추천 제품
product name
4-Nitrophenyl decanoate, lipase substrate
Quality Level
분석
≥98% (TLC)
형태
powder
solubility
chloroform: soluble 100 mg/mL, colorless to faintly yellow
저장 온도
−20°C
SMILES string
CCCCCCCCCC(=O)Oc1ccc(cc1)[N+]([O-])=O
InChI
1S/C16H23NO4/c1-2-3-4-5-6-7-8-9-16(18)21-15-12-10-14(11-13-15)17(19)20/h10-13H,2-9H2,1H3
InChI key
RRNKCSIEGPOIKI-UHFFFAOYSA-N
유사한 제품을 찾으십니까? 방문 제품 비교 안내
애플리케이션
4-Nitrophenyl decanoate has been used as a substrate for assessing the lipase activity spectrophotometrically. It has also been used as a substrate for estimating the carboxylesterases activity.
4-Nitrophenyl decanoate has been used as a substrate to assess the carboxylesterase production by recombinant Penicillium griseoroseum T55 strain. It has also been used for general esterase activity assay of the hepatopancreas extract.
생화학적/생리학적 작용
4-Nitrophenyl decanoate is a substrate for lipase enzyme. The extracellular lipase has greater hydrolysis reaction velocity with 4-nitrophenyl decanoate when compared with other 4-nitropheny esters.
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.
이미 열람한 고객
Prikladnaia biokhimiia i mikrobiologiia, 48(4), 376-382 (2012-10-06)
As a result of sequencing the genome of the termophilic alkali-tolerant lipolytic bacterium Thermosyntropha lipolytica, the gene encoding a lipase secreted into the medium was identified. The recombinant enzyme was expressed in Escherichia coli. It was isolated, purified, and functionally
Methods in Molecular biology: Platelets and Megakaryocytes, volume 1, functional assays, 27-27 (2012)
Scientific reports, 8(1), 10000-10000 (2018-07-04)
We determined the effect of the His-tag on the structure, activity, stability and immobilization of LipC12, a highly active lipase from a metagenomic library. We purified LipC12 with a N-terminal His-tag and then removed the tag using tobacco etch virus
Isolation and characterization of an enzyme from the Greenshell? mussel Perna canaliculus that hydrolyses pectenotoxins and esters of okadaic acid
Toxicon, 60(3), 406-419 (2012)
Frontiers in bioengineering and biotechnology, 8, 844-844 (2020-08-28)
The multiple inhibitors tolerance of microorganism is important in bioconversion of lignocellulosic biomass which is a promising renewable and sustainable source for biofuels and other chemicals. The disruption of an unknown α/β hydrolase, which was termed KmYME and located in
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