Recombinant Human USP33 protein is a Human Fragment protein, in the 71 to 303 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). 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, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
KIAA1097, VDU1, USP33, Ubiquitin carboxyl-terminal hydrolase 33, Deubiquitinating enzyme 33, Ubiquitin thioesterase 33, Ubiquitin-specific-processing protease 33, VHL-interacting deubiquitinating enzyme 1, hVDU1
Recombinant Human USP33 protein is a Human Fragment protein, in the 71 to 303 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
Constituents: 0.58% Sodium chloride, 0.32% Tris HCl
Purified via His tag
Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2 adrenergic receptor (ADRB2). 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, leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Belongs to the peptidase C19 family. USP20/USP33 subfamily.
Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.
USP33 also known as ubiquitin-specific peptidase 33 is an important enzyme involved in the ubiquitin-proteasome system. It has a molecular mass of about 105 kDa. USP33 acts as a deubiquitinating enzyme meaning it removes ubiquitin from target proteins which stabilizes or changes their function. You find USP33 expressed in various tissues with significant levels in the brain lung and heart. Alternate names include VDU1 and a few other names reflecting variations in biological contexts.
USP33 plays roles in cellular processes like signal transduction and intracellular trafficking often as part of protein complexes. Its enzymatic activity influences the regulation of proteins tasked with moving cellular components cytoskeletal dynamics and response to hypoxia. Acting on proteins such as beta-arrestin2 USP33 influences the endocytosis and recycling of G-protein-coupled receptors (GPCRs). This role allows it to impact multiple receptor-mediated signaling pathways.
USP33 participates in critical cellular pathways including the hypoxia response and Wnt signaling. It interacts with hypoxia-inducible factor 1-alpha (HIF-1α) modifying its stability and affecting cellular response to low oxygen levels. In the Wnt signaling pathway it modulates the activity of beta-catenin through deubiquitination which is essential for cell proliferation and differentiation. These roles highlight USP33's position within wide networks of cellular regulation influencing different proteomic interactions and outcomes.
USP33 has been linked to certain cancers and neurodegenerative diseases. Its interaction with HIF-1α connects it to tumor progression as altered USP33 expression can influence cancer cell survival in hypoxic conditions. In neurodegenerative diseases like Parkinson's changes in the deubiquitination activity of USP33 may lead to protein aggregation. Its interactions with proteins such as alpha-synuclein are relevant as these proteins play a significant role in disease pathology. Understanding USP33's functions and associations offers insight into potential therapeutic targets.
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