Recombinant Human USP13 protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human USP13 protein is a Human Full Length protein, in the 1 to 863 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
ISOT3, USP13, Ubiquitin carboxyl-terminal hydrolase 13, Deubiquitinating enzyme 13, Isopeptidase T-3, Ubiquitin thioesterase 13, Ubiquitin-specific-processing protease 13, ISOT-3
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human USP13 protein (AB160279)
ab160279 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
USP13 participates in maintaining protein homeostasis and modulates protein stability. It forms complexes with specific substrate proteins to execute its function efficiently. Through deubiquitinating actions it regulates the levels of proteins involved in cellular signaling apoptosis and cell cycle control. The enzyme influences processes that are important for cell survival and adaptation to stress.
Pathways
USP13 plays significant roles within the ubiquitin-proteasome system and the mitophagy pathway. It cooperates with proteins like Parkin in mitochondrial quality control by stabilizing target proteins necessary for mitophagy. Through interaction with key players in these pathways USP13 ensures the maintenance of cellular health and proper degradation of damaged or misfolded proteins.
Specifications
Form
Liquid
General info
Function
Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy, endoplasmic reticulum-associated degradation (ERAD), cell cycle progression or DNA damage response (PubMed : 21571647, PubMed : 32772043, PubMed : 33592542). Component of a regulatory loop that controls autophagy and p53/TP53 levels : mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Alternatively, forms with NEDD4 a deubiquitination complex, which subsequently stabilizes VPS34 to promote autophagy (PubMed : 32101753). Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity : binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Regulates the cell cycle progression by stabilizing cell cycle proteins such as SKP2 and AURKB (PubMed : 32772043). In addition, plays an important role in maintaining genomic stability and in DNA replication checkpoint activation via regulation of RAP80 and TOPBP1 (PubMed : 33592542). Deubiquitinates the multifunctional protein HMGB1 and subsequently drives its nucleocytoplasmic localization and its secretion (PubMed : 36585612). Positively regulates type I and type II interferon signalings by deubiquitinating STAT1 but negatively regulates antiviral response by deubiquitinating STING1 (PubMed : 23940278, PubMed : 28534493).
Sequence similarities
Belongs to the peptidase C19 family.
Post-translational modifications
Phosphorylated by AURKB at Ser-114; leading to stabilization of cell cycle proteins such as SKP2 and AURKB, but not MCL1.
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com