Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus)
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Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) is a Human Fragment protein, in the 2 to 914 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE, FuncS.
View Alternative Names
KIAA1003, LSFR3A, VDU2, USP20, Ubiquitin carboxyl-terminal hydrolase 20, Deubiquitinating enzyme 20, Ubiquitin thioesterase 20, Ubiquitin-specific-processing protease 20, VHL-interacting deubiquitinating enzyme 2, hVDU2
- FuncS
Supplier Data
Functional Studies - Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) (AB271783)
Functional studies analysis of ab271783 was 10 pmol/min/μg.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) (AB271783)
SDS-PAGE analysis of ab271783.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Removal of ubiquitin from protein substrates is an important function of USP20 which interacts with diverse protein complexes. USP20 modulates stability of multiple proteins by preventing their proteasomal degradation. It is involved in maintaining balance in cellular protein levels which affects cellular activities like cell cycle progression and response to stress. This activity can significantly influence the timing of protein turnover impacting how cells respond to changes.
Pathways
Deubiquitinating activities of USP20 significantly influence stress response and cellular signaling. USP20 functions within the NF-κB signaling pathway a critical mediator of immune response where it interacts with proteins such as IκBα stabilizing them by removing ubiquitin moieties. This regulatory mechanism is essential for proper NF-κB activation and immune response. Additionally USP20 plays a role in endoplasmic reticulum stress pathways by modulating GRP78 levels highlighting its involvement in protein folding and stress handling.
Specifications
Form
Liquid
General info
Function
Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis (PubMed : 27801882, PubMed : 29487085). Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination (PubMed : 26839314). Promotes cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-linked ubiquitination of STING1 leading to its stabilization (PubMed : 27801882). Plays an essential role in autophagy induction by regulating the ULK1 stability through deubiquitination of ULK1 (PubMed : 29487085). Acts as a positive regulator for NF-kappa-B activation by TNF through deubiquitinating 'Lys-48'-linked polyubiquitination of SQSTM1, leading to its increased stability (PubMed : 32354117). Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2) (PubMed : 19424180). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2 (PubMed : 19424180). This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity (PubMed : 15776016). Deubiquitinates MCL1, a pivotal member of the anti-apoptotic Bcl-2 protein family to regulate its stability (PubMed : 35063767). Within the endoplasmic reticulum, participates with USP33 in the rescue of post-translationally targeted membrane proteins that are inappropriately ubiquitinated by the cytosolic protein quality control in the cytosol (PubMed : 33792613).
Sequence similarities
Belongs to the peptidase C19 family. USP20/USP33 subfamily.
Post-translational modifications
Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.
Subcellular localisation
Cytoskeleton
Target data
Product promise
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