|Calculated MW||56069 Da|
|Application & Usage||Western blot: Robust detection of 100 ng of recombinant protein was possible when antibody was used at a final concentration of 5 µg/mL|
|Other Names||Deubiquitinating enzyme 14, TGT, Ubiquitin carboxyl-terminal hydrolase 14, Ubiquitin-specific processing protease 14, Ubiquitin thioesterase 14, Ubiquitin-specific-processing protease 14|
|Formulation||50 µg of antibody in PBS containing 10% glycerol|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||USP14 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).|
|Cellular Location||Cytoplasm. Cell membrane; Peripheral membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action. Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. In humans, there are three proteasomal DUBs: PSMD14 (POH1/RPN11), UCH37 (UCH-L5), and Ubiquitin-Specific Protease 14, which is also known as the 60 kDa subunit of tRNA-guanine transglycosylase (USP14/TGT60 kDa). USP14 is recruited to the proteasome through its reversible association with the PSMD2 (S2/hRPN1) subunit of the 19S regulatory particle. Whereas PSMD14 appears to promote substrate degradation, USP14 is thought to antagonize substrate degradation. While the underlying mechanism for the opposing roles of these two proteasomal DUBs is still uncertain, it is thought that USP14 removes ubiquitin from substrate upon docking of the substrate with the 26S proteasome. Furthermore, USP14 trims ubiquitin residues from the distal end of the polyubiquitin chain, thus decreasing the affinity of the chain for the ubiquitin receptors of the proteasome, and allowing for enhanced substrate stability. Studies have elucidated a physiologic role for USP14 in regulating synaptic activity in mammals. Research studies have shown that targeting this activity with small molecule inhibitors has potential benefits for the treatment of neurodegenerative diseases and cancer.
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