추천 제품
product name
Resorufin β-D-galactopyranoside, ~95%
분석
~95%
Quality Level
형태
powder
solubility
DMSO: 20 mg/mL, clear, orange to red
저장 온도
−20°C
SMILES string
OC[C@H]1O[C@@H](Oc2ccc3N=C4C=CC(=O)C=C4Oc3c2)[C@H](O)[C@@H](O)[C@H]1O
InChI
1S/C18H17NO8/c20-7-14-15(22)16(23)17(24)18(27-14)25-9-2-4-11-13(6-9)26-12-5-8(21)1-3-10(12)19-11/h1-6,14-18,20,22-24H,7H2/t14-,15+,16+,17-,18-/m1/s1
InChI key
QULZFZMEBOATFS-DISONHOPSA-N
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일반 설명
Resorufin β-D-galactopyranoside is a non-fluorescent compound and is orange-yellow in color. It is hydrolyzed by the enzyme β-galactosidase (β-Gal) to yield fluorescent resorufin.
포장
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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.
Microchip device for performing enzyme assays
Hadd AG, et al.
Analytical Chemistry, 69(17), 3407-3412 (1997)
Immobilized enzyme kinetics analyzed by flow-through microfluorimetry: resorufin-beta-D-galactopyranoside as a new fluorogenic substrate for beta-galactosidase
Hofmann J and Sernetz M
Analytica Chimica Acta, 163, 67-72 (1984)
Yuliang Xie et al.
Analytical chemistry, 84(17), 7495-7501 (2012-08-14)
In this work we present an acoustofluidic approach for rapid, single-shot characterization of enzymatic reaction constants K(m) and k(cat). The acoustofluidic design involves a bubble anchored in a horseshoe structure which can be stimulated by a piezoelectric transducer to generate
Seung-Yong Jung et al.
Langmuir : the ACS journal of surfaces and colloids, 24(9), 4439-4442 (2008-03-26)
A device with femtoliter-scale chambers and controlled reaction initiation was developed for single-molecule enzymology. Initially separated substrate and enzyme streams were rapidly mixed in a microfluidic device and encapsulated in an array of individual microreactors, allowing for enzyme kinetics to
Brian P English et al.
Nature chemical biology, 2(2), 87-94 (2006-01-18)
Enzymes are biological catalysts vital to life processes and have attracted century-long investigation. The classic Michaelis-Menten mechanism provides a highly satisfactory description of catalytic activities for large ensembles of enzyme molecules. Here we tested the Michaelis-Menten equation at the single-molecule
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