P0122
Pifithrin-μ
≥97% (HPLC), solid
Synonyme(s) :
2-Phenyl-ethynesulfoanide, PFT-μ
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A propos de cet article
Formule empirique (notation de Hill) :
C8H7NO2S
Numéro CAS:
Poids moléculaire :
181.21
NACRES:
NA.77
PubChem Substance ID:
UNSPSC Code:
12352200
MDL number:
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Laissez-nous vous aiderNom du produit
Pifithrin-μ, ≥97% (HPLC), solid
InChI
1S/C8H7NO2S/c9-12(10,11)7-6-8-4-2-1-3-5-8/h1-5H,(H2,9,10,11)
SMILES string
NS(=O)(=O)C#Cc1ccccc1
InChI key
ZZUZYEMRHCMVTB-UHFFFAOYSA-N
assay
≥97% (HPLC)
form
solid
storage condition
desiccated
solubility
DMSO: soluble >10 mg/mL, clear
H2O: insoluble
storage temp.
2-8°C
Quality Level
Catégories apparentées
Application
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
Biochem/physiol Actions
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.
signalword
Warning
hcodes
Hazard Classifications
Acute Tox. 4 Oral
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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Tomoya Uchimura et al.
Frontiers in endocrinology, 10, 529-529 (2019-08-21)
Medaka (Oryzias latipes) are teleost fish with a XX/XY sex determination system. Recently, it was reported that high temperature (HT) induced the masculinization of XX medaka by increasing the levels of cortisol, a major glucocorticoid produced by interrenal cells in
The anti-inflammatory effects of the small molecule pifithrin-mu on BV2 microglia
Fleiss B, et al.
Developmental Neuroscience, 37(4-5), 363-375 (2015)
Femke M Feringa et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 43(3), 347-358 (2022-12-15)
The presynaptic proteins MUNC18-1, syntaxin-1, and SNAP25 drive SNARE-mediated synaptic vesicle fusion and are also required for neuronal viability. Their absence triggers rapid, cell-autonomous, neuron-specific degeneration, unrelated to synaptic vesicle deficits. The underlying cell death pathways remain poorly understood. Here
Tomohisa Horibe et al.
Molecular cancer, 11, 59-59 (2012-08-24)
Heat-shock protein 90 (Hsp90) is vital to cell survival under conditions of stress, and binds client proteins to assist in protein stabilization, translocation of polypeptides across cell membranes, and recovery of proteins from aggregates. Therefore, Hsp90 has emerged as an
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
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