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质量水平
储存温度
−20°C
SMILES字符串
OC(=O)CNC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)\C=C\c2ccco2
InChI
1S/C20H21N3O6/c24-17(9-8-15-7-4-10-29-15)23-16(11-14-5-2-1-3-6-14)20(28)22-12-18(25)21-13-19(26)27/h1-10,16H,11-13H2,(H,21,25)(H,22,28)(H,23,24)(H,26,27)/b9-8+/t16-/m0/s1
InChI key
ZDLZKMDMBBMJLI-FDMDGMSGSA-N
基因信息
human ... ACE(1636) , ACE2(59272)
mouse ... ACE3(217246)
rat ... ACE(11421) , ACE2(70008) , ACE3(498012)
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Amino Acid Sequence
FA-Phe-Gly-Gly
一般描述
N-[3-(2-呋喃基)丙烯酰基]-Phe-Gly-Gly 作为血管紧张素转化酶 (ACE) 的底物,用于 ACE 的抑制试验。
应用
N-[3-(2-呋喃基)丙烯酰基] 苯基-Gly-Gly 已用于 ACE(血管紧张素转化酶)抑制活性的动力学分光光度法测定。
底物
连续分光光度法测定血管紧张素转化酶 (ACE) 的底物。
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
Scientific reports, 7(1), 12243-12243 (2017-09-28)
Quality control is critical for ensuring the safety and effectiveness of drugs. Current quality control method for botanical drugs is mainly based on chemical testing. However, chemical testing alone may not be sufficient as it may not capture all constituents
Clinical chemistry, 39(2), 312-316 (1993-02-01)
In the kinetic angiotensin-converting enzyme (ACE) method, a practical and optimal buffer is 80 mmol/L borate buffer at pH 8.2 (37 degrees C). A lag phase is detected in the reaction, and a 5-min incubation of substrate and plasma is
Clinical chemistry, 30(6), 901-902 (1984-06-01)
In this automated kinetic modification of a previous method (Anal Biochem 95: 540-548, 1979) for determining angiotensin-converting enzyme (EC 3.4.15.1), 3-(2- furylacryloyl )-L- phenylalanylglycylglycine is used as the substrate. The change in absorbance at 340 nm is used to monitor
Journal of pharmaceutical and biomedical analysis, 24(5-6), 1151-1156 (2001-03-15)
For determination of levels of plasmatic inhibitor of ACE (angiotensin convertase) a simple method was used based on a combination of enzymatic reaction followed by an HPLC determination of its product. The inhibitor (e.g. enalaprilat) was at first separated from
Marine drugs, 17(3) (2019-03-22)
Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis.
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