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Z-(L-Arg)-AMC (hydrochloride) Sale

(Synonyms: Z-L-精氨酸-7-胺基-4-甲基香豆素盐酸盐) 目录号 : GC48471

A fluorogenic substrate for trypsin, cathepsin B, and cathepsin H

Z-(L-Arg)-AMC (hydrochloride) Chemical Structure

Cas No.:70375-22-3

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10mg
¥942.00
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25mg
¥1,645.00
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50mg
¥3,066.00
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100mg
¥5,654.00
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Sample solution is provided at 25 µL, 10mM.

产品文档

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产品描述

Z-(L-Arg)-AMC is a fluorogenic substrate for trypsin, cathepsin B, and cathepsin H.1,2 Upon enzymatic cleavage by trypsin, cathepsin B, or cathepsin H, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify trypsin, cathepsin B, and cathepsin H activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively.

1.Zimmerman, M., Ashe, B., Yurewicz, E.C., et al.Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substratesAnal. Biochem.78(1)47-51(1977) 2.Brindley, P.J., Kalinna, B.H., Dalton, J.P., et al.Proteolytic degradation of host hemoglobin by schistosomesMol. Biochem. Parasitol.89(1)1-9(1997)

Chemical Properties

Cas No. 70375-22-3 SDF
别名 Z-L-精氨酸-7-胺基-4-甲基香豆素盐酸盐
Canonical SMILES NC(NCCC[C@@H](C(NC1=CC=C(C(C)=CC(O2)=O)C2=C1)=O)NC(OCC3=CC=CC=C3)=O)=N.Cl
分子式 C24H27N5O5•HCl 分子量 502
溶解度 DMF: 1 mg/ml,DMSO: 1 mg/ml 储存条件 -20°C
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储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
为了提高溶解度,请将管子加热至37℃,然后在超声波浴中震荡一段时间。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.992 mL 9.9602 mL 19.9203 mL
5 mM 0.3984 mL 1.992 mL 3.9841 mL
10 mM 0.1992 mL 0.996 mL 1.992 mL
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Research Update

Differential Cleaving of Specific Substrates for Cathepsin-Like Activity Shows Cysteine and Serine Protease Activities and a Differential Profile Between Anisakis simplex s.s. and Anisakis pegreffii, Sibling Species Major Etiologic Agents of Anisakiasis

Foodborne Pathog Dis 2019 Nov;16(11):744-751.PMID:31215796DOI:10.1089/fpd.2019.2633

Humans can contract anisakiasis by eating fish or squid containing live larvae of the third stage (L3) of the parasitic nematodes of the genus Anisakis, majorly from Anisakis simplex s.s. and Anisakis pegreffii, sibling species of the A. simplex s.l. complex. Most cases diagnosed molecularly are due to A. simplex s.s., although A. pegreffii has also been identified in human cases. Cathepsins are mostly lysosomal multifunctional cysteine proteases and can participate in the pathogenicity of parasites. Cathepsin B and L activities were investigated in the two sibling species of Anisakis mentioned. L3 and L4 of both species were collected during their in vitro development, and cathepsin activity was determined in the range of pH 4.0-8.5, using specific fluorogenic substrates. The activity detected with the substrate Z-FR-AMC (N-α-benzyloxycarbonyl-L-phenylalanyl-L-arginine-7-amido-4-methyl-coumarin) was identified as cathepsin L (optimum pH = 5.0, range 4.0-6.0, p < 0.001). Activity was highest in L3 freshly collected from fish, especially in A. simplex s.s., and decreased during development, which could be related to virulence, invasion of host tissues, and/or intracellular digestion. Cathepsin B-like activity was not identified with either of the substrates used (Z-RR-AMC [N-α-benzyloxycarbonyl-L-arginyl-L-arginine-7-amido-4-methyl-coumarin] and Z-FR-AMC). With Z-RR-AMC, cleaving activity was detected almost exclusively in L4 of A. simplex s.s. (p < 0.05) with optimum pH = 8.0 (range 7.0-8.5). Assays with class-specific protease inhibitors showed that this activity was mainly due to serine proteases [up to 90% inhibition with 4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride (AEBSF)], although metalloproteases (up to 40-45% inhibition with 1,10 phenanthroline) and slight cysteine protease activity (<15% inhibition with E64 [L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane]; putative cathepsin B-like) were also detected. These results show differential serine protease activity between sibling Anisakis species, regulated by larval development, at least in A. simplex s.s. The higher cathepsin L and serine protease activities detected in this species could be related to its greater pathogenicity, reported in experimental animals, compared to that of A. pegreffii.