跳转至内容
Merck
CN
所有图片(1)

主要文件

539175

Sigma-Aldrich

Proteasome Inhibitor IV

The Proteasome Inhibitor IV controls the biological activity of Proteasome. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.

别名:

Proteasome Inhibitor IV, Z-GPFL-CHO

登录查看公司和协议定价


About This Item

经验公式(希尔记法):
C30H38N4O6
分子量:
550.65
UNSPSC代码:
12352200

质量水平

方案

≥90% (HPLC)

表单

lyophilized solid

制造商/商品名称

Calbiochem®

储存条件

OK to freeze
protect from light

颜色

white

溶解性

DMSO: 5 mg/mL

运输

ambient

储存温度

−20°C

一般描述

A tetrapeptide aldehyde that acts as a highly selective and potent proteasomal inhibitor (Ki = 1.5 µM for branched chain amino acid preferring, 2.3 µM for small neutral amino acid preferring, and 40.5 µM for chymotrypsin-like activities; IC50 = 3.1 µM for peptidyl-glutamyl peptide hydrolyzing activity). Shown to be a weak inhibitor of trypsin-like proteasomal activity.

生化/生理作用

Cell permeable: no
Primary Target
branched chain amino acid preferring,small neutral amino acid preferring, chymotrypsin-like activities
Product does not compete with ATP.
Reversible: no
Target Ki: 1.5 µM, 2.3 µM, and 40.5 µM against branched chain amino acid preferring, small neutral amino acid preferring, and chymotrypsin-like activities of proteasomes, respectively

包装

Packaged under inert gas

警告

Toxicity: Standard Handling (A)

序列

Z-Gly-Pro-Phe-Leu-CHO

重悬

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

其他说明

Oberdorf, J., et al. 2001. Biochemistry40, 13397.
Cardozo, C., et al. 1999. Biochemistry38, 9768.
Eleuteri, A.M., et al. 1997. J. Biol. Chem.272, 11824.
Orlowski, M., et al. 1997. Biochemistry36, 13946.
Vinitsky, A., et al. 1994. J. Biol. Chem.269, 29860.

法律信息

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

储存分类代码

11 - Combustible Solids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable


分析证书(COA)

输入产品批号来搜索 分析证书(COA) 。批号可以在产品标签上"批“ (Lot或Batch)字后找到。

已有该产品?

在文件库中查找您最近购买产品的文档。

访问文档库

J Oberdorf et al.
Biochemistry, 40(44), 13397-13405 (2001-10-31)
Misfolded proteins in the endoplasmic reticulum (ER) are degraded by N-terminal threonine proteases within the 26S proteasome. Each protease is formed by an activated beta subunit, beta5/X, beta1/Y, or beta2/Z, that exhibits chymotrypsin-like, peptidylglutamyl-peptide hydrolyzing, or trypsin-like activity, respectively. Little
A M Eleuteri et al.
The Journal of biological chemistry, 272(18), 11824-11831 (1997-05-02)
Amino acid sequencing of subunits of the multicatalytic proteinase complex (MPC) isolated from bovine spleen showed an almost complete replacement of the X, Y, and Z subunits, constitutively expressed in most tissues, by the interferon-gamma-inducible LMP7, LMP2, and MECL1 subunits.
A Vinitsky et al.
The Journal of biological chemistry, 269(47), 29860-29866 (1994-11-25)
Evidence indicates that a component of the multicatalytic proteinase complex (MPC) that preferentially cleaves bonds after branched chain amino acids (BrAAP) is a major factor responsible for the protein-degrading activity of the MPC. We report here the synthesis of substrate-related
C Cardozo et al.
Biochemistry, 38(30), 9768-9777 (1999-07-28)
Two catalytic components of the multicatalytic proteinase complex (MPC, proteasome) designated as chymotrypsin-like (ChT-L) and branched chain amino acid preferring (BrAAP) cleave bonds after hydrophobic amino acids. The possible involvement of the ChT-L and peptidylglutamyl-peptide hydrolyzing (PGPH) activities in the
M Orlowski et al.
Biochemistry, 36(45), 13946-13953 (1997-12-31)
Exposure to [14C]-3,4-dichloroisocoumarin (DCI) of multicatalytic proteinase complexes (MPC) isolated from bovine pituitary and spleen leads to label incorporation into several beta-type subunits, to rapid inactivation of the chymotrypsin-like (ChT-L) activity, and to a slower inactivation of other activities of

我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.

联系技术服务部门