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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
底の開いたガラス瓶内容物は内部に挿入され接着された円錐部に入っています。
品質
微量の遊離β-ナフチルアミン。
基質
アミノペプチダ-ゼMの基質
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
L1635-BULK:
L1635-1G:
L1635-500MG:
L1635-250MG:
L1635-100MG:
L1635-VAR:
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Proteolytic activity in the placenta, decidua and postimplantation embryos of the rat.
A Fein et al.
Israel journal of medical sciences, 21(4), 394-396 (1985-04-01)
A M Reisenauer et al.
Science (New York, N.Y.), 227(4682), 70-72 (1985-01-04)
The regulation of amino-oligopeptidase (AOP), an intestinal brush border hydrolase essential for the surface digestion of peptide nutrients, was examined in rats in vivo. Short-term (30-minute) intraintestinal perfusion of a tetrapeptide substrate, Gly-Leu-Gly-Gly, or a synthetic substrate, leucyl-beta-naphthylamide, induced a
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
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
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