino-3-[N-(2-maleimidoethyl)carbamoyl]coumarin is utilized as a fluoresencent biological sensing device . Used for real-time measurements for the release of inorganic phosphates during enzymatic reaction when MDCC is conjugated to a mutant phosphate-binding protein . Also, utilized for intramolecular fluorescence energy transfer (FRET) experiments .
Thiol-reactive probe for protein labelling
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이미 열람한 고객
A Vandecandelaere et al.
Biochemistry, 38(25), 8179-8188 (1999-07-01)
The molecular mechanism underlying microtubule dynamic instability depends on the relationship between the addition of tubulin-GTP to a growing microtubule and its hydrolysis in the microtubule lattice to tubulin-GDP, with release of inorganic phosphate (Pi). Since this relationship remains controversial
Z He et al.
Biophysical journal, 75(5), 2389-2401 (1998-10-28)
Inorganic phosphate (Pi) release was determined by means of a fluorescent Pi-probe in single permeabilized rabbit soleus and psoas muscle fibers. Measurements of Pi release followed photoliberation of approximately 1.5 mM ATP by flash photolysis of NPE-caged ATP in the
Adam Shutes et al.
Methods in enzymology, 407, 9-22 (2006-06-08)
Ras proteins are small GTPases that exhibit high-affinity binding to GDP and GTP and hydrolyze bound GTP to GDP. The intrinsic GTPase activity of Ras proteins is accelerated by GTPase activating proteins (GAPs), which act to attenuate GTPase signaling by
Simone Kunzelmann et al.
The Journal of biological chemistry, 284(48), 33130-33138 (2009-10-06)
Nearly every cellular process requires the presence of ATP. This is reflected in the vast number of enzymes like kinases or ATP hydrolases, both of which cleave the terminal phosphate from ATP, thereby releasing ADP. Despite the fact that ATP
Robert A Phillips et al.
Biochemistry, 42(13), 3956-3965 (2003-04-02)
Individual rate constants have been determined for each step of the Ras.GTP hydrolysis mechanism, activated by neurofibromin. Fluorescence intensity and anisotropy stopped-flow measurements used the fluorescent GTP analogue, mantGTP (2'(3')-O-(N-methylanthraniloyl)GTP), to determine rate constants for binding and release of neurofibromin.
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