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方案
≥98% (TLC)
表单
powder
溶解性
H2O: insoluble
储存温度
−20°C
SMILES字符串
CC(C)C[C@H](N)C(=O)Nc1ccc2ccccc2c1
InChI
1S/C16H20N2O/c1-11(2)9-15(17)16(19)18-14-8-7-12-5-3-4-6-13(12)10-14/h3-8,10-11,15H,9,17H2,1-2H3,(H,18,19)/t15-/m0/s1
InChI key
JWHURRLUBVMKOT-HNNXBMFYSA-N
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应用
L-Leucine β-naphthylamide has been used as a substrate:
- to measure the activity of aminopeptidase in Escherichia coli
- to evaluate the enzyme activity of cathepsin H from rabbit skeletal muscles
- in the proteolytic assay of L-Leucine aminopeptidase
Substrate for leucine aminopeptidase determination in colorimetric and histochemical procedures.
包装
Bottomless glass bottle. Contents are inside inserted fused cone.
质量
Very low free β-naphthylamine.
底物
Substrate for aminopeptidase M
其他客户在看
Aminopeptidase (arylamidase) activity in discrete areas of the rat brain: sex differences.
J M de Gandarias et al.
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme, 21(5), 285-286 (1989-05-01)
Masanori Matsuishi et al.
The international journal of biochemistry & cell biology, 35(4), 474-485 (2003-02-05)
Rabbit muscle cathepsin H classified as an aminoendopeptidase was purified and its properties were investigated to clarify its contribution to the proteolysis of postmortem muscle. The purification was performed by ammonium sulfate fractionation and successive chromatographies on Sephadex G-75, phosphocelluose
J M de Gandarias et al.
Journal of biochemical toxicology, 7(3), 171-175 (1992-01-01)
Carbon disulfide, a volatile solvent, is widely used in industry. It has been demonstrated that it causes several neuropsychological symptoms. However, the neurochemical basis of its neurotoxic effect is relatively unknown. In this paper we have measured the effect of
T Nishimura et al.
European journal of biochemistry, 137(1-2), 23-27 (1983-12-01)
The mode of action towards oligopeptides and proteins of hydrolase H purified from rabbit skeletal muscle was studied. The presence of protamine or alpha-N-benzoylarginine p-nitroanilide (an endopeptidase substrate) changed both the Km and V values of the enzyme towards Leu-beta-naphthylamide
F Marciano-Cabral et al.
The Journal of protozoology, 34(2), 146-149 (1987-05-01)
An intracellular alpha-aminoacyl-peptide hydrolase (EC 3.4.11.-) from Naegleria fowleri nN68 (ATCC 30894) has been characterized. The enzyme preparation hydrolyzed phenylalanyl-, tyrosyl-, leucyl-, arginyl-, alanyl-, tryptophanyl-, histidyl-, methionyl-, and lysyl-naphthylamide but not benzoylleucyl-, leucylglycyl-, glycylprolylleucyl-, glycyl-, threonyl-, aspartyl-, or glutamyl-naphthylamide. The
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