Ubiquitin (E4I2J) Rabbit mAb (Biotinylated) #91112
- WB
Supporting Data
| REACTIVITY | All |
| SENSITIVITY | Endogenous |
| MW (kDa) | 9-300 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- All-All Species Expected
Product Information
Product Description
| MW (kDa) | 9-300 |
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Ubiquitin (E4I2J) Rabbit mAb (Biotinylated) recognizes endogenous levels of free ubiquitin and polyubiquitinated proteins. This antibody is able to detect free ubiquitin, linear polyubiquitin (M1-linked), and homotypic polyubiquitin chains consisting of K6, K11, K27, K29, K33, K48, and K63 linkages.
Species Reactivity:
All Species Expected
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly35 of human ubiquitin protein.
Background
Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7).
- Ciechanover, A. (1998) EMBO J 17, 7151-60.
- Hochstrasser, M. (2000) Nat Cell Biol 2, E153-7.
- Hochstrasser, M. (2000) Science 289, 563-4.
- Bernardi, R. et al. (2000) Oncogene 19, 2447-54.
- Aberle, H. et al. (1997) EMBO J 16, 3797-804.
- Salomoni, P. and Pandolfi, P.P. (2002) Nat Cell Biol 4, E152-3.
- Jesenberger, V. and Jentsch, S. (2002) Nat Rev Mol Cell Biol 3, 112-21.
Limited Uses
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