概述货号 | K-280 |
别名 | Antigen NY-CO-7; Carboxy terminus of Hsp70-interacting protein; CHIPSTIP1 homology and U box-containing protein 1; CLL-associated antigen KW-8; E3 ubiquitin-protein ligase CHIP; EC 6.3.2.-; heat shock protein A binding protein 2 (c-terminal); HSPABP2; NY-CO-7; SDCCAG7; serologically defined colon cancer antigen 7; STIP1 homology and U-box containing protein 1; STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase; STUB1; UBOX1 |
全称 | C-terminus of Hsc70 Interacting Protein | 反应种属 | Human |
性能供应商 | R&D Systems |
Entrez Gene IDs | 10273 (Human); 56424 (Mouse) |
应用文献 |
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. The E3 Ligase CHIP Mediates p21 Degradation to Maintain Radioresistance Authors: K Biswas, S Sarkar, K Du, DL Brautigan, T Abbas, JM Larner Mol. Cancer Res, 2017;0(0):. 2017
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背景 | STIP1 Homology and U-box Containing Protein 1 (STUB1), also known as Carboxyl Terminus of Hsp70-interacting Protein (CHIP), is a cytoplasmic protein that functions as a U-box Ubiquitin ligase (E3). It is highly expressed in striated muscle and brain and has been observed at lower levels in other organs including the pancreas, lung, liver, and kidney. STUB1/CHIP is 303 amino acids (aa) in length with a predicted molecular weight of 34.8 kDa. Human STUB1/CHIP shares 97% aa sequence identity with the mouse ortholog but only 67% sequence identity with the rat ortholog. It consists of three 34 aa N-terminal tetratricopeptide repeat (TRP) domains (aa 26-127) that are responsible for protein-protein interactions and a C-terminal U-box domain (aa 226-300) that participates in ubiquitination. A central domain containing charged residues lies between the TRP and U-box domains and is thought to be necessary for TRP-dependent interactions. STUB1/CHIP participates in intracellular protein folding/refolding and degradation. It complexes with several molecular chaperone proteins, including HSP70/HSPA1A, HSC70, and HSP90, and modulates their activity. It also facilitates the ubiquitination of chaperone substrates, including nascent CFTR, phosphorylated Tau, p53, PTEN, Synuclein-alpha, and beta-APP, promoting their degradation. |
运输条件 | Dry Ice |
存放说明 | -80℃ |
参考文献 | - Adaptor Proteins
- E3 Ubiquitin Ligases
- HIF Transcription Factors
- Ubiquitin-related Molecules in the Akt Pathway
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