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Merck
CN

474791

Sigma-Aldrich

MG-132

≥98% (HPLC), proteasome inhibitor, liquid

别名:

Z-Leu-Leu-Leu-al, InSolution MG-132, 碳苯并-L-亮氨酰-L-亮氨酰-L-亮氨酸，Z-LLL-CHO，蛋白酶体抑制剂XI, MG-132

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关于此项目

经验公式（希尔记法）:
C26H41N3O5
化学文摘社编号:
133407-82-6
分子量:
475.62
MDL编号:
MFCD00674886
UNSPSC代码:
12352200
NACRES:
NA.77

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产品名称

MG-132, InSolution, ≥98%, 10 mM, reversible proteasome inhibitor

质量水平

100

方案

≥98% (HPLC)

表单

liquid

制造商/商品名称

Calbiochem®

储存条件

OK to freeze
protect from light

运输

wet ice

储存温度

−20°C

SMILES字符串

[H]C(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCc1ccccc1

InChI

1S/C26H41N3O5/c1-17(2)12-21(15-30)27-24(31)22(13-18(3)4)28-25(32)23(14-19(5)6)29-26(33)34-16-20-10-8-7-9-11-20/h7-11,15,17-19,21-23H,12-14,16H2,1-6H3,(H,27,31)(H,28,32)(H,29,33)/t21-,22-,23-/m0/s1

InChI key

TZYWCYJVHRLUCT-VABKMULXSA-N

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相关类别

Amino Acid Sequence

Z-Leu-Leu-Leu-al

一般描述

高效、可逆和细胞可透过性蛋白酶体抑制剂（(Ki = 4 nM）。可通过26S复合物降低哺乳动物细胞和酵母可渗透菌株中泛素结合蛋白的降解，而不会影响其ATP酶或异肽酶的活性。可激活c-Jun N端激酶（JNK1）、抑制NF-κB的活化（IC50 = 3 µM）。

生化/生理作用

产品不与ATP竞争。
可逆性：是
细胞渗透性：是
靶标IC50：3 µM抑制NF-κB活化
靶标Ki：4 nM作为蛋白酶体抑制剂

包装

用惰性气体包装

外形

10 mM（1 mg/210 µl）或（5 mg/1050 l）MG-132 DMSO溶液（货号474790）提供。

其他说明

Meriin, A.B., et al. 1998.J. Biol. Chem.273, 6373.
Adams, J., and Stein, R. 1996.Ann.Rep.Med. Chem.31, 279.
Lee, D.H., and Goldberg, A.L.1996.J. Biol. Chem.271, 27280.
Wiertz, E.J.H.J., et al. 1996.Cell84, 769.
Read, M.A., et al. 1995.Immunity2, 493.
Rock, K.L., et al. 1994.Cell78, 761.

法律信息

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

免责声明

毒性：刺激性（B）

储存分类代码

10 - Combustible liquids

WGK

WGK 2

闪点(°F)

188.6 °F - closed cup - (Dimethylsulfoxide)

闪点(°C)

87 °C - closed cup - (Dimethylsulfoxide)

分析证书(COA)

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E J Wiertz et al.
Cell, 84(5), 769-779 (1996-03-08)
Human cytomegalovirus (HCMV) down-regulates expression of MHC class I products by selective proteolysis. A single HCMV gene, US11, which encodes an endoplasmic reticulum (ER) resident type-I transmembrane glycoprotein, is sufficient to cause this effect. In US11+cells, MHC class I molecules
D H Lee et al.
The Journal of biological chemistry, 271(44), 27280-27284 (1996-11-01)
We have studied whether various agents that inhibit purified yeast and mammalian 26 S proteasome can suppress the breakdown of different classes of proteins in Saccharomyces cerevisiae. The degradation of short-lived proteins was inhibited reversibly by peptide aldehyde inhibitors of
Clarissa Braun et al.
Cell stress, 5(12), 176-182 (2021-12-18)
Programmed cell death protein 4 (PDCD4) exerts critical functions as tumor suppressor and in immune cells to regulate inflammatory processes. The phosphoinositide 3-kinase (PI3K) promotes degradation of PDCD4 via mammalian target of rapamycin complex 1 (mTORC1). However, additional pathways that
A B Meriin et al.
The Journal of biological chemistry, 273(11), 6373-6379 (1998-04-16)
Inhibition of the major cytosolic protease, proteasome, has been reported to induce programmed cell death in several cell lines, while with other lines, similar inhibition blocked apoptosis triggered by a variety of harmful treatments. To elucidate the mechanism of pro-
M A Read et al.
Immunity, 2(5), 493-506 (1995-05-01)
Multiple cell adhesion proteins are up-regulated in vascular endothelial cells in response to TNF alpha and other inflammatory cytokines. This increase in cell adhesion gene expression is thought to require the transcription factor NF-kappa B. Here, we show that peptide
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