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Pifithrin-mu

p53抑制剂

产品号 #(选择产品)

产品号 #72802_C

p53抑制剂

总览

Pifithrin-mu(PFT-µ)是p53介导的细胞凋亡抑制剂,可阻止p53在线粒体表面与Bcl-xL和Bcl-2结合,而不影响p53的转录活化的功能(Strom et al.)。在体外实验中,PFT-µ可与p53 (Kd = 0.82 mM)和Bcl-xL (Kd = 0.80 mM)结合(Hagn et al.)。

维持和自我更新
·与Rho 相关卷曲螺旋蛋白激酶(ROCK)抑制剂Y-27632一起使用,可提高细胞冻存复苏后的存活率(Xu et al.)。
·抑制人胚胎干细胞中由DNA损伤引起的凋亡(Qin et al.)。

细胞类型
多能干细胞
 
种属
人,小鼠,非人灵长类,其它细胞系,大鼠
 
应用
培养
 
研究领域
干细胞生物学
 
CAS 编号
64984-31-2
 
化学式
C₈H₇NO₂S
 
纯度
≥98%
 
通路
p53
 
靶点
p53
 

产品说明书及文档

请在《产品说明书》中查找相关支持信息和使用说明,或浏览下方更多实验方案。

Document Type
Product Name
Catalog #
Lot #
Language
Product Name
Pifithrin-mu
Catalog #
72802
Lot #
All
Language
English
Document Type
Safety Data Sheet
Product Name
Pifithrin-mu
Catalog #
72802
Lot #
All
Language
English

应用领域

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相关材料与文献

技术资料 (3)

文献 (5)

BclxL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain. Hagn F et al. The Journal of biological chemistry 2010 JAN

Abstract

p53 can induce apoptosis through mitochondrial membrane permeabilization by interaction of its DNA binding region with the anti-apoptotic proteins BclxL and Bcl2. However, little is known about the action of p53 at the mitochondria in molecular detail. By using NMR spectroscopy and fluorescence polarization we characterized the binding of wild-type and mutant p53 DNA binding domains to BclxL and show that the wild-type p53 DNA binding domain leads to structural changes in the BH3 binding region of BclxL, whereas mutants fail to induce such effects due to reduced affinity. This was probed by induced chemical shift and residual dipolar coupling data. These data imply that p53 partly achieves its pro-apoptotic function at the mitochondria by facilitating interaction between BclxL and BH3-only proteins in an allosteric mode of action. Furthermore, we characterize for the first time the binding behavior of Pifithrin-mu, a specific small molecule inhibitor of the p53-BclxL interaction, and present a structural model of the protein-ligand complex. A rather unusual behavior is revealed whereby Pifithrin-mu binds to both sides of the protein-protein complex. These data should facilitate the rational design of more potent specific BclxL-p53 inhibitors.
Enhancement of cell recovery for dissociated human embryonic stem cells after cryopreservation. Xu X et al. Biotechnology progress 2010

Abstract

Due to widespread applications of human embryonic stem (hES) cells, it is essential to establish effective protocols for cryopreservation and subsequent culture of hES cells to improve cell recovery. We have developed a new protocol for cryopreservation of dissociated hES cells and subsequent culture. We examined the effects of new formula of freezing solution containing 7.5% dimethylsulfoxide (DMSO) (v/v %) and 2.5% polyethylene glycol (PEG) (w/v %) on cell survival and recovery of hES cells after cryopreservation, and further investigated the role of the combination of Rho-associated kinase (ROCK) inhibitor and p53 inhibitor on cell recovery during the subsequent culture. Compared with the conventional slow-freezing method which uses 10% DMSO as a freezing solution and then cultured in the presence of ROCK inhibitor at the first day of culture, we found out that hES cell recovery was significantly enhanced by around 30 % (P textless 0.05) by the new freezing solution. Moreover, at the first day of post-thaw culture, the presence of 10 microM ROCK inhibitor (Y-27632) and 1 microM pifithrin-mu together further significantly improved cell recovery by around 20% (P textless 0.05) either for feeder-dependent or feeder-independent culture. hES cells remained their undifferentiated status after using this novel protocol for cryopreservation and subsequent culture. Furthermore, this protocol is a scalable cryopreservation method for handling large quantities of hES cells.
A small molecule inhibitor of inducible heat shock protein 70. Leu JI-J et al. Molecular cell 2009 OCT

Abstract

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 called 2-phenylethynesulfonamide (PES) interacts selectively with HSP70 and leads to a disruption of the association between HSP70 and several of its cochaperones and substrate proteins. Treatment of cultured tumor cells with PES promotes cell death that is associated with protein aggregation, impaired autophagy, and inhibition of lysosomal function. Moreover, this small molecule is able to suppress tumor development and enhance survival in a mouse model of Myc-induced lymphomagenesis. The data demonstrate that PES disrupts actions of HSP70 in multiple cell signaling pathways, offering an opportunity to better understand the diverse functions of this molecular chaperone and also to aid in the development of new cancer therapies.

更多信息

更多信息
种属 Human, Mouse, Non-Human Primate, Other, Rat
Cas Number 64984-31-2
Chemical Formula C₈H₇NO₂S
纯度 ≥ 98%
Target p53
Pathway p53
质量保证:

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