추천 제품
product name
4-Nitrophenyl β-D-galactopyranoside, ≥98% (enzymatic)
분석
≥98% (TLC)
≥98% (enzymatic)
형태
powder
solubility
water: 10 mg/mL, clear, colorless to very faintly green
저장 온도
−20°C
SMILES string
OC[C@H]1O[C@@H](Oc2ccc(cc2)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@H]1O
InChI
1S/C12H15NO8/c14-5-8-9(15)10(16)11(17)12(21-8)20-7-3-1-6(2-4-7)13(18)19/h1-4,8-12,14-17H,5H2/t8-,9+,10+,11-,12-/m1/s1
InChI key
IFBHRQDFSNCLOZ-YBXAARCKSA-N
유사한 제품을 찾으십니까? 방문 제품 비교 안내
애플리케이션
4-Nitrophenyl β-D-galactopyranoside has been used:
- as a substrate to assess the activity of glycosaminoglycan (GAG)-degrading enzymes
- as a substrate to study the kinetic properties of recombinant Leuconostoc mesenteroides glycosidase (BgLm1) and determine β-glucosidase activity
- to prepare substrate solution in a modified universal buffer
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.
이미 열람한 고객
Identification, purification and characterization of a novel glycosidase (BgLm1) from Leuconostoc mesenteroides
LWT--Food Science and Technology null
A high-throughput microplate assay for simultaneous colorimetric quantification of multiple enzyme activities in soil
Applied soil ecology : a section of Agriculture, Ecosystems & Environment null
Journal of vascular research, 43(1), 95-100 (2005-11-19)
The abdominal aortic aneurysm (AAA) wall represents an extreme example of arterial remodeling with disturbed elastin, collagen and proteoglycan metabolism. The aim of this study was to evaluate enzymes involved in the degradation of glycosaminoglycan chains and core proteins of
Biochemistry, 42(6), 1796-1803 (2003-02-13)
Trp-999 is a key residue for the action of beta-galactosidases (Escherichia coli). Several site specific substitutions (Phe, Gly, Tyr, Leu) for Trp-999 were made. Each substitution caused greatly decreased affinities for substrates and inhibitors that bind in the "shallow" mode
Proceedings of the National Academy of Sciences of the United States of America, 108(37), 15147-15151 (2011-09-08)
The lactose permease (LacY) catalyzes galactoside/H(+) symport via an alternating access mechanism in which sugar- and H(+)-binding sites in the middle of the molecule are alternatively exposed to either side of the membrane by opening and closing of inward- and
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