Recombinant Human CHIP/STUB1 Protein, CF Summary
Contains a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||X mg/ml (X μM) in 50 mM HEPES pH 8.0, 100 mM NaCl, 10% Glycerol (v/v), 5 mM DTT|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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) (1). 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 (2,3). STUB1/CHIP is 303 amino acids (aa) in length with a predicted molecular weight of 34.8 kDa (2). Human STUB1/CHIP shares 97% aa sequence identity with the mouse ortholog but only 67% sequence identity with the rat ortholog (2). 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 (1,4,5). A central domain containing charged residues lies between the TRP and U-box domains and is thought to be necessary for TRP-dependent interactions (3). 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 (2,3,5,6). It also facilitates the ubiquitination of chaperone substrates, including nascent CFTR, phosphorylated Tau, p53, PTEN, Synuclein-alpha, and beta -APP, promoting their degradation (5,7-11). This recombinant human protein contains a C-terminal His6 tag.
- Jiang, J. et al. (2001) J. Biol. Chem. 276:42938.
- Ballinger, C.A. et al. (1999) Mol. Cell. Biol. 19:4535.
- McDonough, H. & C. Patterson (2003) Cell Stress Chaperones 8:303.
- Schulman, B.A. & Z.J. Chen (2005) Mol. Cell 20:653.
- Kumar, P. et al. (2012) J. Neurochem. 120:350.
- Connell, P. et al. (2001) Nat. Cell Biol. 3:93.
- Meacham, G.C. et al. (2001) Nat. Cell Biol. 3:100.
- Shin, Y. et al. (2005) J. Biol. Chem. 280:23727.
- Esser, C. et al. (2005) J. Biol. Chem. 280:27443.
- Kumar, P. et al. (2007) Hum. Mol. Genet. 16:848.
- Ahmed, S.F. et al. (2012) J. Biol. Chem. 287:15996.
Citations for Recombinant Human CHIP/STUB1 Protein, CF
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Citations: Showing 1 - 2
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CHIP ubiquitylates NOXA and induces its lysosomal degradation in response to DNA damage
Authors: MC Albert, K Brinkmann, W Pokrzywa, SD Günther, M Krönke, T Hoppe, H Kashkar
Cell Death & Disease, 2020;11(9):740.
Sample Types: Whole Cells
Syntaphilin Ubiquitination Regulates Mitochondrial Dynamics And Tumor Cell Movements
Authors: JH Seo, E Agarwal, KG Bryant, MC Caino, ET Kim, AV Kossenkov, HY Tang, LR Languino, DI Gabrilovic, AR Cohen, DW Speicher, DC Altieri
Cancer Res., 2018;0(0):.
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