Ubiquitin specific peptidase 14 (USP14) is a 494 amino acid protein containing a 45kDa catalytic domain at its amino-terminus. Its ubiquitin-like (Ubl) domain associates with 19S regulatory particle (RP) 26S proteasome. This binding activates the deubiquitinating activity of the protein. USP14 is part of the ubiquitin-specific processing (UBP) family of proteases.
Immunogen
USP14 (NP_005142, 395 a.a. ~ 494 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Ubiquitin specific peptidase 14 (USP14) releases ubiquitin from the proteasome-targeted ubiquitinated proteins resulting in regeneration of ubiquitin at the proteasome. It is involved in the degradation of chemokine receptor CXCR4. Under endoplasmic reticulum (ER) stress, USp14 binds to ER stress receptor, which is involved in unfolded protein response (UPR), a mechanism to control the accumulation of unfolded proteins within the ER lumen. Its overexpression leads to ER-associated degradation (ERAD) pathway inhibition.
Physical form
Solution in phosphate buffered saline, pH 7.4
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The 26S proteasome is the ATP-dependent protease responsible for regulating the proteome of eukaryotic cells through degradation of mainly ubiquitin-tagged substrates. In order to understand how proteasome responds to ubiquitin signal, we resolved an ensemble of cryo-EM structures of proteasome
USP14 is a cysteine protease deubiquitinase associated with the proteasome and plays important catalytic and allosteric roles in proteasomal degradation. USP14 inhibition has been considered a therapeutic strategy for accelerating degradation of aggregation-prone proteins in neurodegenerative diseases and for inhibiting
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