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I1911

Sigma-Aldrich

IU1

≥98% (HPLC)

Sinônimo(s):

1-[1-(4-Fluoro-phenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-pyrrolidin-1-yl-ethanone

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R$ 1.091,00
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5 MG
R$ 1.091,00
25 MG
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About This Item

Fórmula empírica (Notação de Hill):
C18H21FN2O
Número CAS:
314245-33-5
Peso molecular:
300.37
Número MDL:
MFCD01917473
Código UNSPSC:
12352200
ID de substância PubChem:
329815361
NACRES:
NA.77

R$ 1.091,00

Previsão de entrega em12 de maio de 2025

Solicite uma grande encomenda

Nível de qualidade

100

Ensaio

≥98% (HPLC)

Formulário

powder

cor

off-white to light brown

solubilidade

DMSO: >10 mg/mL

temperatura de armazenamento

2-8°C

cadeia de caracteres SMILES

FC1=CC=C(N2C(C)=CC(C(CN3CCCC3)=O)=C2C)C=C1

InChI

1S/C18H21FN2O/c1-13-11-17(18(22)12-20-9-3-4-10-20)14(2)21(13)16-7-5-15(19)6-8-16/h5-8,11H,3-4,9-10,12H2,1-2H3

chave InChI

JUWDSDKJBMFLHE-UHFFFAOYSA-N

Aplicação

IU1 has been used for the inhibition of Ubiquitin Specific Peptidase 14 (USP14) in human neuroblastoma cells (SH-SY5Y)[1] and in ubiquitin-rhodamine hydrolysis plate assay.[2]

Ações bioquímicas/fisiológicas

IU1 is an inhibitor of USP14, a deubiquitinating enzyme associated with the proteasome.
IU1 is an inhibitor of USP14, a deubiquitinating enzyme associated with the proteasome. The proteasome mediates the cellular degradation of oxidized, damaged and misfolded proteins which, if not removed, accumulate and become toxic to cells. Proteins targeted for proteasomal degradation are first ubiquitinated, with longer length ubiquitin chains interacting more strongly with the proteasome. Deubiquitinating enzymes (DUBs) such as USP14 interfere with the degradation process. IU1 inhibits USP14-mediated ubiquitin "chain-trimming" thereby enhancing substrate degradation by the proteasome. The compound may help to eliminate toxic proteins more effectively by enhancing their degradation.

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

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Certificados de análise (COA)

Lot/Batch Number
0000230419
0000289208
105M4609V
091M4602V
011M4605V

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Ningning Liu et al.
Molecular and cellular biochemistry, 431(1-2), 87-96 (2017-04-02)
Persistent activation of nuclear factor B (NF-κB) is very important in the modulation of macrophages cellular response to microbial infections. The deubiquitinase USP14, which is critical for ubiquitin-mediated proteasomal degradation of proteins, is known to be involved in cancer, neurological
USP14 inhibition corrects an in vivo model of impaired mitophagy.
Chakraborty J, et al.
EMBO Molecular Medicine, 10(11), e9014-e9014 (2018)
Liu Xu et al.
International journal of biological sciences, 16(15), 2951-2963 (2020-10-17)
Previous studies have demonstrated that the antitumor potential of IU1 (a pharmacological compound), which was mediated by selective inhibition of proteasome-associated deubiquitinase ubiquitin-specific protease 14 (USP14). However, the underlying molecular mechanisms remain elusive. It has been well established that mdm2
Inactive USP14 and inactive UCHL5 cause accumulation of distinct ubiquitinated proteins in mammalian cells.
Chadchankar J, et al.
bioRxiv, 10(11), 479758-479758 (2018)
Kapil Sareen-Khanna et al.
American journal of physiology. Renal physiology, 311(5), F1035-F1046 (2016-09-16)
Kidney cell injury may be associated with protein misfolding and induction of endoplasmic reticulum (ER) stress. Examples include complement-induced glomerular epithelial cell (GEC)/podocyte injury in membranous nephropathy and ischemia-reperfusion injury. Renal cell injury can also result from mutations in integral
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