Recombinant Human CHIP/STUB1 Protein Summary
| Description |
A recombinant protein corresponding to STUB1.
Amino Acid Sequence: MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV EDY |
| Preparation Method |
E.coli
|
| Protein/Peptide Type |
Recombinant Protein
|
| Gene |
STUB1
|
| Purity |
>90%, by SDS-PAGE
|
| Endotoxin Note |
< 1.0 EU per 1 microgram of protein (determined by LAL method)
|
Applications/Dilutions
| Theoretical MW |
34.8 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Reactivity Notes
Human
Packaging, Storage & Formulations
| Storage |
Store at -80C. Avoid freeze-thaw cycles.
|
| Buffer |
20 mM Tris-HCl buffer (pH 7.5) containing 5 mM DTT, 10% glycerol
|
| Preservative |
No Preservative
|
| Concentration |
1 mg/ml
|
| Purity |
>90%, by SDS-PAGE
|
Notes
The purity of this protein is > 90% by SDS-PAGE. Molecular weight is 34.8 kDa (303 aa), confirmed by MALDI-TOF.
Alternate Names for Recombinant Human CHIP/STUB1 Protein
- Antigen NY-CO-7
- Carboxy terminus of Hsp70-interacting protein
- CHIP
- 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
Background
CHIP, also known as STUB1, is a cytoplasmic protein whose amino acid sequence is highly conserved across species. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain, whereas its U-box domain contains its E3 ubiquitin ligase activity. Its interaction with these molecular chaperones results in client substrate ubiquitylation and degradation by the proteasome. Thus, CHIP acts to tilt the folding-refolding machinery toward the degradative pathway, and it serves as a link between the two. Recombinant human CHIP protein was expressed in E.coli and purified by using conventional chromatography techniques.
