P0122
Pifithrin-μ
≥97% (HPLC), solid
别名:
2-苯乙炔磺胺, PFTμ
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关于此项目
经验公式（希尔记法）:
C8H7NO2S
化学文摘社编号:
分子量:
181.21
NACRES:
NA.77
PubChem Substance ID:
UNSPSC Code:
12352200
MDL number:
产品名称
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
相关类别
Application
菲丝菌素-μ 已用于:
- 处理小胶质细胞系以分析其对M1样和M2样表型的神经保护作用
- 作为热休克蛋白（HSP）-70抑制剂用于处理转染的Marc-145细胞
- 抑制热休克相关蛋白70（heat shock cognate，Hsc70）以阐明小鼠胚胎干细胞的热休克伴侣蛋白
Biochem/physiol Actions
Pifithrin- μ是p53结合和抗凋亡的抑制剂，其可直接抑制p53与线粒体以及Bcl-xL和Bcl-2蛋白的结合。
Pifithrin- μ是p53结合和抗凋亡的抑制剂，其可直接抑制p53与线粒体以及Bcl-xL和Bcl-2蛋白的结合。PFT μ可从致死γ -辐射诱导的细胞死亡中解救细胞。由于pifithrin- μ仅关闭p53-线粒体途径而不影响p53的转录功能，所以它比pifithrin-α 具有更优的性能。
在缺氧缺血（HI）诱发的新生儿脑病的临床前模型中，菲丝菌素μ（PFT-μ）具有防止细胞死亡的神经保护能力。它通过抑制分子伴侣热休克蛋白（HSP）-70与其底物的相互作用来抑制核因子ΙB（NF-ΙB）通路。
signalword
Warning
hcodes
Hazard Classifications
Acute Tox. 4 Oral
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
Ramon D Jones et al.
Molecular biology of the cell, 31(3), 221-233 (2019-12-12)
Protein misfolding is a recurring phenomenon that cells must manage; otherwise misfolded proteins can aggregate and become toxic should they persist. To counter this burden, cells have evolved protein quality control (PQC) mechanisms that manage misfolded proteins. Two classes of
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)
Fernando Mérida et al.
International journal of nanomedicine, 15, 419-432 (2020-02-06)
Magnetic Fluid Hyperthermia (MFH) is a promising adjuvant for chemotherapy, potentiating the action of anticancer agents. However, drug delivery to cancer cells must be optimized to improve the overall therapeutic effect of drug/MFH combination treatments. The aim of this work
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
Christophe Bignon et al.
Biomolecules, 9(1) (2018-12-29)
In this paper we review our recent findings on the different interaction mechanisms of the C-terminal domain of the nucleoprotein (N) of measles virus (MeV) NTAIL, a model viral intrinsically disordered protein (IDP), with two of its known binding partners
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