| References |
| Formulation |
protein G-purified IgG at a concentration of 1 mg/ml in PBS, pH 7.4, containing 50% glycerol and 0.09% sodium azide |
| Stability |
1 year |
| Storage |
-20°C |
| Shipping |
Wet ice
in continental US; may vary elsewhere
|
| Specificity |
| Human Ubiquitin |
+ |
| Murine Ubiquitin |
+ |
| Rat Ubiquitin |
+ |
| Bovine Ubiquitin |
+ |
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|
Background Reading
Yang, M., Omura, S., Bonifacino, J.S., et al. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J Exp Med 187(6) 835-846 (1998).
. Ubiquitin Proteasome Pathway. (2009).
Bonifacino, J.S., and Weissman, A.M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol 14 19-57 (1998).
Wilkinson, K.D. Roles of ubiquitinylation in proteolysis and cellular regulation. Annu Rev Nutr 15 161-189 (1995).
Chen, Z.J., Parent, L., and Maniatis, T. Site-specific phosphorylation of IkBa by a novel ubiquitination-dependent protein kinase activity. Cell 84 853-862 (1996).
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Hide all but first 3
| Size |
Global Purchasing |
| 50 µg |
|
| 200 µg |
|
Description
Antigen:
native bovine ubiquitin conjugated to KLH
·
Clone designation:
6C11-B3
·
Host:
Mouse
·
Isotype:
IgG2aκ
·
Application(s):
WB and ELISA
·
Ubiquitin is a small protein that occurs in all eukaryotic cells. The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about 8.5 kDa. Key features include its C-terminal tail and the 7 Lys residues. It is highly conserved among eukaryotic species: human and yeast ubiquitin share 96% sequence identity.1 The main function of ubiquitin is to clear abnormal, foreign and improperly folded proteins by targeting them for degradation by the 26S proteosome.2 Ubiquitination represents an essential cellular process affected by a multi-enzyme cascade involving classes of enzymes known as ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s or Ubcs) and ubiquitin-protein ligases (E3s). Ubiquitin is activated in a two-step reaction by an E1 ubiquitin-activating enzyme in a process requiring ATP as an energy source. The initial step involves production of a ubiquitin-adenylate intermediate. The second step transfers ubiquitin to the E1 active site cysteine residue, with release of AMP. This step results in a thioester linkage between the C-terminal carboxyl group of ubiquitin and the E1 cysteine sulfhydryl group. The third step is a transfer of ubiquitin from E1 to the active site cysteine of a ubiquitin-conjugating enzyme E2 via a trans(thio)esterification reaction. And the final step of the ubiquitylation cascade creates an isopeptide bond between a lysine of the target protein and the C-terminal glycine of ubiquitin. In general, this step requires the activity of one of the hundreds of E3 ubiquitin-protein ligases (often termed simply ubiquitin ligase). E3 enzymes function as the substrate recognition modules of the system and are capable of interaction with both E2 and substrate.2,3 Ubiquitination also participates in the internalization and degradation of plasma membrane proteins such as some of the TCR subunits while still ER-membrane associated.4 Ubiquitin also plays a role in regulating signal transduction cascades through the elimination inhibitor proteins, such as IκBα and p27.5
1
Wilkinson, K.D. Roles of ubiquitinylation in proteolysis and cellular regulation. Annu Rev Nutr 15 161-189 (1995).
2
Bonifacino, J.S., and Weissman, A.M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol 14 19-57 (1998).
3
. Ubiquitin Proteasome Pathway. (2009).
4
Yang, M., Omura, S., Bonifacino, J.S., et al. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J Exp Med 187(6) 835-846 (1998).
5
Chen, Z.J., Parent, L., and Maniatis, T. Site-specific phosphorylation of IkBa by a novel ubiquitination-dependent protein kinase activity. Cell 84 853-862 (1996).
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