Isopeptidase T/USP5 Antibody Summary
| Immunogen |
Recombinant protein encompassing a sequence within the center region of human USP5. The exact sequence is proprietary.
|
| Isotype |
IgG
|
| Clonality |
Polyclonal
|
| Host |
Rabbit
|
| Gene |
USP5
|
| Purity |
Immunogen affinity purified
|
| Innovators Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase.
Learn about the Innovators Reward
|
Applications/Dilutions
| Dilutions |
|
Packaging, Storage & Formulations
| Storage |
Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles.
|
| Buffer |
0.1M Tris (pH 7.0), 0.1M Glycine and 10% Glycerol
|
| Preservative |
0.01% Thimerosal
|
| Concentration |
0.81 mg/ml
|
| Purity |
Immunogen affinity purified
|
Alternate Names for Isopeptidase T/USP5 Antibody
- Deubiquitinating enzyme 5
- EC 3.1.2.15
- EC 3.4.19.12
- Isopeptidase T
- IsoT
- ISOTubiquitin carboxyl-terminal hydrolase 5
- ubiquitin isopeptidase T
- ubiquitin specific peptidase 5 (isopeptidase T)
- ubiquitin specific protease 5 (isopeptidase T)
- ubiquitin thioesterase 5
- Ubiquitin thiolesterase 5
- ubiquitin-specific protease-5 (ubiquitin isopeptidase T)
- Ubiquitin-specific-processing protease 5
- USP5
Background
Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs),1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.