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474791

Sigma-Aldrich

MG-132

InSolution, ≥98%, 10 mM, reversible proteasome inhibitor

Sinonimo/i:

Z-Leu-Leu-Leu-al, Carbobenzoxy-L-leucyl-L-leucyl-L-leucinal, Z-LLL-CHO, Proteasome Inhibitor XI, InSolution MG-132, MG-132

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1 MG
87,00 €
5 MG
294,00 €

87,00 €

Spedizione prevista il18 aprile 2025Dettagli

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Cambia visualizzazione
1 MG
87,00 €
5 MG
294,00 €

About This Item

Formula empirica (notazione di Hill):
C26H41N3O5
Numero CAS:
133407-82-6
Peso molecolare:
475.62
Numero MDL:
MFCD00674886
Codice UNSPSC:
12352200
NACRES:
NA.77

87,00 €

Spedizione prevista il18 aprile 2025Dettagli

Livello qualitativo

100

Saggio

≥98% (HPLC)

Stato

liquid

Produttore/marchio commerciale

Calbiochem®

Condizioni di stoccaggio

OK to freeze
protect from light

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

Stringa SMILE

[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
TZYWCYJVHRLUCT-VABKMULXSA-N

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Amino Acid Sequence

Z-Leu-Leu-Leu-al

Descrizione generale

Potent, reversible, and cell-permeable proteasome inhibitor (Ki = 4 nM). Reduces the degradation of ubiquitin-conjugated proteins in mammalian cells and permeable stains of yeast by the 26S complex without affecting its ATPase or isopeptidase activities. Activates c-Jun N-terminal kinase (JNK1) and inhibits NF-κB activation (IC50 = 3 µM).

Azioni biochim/fisiol

Cell permeable: yes
Product does not compete with ATP.
Reversible: yes
Target IC50: 3 µM in inhibiting NF-κB activation
Target Ki: 4 nM as proteasome inhibitor

Confezionamento

Packaged under inert gas

Attenzione

Toxicity: Irritant (B)

Stato fisico

A 10 mM (1 mg/210 µl) or (5mg/1050 µl) solution of MG-132 (Cat. No. 474790) in DMSO.

Altre note

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.

Note legali

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

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

188.6 °F - closed cup - (Dimethylsulfoxide)

Punto d’infiammabilità (°C)

87 °C - closed cup - (Dimethylsulfoxide)

Certificati d'analisi (COA)

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Sigma-Aldrich

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Sigma-Aldrich

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Sigma-Aldrich

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Sigma-Aldrich

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Cicloesimide from microbial, ≥94% (TLC)

Sigma-Aldrich

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Cicloesimide

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
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
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-
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
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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