|Application ||WB, FC, E|
|Calculated MW||158658 Da|
|Antigen Region||1280-1310 aa|
|Other Names||Ubiquitin carboxyl-terminal hydrolase 6, Deubiquitinating enzyme 6, Proto-oncogene TRE-2, Ubiquitin thioesterase 6, Ubiquitin-specific-processing protease 6, USP6, HRP1, TRE2|
|Target/Specificity||This USP6 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1280-1310 amino acids from the C-terminal region of human USP6.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|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||USP6 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Deubiquitinase with an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Catalyzes its own deubiquitination. In vitro, isoform 2, but not isoform 3, shows deubiquitinating activity. Promotes plasma membrane localization of ARF6 and selectively regulates ARF6- dependent endocytic protein trafficking. Is able to initiate tumorigenesis by inducing the production of matrix metalloproteinases following NF-kappa-B activation.|
|Cellular Location||Cell membrane. Cytoplasm. Endosome. Note=Localizes to the plasma membrane and to filamentous structures within the cell corresponding to ARF6 regulated tubular endosomes. Activation of RAC1 and CDC42 can direct the relocalization of USP6 to the plasma membrane in a manner that depends on the integrity of the actin cytoskeleton|
|Tissue Location||Testis specific. Expressed in various cancer cell lines.|
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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.
Paulding, C.A., et al., Proc. Natl. Acad. Sci. U.S.A. 100(5):2507-2511 (2003). Papa, F.R., et al., Nature 366(6453):313-319 (1993). Nakamura, T., et al., Oncogene 7(4):733-741 (1992).
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