|Application ||WB, IHC-P, E|
|Other Accession||A7Z056, NP_006667|
|Calculated MW||102003 Da|
|Antigen Region||814-844 aa|
|Other Names||Ubiquitin carboxyl-terminal hydrolase 20, Deubiquitinating enzyme 20, Ubiquitin thioesterase 20, Ubiquitin-specific-processing protease 20, VHL-interacting deubiquitinating enzyme 2, hVDU2, USP20, KIAA1003, LSFR3A, VDU2|
|Target/Specificity||This USP20 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 814-844 amino acids from the C-terminal region of human USP20.|
|Precautions||USP20 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||KIAA1003, LSFR3A, VDU2|
|Function||Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination 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, possibly 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. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.|
|Cellular Location||Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=According to PubMed:12865408, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear|
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Provided below are standard protocols that you may find useful for product applications.
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.
Nagase, T., et al., DNA Res. 6(1):63-70 (1999).
Gilley, J., et al., Hum. Mol. Genet. 8(7):1313-1320 (1999).
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