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Chymostatin
本产品不向个人销售，仅用作科学研究，不用于任何人体实验及非科研性质的动物实验。
Chymostatin图片
CAS NO:9076-44-2
包装与价格：
包装价格(元)
5mg电议
10mg电议
25mg电议
50mg电议

产品介绍
Chymostatin 是一种有效的组织蛋白酶 G 抑制剂。
Cas No.9076-44-2
别名胰凝乳蛋白酶抑制剂
化学名(2R,6R,9R,12R)-6-((R)-2-amino-3,4,5,6-tetrahydropyrimidin-4-yl)-2,12-dibenzyl-9-isobutyl-4,7,10,13-tetraoxo-3,5,8,11-tetraazatridecan-1-oic acid
Canonical SMILESO=C(O)[C@H](NC(N[C@H]([C@H]1CCN=C(N)N1)C(N[C@H](CC(C)C)C(N[C@H](CC2=CC=CC=C2)C=O)=O)=O)=O)CC3=CC=CC=C3
分子式C31H41O6N7
分子量607.7
溶解度DMSO: 10 mg/ml,DMSO:PBS (pH 7.2) (1:1): 0.5 mg/ml
储存条件Store at -20℃
General tipsFor obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.
Shipping ConditionEvaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
产品描述

Chymostatin is a bioactive peptide of microbial origin that acts as a protease inhibitor with selectivity for chymotryptase-like serine proteases.[1] It potently inhibits chymotrypsin and chymase (Ki = 9.36 and 13.1 nM, respectively) while less effectively blocking the activity of cathepsins, papain, and leukocyte elastase.[2],[1],[3],[4],[5] It is without effect on trypsin, thrombin, plasmin, pepsin, and kallikrein.[1]

Reference:
[1]. Umezawa, H., Aoyagi, T., Morishima, H., et al. Chymostatin, a new chymotrypsin inhibitor produced by actinomycetes. J.Antibiot.(Tokyo) 23(8), 425-427 (1970).
[2]. Akahoshi, F., Ashimori, A., Sakashita, H., et al. Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic difluoromethylene ketones as novel inhibitors of human chymase. Journal of Medicinal Chemistry 44(8), 1297-1304 (2001).
[3]. Feinstein, G., Malemud, C.J., and Janoff, A. The inhibition of human leucocyte elastase and chymotrypsin-like protease by elastatinal and chymostatin. Biochim.Biophys.Acta. 429(3), 925-932 (1976).
[4]. Stein, R.L., and Strimpler, A.M. Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin. Biochemistry 26(9), 2611-2615 (1987).
[5]. Yamamoto, K., Takeda, M., and Kato, Y. Characteristics of activation of cathepsin B by sodium salicylate and comparison of catalytic site properties of cathepsins B and H. Japanese Journal of Pharmacology 39(2), 207-215 (1985).