- CITATIONS: 1
|Application ||WB, IHC-P, E|
|Other Accession||Q9JMA1, Q0IIF7, NP_005142|
|Calculated MW||56069 Da|
|Antigen Region||1-30 aa|
|Other Names||Ubiquitin carboxyl-terminal hydrolase 14, Deubiquitinating enzyme 14, Ubiquitin thioesterase 14, Ubiquitin-specific-processing protease 14, USP14, TGT|
|Target/Specificity||This USP14 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human USP14.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||USP14 Antibody (N-term) 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|
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.
Puente, X.S., et al., Nat. Rev. Genet. 4(7):544-558 (2003). D'Andrea, A., et al., Crit. Rev. Biochem. Mol. Biol. 33(5):337-352 (1998). Deshpande, K.L., et al., Arch. Biochem. Biophys. 326(1):1-7 (1996).
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