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STUB1/CHIP His Tag Protein, Human
品牌： UA BIOSCIENCE
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对比
咨询分子量：
33-43kDa (Reducing)
纯度：
＞95% by SDS-PAGE,> 90% by HPLC
产品介绍
产品介绍
产品信息
荧光素标记
Unconjugated
氨基酸序列
Ser23-Tyr303 with His Tag at the N-Terminus
分子量
33-43kDa (Reducing)
纯度
＞95% by SDS-PAGE,> 90% by HPLC
性状
Liquid
缓冲体系
50mM Tris, 150mM NaCl, pH7.5, 1mM DTT, 10%Glycerol
种属
Human
电泳JSON
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2μg (R: reducing condition, N: non-reducing condition).
"}]背景
别名
CHIP, PP1131, STUB1, E3 ubiquitin-protein ligase CHIP, Antigen NY-CO-7
背景
STUB1 (STIP1 Homology and U-Box Containing Protein 1), commonly known as CHIP (C-terminus of Hsc70 Interacting Protein), is a crucial dual-function protein in cellular proteostasis. It serves as both a co-chaperone and an E3 ubiquitin ligase. As a co-chaperone, it binds to the molecular chaperones Hsp70/Hsc70 and Hsp90 via its N-terminal tetratricopeptide repeat (TPR) domain, assisting in client protein folding and stabilization. Its central role lies in its C-terminal U-box domain, which confers E3 ubiquitin ligase activity. This unique combination allows CHIP to ubiquitinate misfolded or damaged client proteins that are delivered by the chaperones, thereby targeting them for proteasomal degradation. It is a central component of the Protein Quality Control (PQC) system, clearing toxic protein aggregates and maintaining proteome integrity.Dysregulation of CHIP function is linked to various human diseases. Loss-of-function mutations or reduced expression are associated with neurodegenerative disorders (e.g., spinocerebellar ataxia, Alzheimer's, Parkinson's) due to defective clearance of pathogenic proteins like tau and α-synuclein. Conversely, its role in degrading oncogenic clients (e.g., HER2, c-Myc) positions it as a potential tumor suppressor in certain cancers. It also plays key roles in aging, cardiac function, and immune responses, making it a significant therapeutic target.
制备和贮存
保存方式
Stable for 12 months upon stored at -80℃ from the date of receipt.
And avoid repeated freeze-thaws cycles.
文献
文献
1. Ballinger, C.A., et al. (1999). Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Molecular and Cellular Biology, 19(6), 4535-4545.
2. Jiang, J., et al. (2001). CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. Journal of Biological Chemistry, 276(46), 42938-42944.
数据库链接
Accession
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