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Merck
모든 사진(1)

주요 문서

P0122

Sigma-Aldrich

Pifithrin-μ

≥97% (HPLC), solid

동의어(들):

2-Phenylethynesulfonamide, PFTμ

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About This Item

실험식(Hill 표기법):
C8H7NO2S
CAS Number:
Molecular Weight:
181.21
MDL number:
UNSPSC 코드:
12352200
PubChem Substance ID:
NACRES:
NA.77

Quality Level

분석

≥97% (HPLC)

양식

solid

저장 조건

desiccated

solubility

DMSO: soluble >10 mg/mL, clear
H2O: insoluble

저장 온도

2-8°C

SMILES string

NS(=O)(=O)C#Cc1ccccc1

InChI

1S/C8H7NO2S/c9-12(10,11)7-6-8-4-2-1-3-5-8/h1-5H,(H2,9,10,11)

InChI key

ZZUZYEMRHCMVTB-UHFFFAOYSA-N

애플리케이션

Pifithrin-μ has been used:
  • to treat microglial cell line to analyse its neuroprotective effect on M1-like and M2-like phenotype
  • as heat shock protein (HSP)-70 inhibitor, to treat transfected Marc-145 cells
  • to inhibit heat shock cognate 70 (Hsc70) to elucidate heat shock chaperones mouse embryonic stem cells

생화학적/생리학적 작용

Pifithrin-μ is an inhibitor of p53 binding and anti-apoptotic, which directly inhibits p53 binding to mitochondria as well as to Bcl-xL and Bcl-2 proteins.
Pifithrin-μ is an inhibitor of p53 binding and anti-apoptotic, which directly inhibits p53 binding to mitochondria as well as to Bcl-xL and Bcl-2 proteins. PFTμ rescues cells from lethal γ-irradiation-induced cell death. Because pifithrin-μ shuts down only the p53-mitochondrial pathway without affecting the transcriptional functions of p53, it is superior to pifithrin-α.
Pifithrin-μ(PFT-μ) has neuroprotective capabilities against cell death in a preclinical model of hypoxia-ischemia (HI)-induced neonatal encephalopathy. It inhibits nuclear factor-ΙB (NF-ΙB) pathway by inhibiting the interaction of molecular chaperone heat shock protein (HSP)-70 with its substrates.

픽토그램

Exclamation mark

신호어

Warning

유해 및 위험 성명서

예방조치 성명서

Hazard Classifications

Acute Tox. 4 Oral

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

dust mask type N95 (US), Eyeshields, Gloves


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문서 라이브러리 방문

Julia I-Ju Leu et al.
ACS chemical biology, 9(11), 2508-2516 (2014-08-26)
The stress-inducible mammalian heat shock protein 70 (HSP70) and its bacterial orthologue DnaK are highly conserved nucleotide binding molecular chaperones. They represent critical regulators of cellular proteostasis, especially during conditions of enhanced stress. Cancer cells rely on HSP70 for survival
J I-Ju Leu et al.
Molecular cell, 36(1), 15-27 (2009-10-13)
The multifunctional, stress-inducible molecular chaperone HSP70 has important roles in aiding protein folding and maintaining protein homeostasis. HSP70 expression is elevated in many cancers, contributing to tumor cell survival and resistance to therapy. We have determined that a small molecule
Determination of the interactome of non-structural protein12 from highly pathogenic porcine reproductive and respiratory syndrome virus with host cellular proteins using high throughput proteomics and identification of HSP70 as a cellular factor for virus replication
Dong S, et al.
Journal of Proteomics, 146, 58-69 (2016)
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Molecular and cellular biology, 39(9) (2019-02-13)
Delineating the mechanisms that drive hepatic injury and hepatocellular carcinoma (HCC) progression is critical for development of novel treatments for recurrent and advanced HCC but also for the development of diagnostic and preventive strategies. Heat shock protein 70 (HSP70) acts
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