Ubiquitin Antibody (5B9-B3) Summary
| Immunogen |
Native bovine ubiquitin, conjugated to KLH
|
| Localization |
Cytoplasm, Nucleus
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| Specificity |
Detects approx 10kDa.
|
| Isotype |
IgG2a Kappa
|
| Clonality |
Monoclonal
|
| Host |
Mouse
|
| Gene |
RPS27A
|
| Purity |
Protein G purified
|
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|
Applications/Dilutions
| Dilutions |
|
| Application Notes |
1 ug/ml of Ubiquitin Antibody was sufficient for detection of ubiquitin in 10 ug of Heal Lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary Antibody.
|
Reactivity Notes
Based on homology, It is predicted to detect Human, Mouse and Rat.
Packaging, Storage & Formulations
| Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
|
| Buffer |
PBS (pH 7.4) and 50% Glycerol
|
| Preservative |
0.09% Sodium Azide
|
| Concentration |
1 mg/ml
|
| Purity |
Protein G purified
|
Alternate Names for Ubiquitin Antibody (5B9-B3)
- RPS27A
- UBA52
- UBB ubiquitin B
- UBB
- UBC
- Ubiquitin
Background
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 8.5kDa. 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 an 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 inhibitory proteins, such as IkappaBalpha and p27 (5).