Anti-Human USP20 Antibody Pair

Product Description: Ubiquitin specific peptidase 20 (USP20) is a cysteine protease deubiquitinating enzyme encoded by the USP20 gene located on chromosome 9q34.11. It is a 914-amino acid protein containing conserved cysteine and histidine residues at its catalytic site and has four domains: an N-terminal zinc finger ubiquitin-binding domain, a catalytic domain, and two C-terminal DUSP domains. USP20 functions by cleaving ubiquitin molecules from substrate proteins, thereby regulating protein stability and recycling. It is known to deubiquitinate proteins such as thyronine deiodinase type 2, hypoxia-inducible factor 1alpha, and beta2-adrenergic receptor, impacting various cellular processes including proliferation and migration. Dysregulation of USP20 is implicated in diseases such as cancer, particularly in tumorigenesis where it stabilizes tumorigenic or antitumor proteins, as well as in inflammation-related conditions like atherosclerosis and cancer through modulation of NF-kappaB signaling. Its alteration has been linked to colorectal cancer metastasis, antiviral immunity, metabolic disorders, and neurological diseases, highlighting USP20's potential as a therapeutic target. Protein 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-alpha 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) [The Uniprot Consortium]