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SML1135

Sigma-Aldrich

MG-132(R)

≥95% (HPLC)

Sinonimo/i:

Z-L-Leu-D-Leu-L-Leu-al

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About This Item

Formula empirica (notazione di Hill):
C26H41N3O5
Numero CAS:
1211877-36-9
Peso molecolare:
475.62
Numero MDL:
MFCD28580122
Codice UNSPSC:
12352200
ID PubChem:
329825671
NACRES:
NA.32

Nome Commerciale

SAFC Hitech®

Livello qualitativo

200

Saggio

≥95% (HPLC)

Stato

powder

Solubilità

DMSO: soluble

Temperatura di conservazione

−20°C

Stringa SMILE

O=C(N[C@H](CC(C)C)C(N[C@H](C=O)CC(C)C)=O)[C@H](CC(C)C)NC(OCC1=CC=CC=C1)=O

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-ZRBLBEILSA-N

Informazioni sul gene

human ... CTSB(1508) , NFKB1(4790) , PSMA1(5682)

Categorie correlate

Azioni biochim/fisiol

MG-132(R) is a potent, membrane-permeable proteasome inhibitor. It induces neurite outgrowth in PC12 cells at 10 M. MG-132(R) blocks cleavage of poly(ADP-ribose) polymerase and apoptosis in thymocytes. However, MG-132(R) also activates c-Jun N-terminal protein kinase (JNK-1), which initiates apoptosis in response to cell stress. Proteasome inhibition induces accumulation of heat shock protein mRNA, activation of heat-shock proteins, and enhanced thermotolerance in various cell types.

Note legali

SAFC Hitech is a registered trademark of Sigma-Aldrich Co. LLC

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

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Certificati d'analisi (COA)

Lot/Batch Number
128M4095V
048M4061V
087M4104V
106M4029V
065M4044V

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Sigma-Aldrich

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SN50 trifluoroacetate salt ≥95% (HPLC)

Sigma-Aldrich

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SN50 trifluoroacetate salt

ALLN Cell-permeable inhibitor of calpain I (Ki = 190 nM), calpain II (Ki = 220 nM), cathepsin B (Ki = 150 nM), and cathepsin L (Ki = 500 pM).

Sigma-Aldrich

208719

ALLN

The effect of MG132, a proteasome inhibitor on HeLa cells in relation to cell growth, reactive oxygen species and GSH.
Han YH
Oncology Reports, 22(1), 215-221 (2009)
Yinfeng Xu et al.
FEBS letters, 593(15), 1974-1982 (2019-06-04)
The tumor protein p53-inducible nuclear protein 2 (TP53INP2) has been reported to participate in autophagy by interacting with autophagosome-localized autophagy-related protein 8 (Atg8) family proteins, including LC3. Here, we uncover a novel function for TP53INP2 in the autophagic degradation of
Ling-Yun Chu et al.
Scientific reports, 7(1), 12472-12472 (2017-10-01)
Pro-inflammatory cytokines are known to induce endothelial cell autophagy, but the role of autophagy in regulating the expression of pro-inflammatory molecules has not been characterized. We hypothesized that autophagy facilitates expression of endothelial adhesion molecules. TNFα and IL-1β induced autophagy
Yalong Wang et al.
Neuroscience letters, 739, 135402-135402 (2020-09-26)
Synaptotagmin-11 (Syt11) is associated with schizophrenia and Parkinson's disease (PD) and is a critical substrate of parkin, an E3 ubiquitin ligase linked to PD. Previously we reported that Syt11 regulates multiple membrane trafficking pathways in neurons and glia. However, the
Corinna Wentzel et al.
Nature communications, 9(1), 267-267 (2018-01-20)
Here we explore the relationship between presynaptic homeostatic plasticity and proteasome function at the Drosophila neuromuscular junction. First, we demonstrate that the induction of homeostatic plasticity is blocked after presynaptic proteasome perturbation. Proteasome inhibition potentiates release under baseline conditions but
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