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L-Lysine lactam (hydrochloride) Sale

(Synonyms: 3-氨基六氢-2H-氮杂卓-2-酮盐酸盐) 目录号 : GC47572

A building block

L-Lysine lactam (hydrochloride) Chemical Structure

Cas No.:26081-07-2

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50 mg
¥428.00
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100 mg
¥823.00
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500 mg
¥2,141.00
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1 g
¥3,854.00
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Sample solution is provided at 25 µL, 10mM.

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产品描述

L-lysine lactam is a building block.1,2 It has been used in the synthesis of lysine sulfonamide HIV protease inhibitors, as well as bengamide derivatives with in vitro anticancer activity.

1.Stranix, B.R., LavallÉe, J.-F., SÉvigny, G., et al.Lysine sulfonamides as novel HIV-protease inhibitors: N?-Acyl aromatic ɑ-amino acidsBioorg. Med. Chem. Lett.16(13)3459-3462(2006) 2.Phi, T.D., Mai, H.D.T., Tran, V.H., et al.Design, synthesis and cytotoxicity of bengamide analogues and their epimersMedchemcomm.8(2)445-451(2016)

Chemical Properties

Cas No. 26081-07-2 SDF
别名 3-氨基六氢-2H-氮杂卓-2-酮盐酸盐
Canonical SMILES N[C@@H]1C(NCCCC1)=O.Cl
分子式 C6H12N2O.HCl 分子量 164.6
溶解度 PBS (pH 7.2): 10 mg/ml 储存条件 Store at -20°C
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1 mM 6.0753 mL 30.3767 mL 60.7533 mL
5 mM 1.2151 mL 6.0753 mL 12.1507 mL
10 mM 0.6075 mL 3.0377 mL 6.0753 mL
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Research Update

Effects of penicillins and 6-aminohexanoic acid on the kinetics of human plasmin

Biochem J 1989 Jun 1;260(2):609-12.PMID:2527494DOI:PMC1138714

Human plasmin activity is inhibited by various penicillins in a dose-dependent manner. Ampicillin and cloxacillin produce a 50% inhibition of the globinolytic activity of plasmin at 4.5 and 5.3 mM respectively. A lower inhibitory capacity is displayed by carbenicillin. Assay of plasmin by its amidolytic activity on D-valyl-L-leucyl-L-lysine p-nitroanilide dihydrochloride showed that ampicillin at a concentration producing half-maximal inhibition converted the hyperbolic activity-substrate concentration curve into a sigmoidal curve. A similar conversion occurred in the presence of ampicillin when plasmin was assayed with an alternative chromogenic substrate, L-pyroglutamyl-glycyl-L-arginine p-nitroanilide hydrochloride 6-Aminohexanoic acid at 7.5 microM abolished the inhibition of plasmin induced by ampicillin. The present observations suggest that ampicillin interacts with plasmin at a regulatory site different from the active site of the enzyme. The effect of 6-aminohexanoic acid indicates that the lysine-binding site may be part of a regulatory site. It is possible that modulation of plasmin activity by ligands plays a role in the control of fibrinolysis.