Western blot analysis of extracts from various cell lines using USP39 Antibody.
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Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
For western blots, incubate membrane with diluted primary antibody in 5% w/v nonfat dry milk, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 263
USP39 Antibody recognizes endogenous levels of total USP39 protein.
Human, Mouse, Rat, Monkey
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val88 of human USP39 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Ubiquitin specific protease 39 (USP39) is a 65 kDa protein that plays an important role in pre-mRNA splicing, as well as mitotic spindle formation. It displays significant homology with ubiquitin C-terminal hydrolase proteins (UCHs), containing both an N-terminal zinc finger domain as well as UCH-1 and UCH-2-like domains also observed in the UCH2 family of proteins (1). However, USP39 lacks a catalytic cysteine residue found in UCHs and has been shown experimentally to lack peptidase activity (2). USP39 associates with the U4/U6-U5 tri-small nuclear ribonucleoprotein (U4/U6-U5 tri-snRNP) complex and is necessary for the formation of the mature spliceosome. Silencing of USP39 has been shown to adversely affect chromosome segregation and cytokinesis in U2OS cells, likely due to improper splicing of Aurora B and other mRNAs necessary for mitotic spindle formation and checkpoint function (2). In addition, USP39 has been found to be overexpressed in many types of cancers, and in most cases is associated with tumor progression and poor prognosis. Overexpression has been observed in pancreatic (3), prostate (4), colorectal (5,6), lung (6,7), gastric (8), and triple negative breast cancers (9), as well as melanoma (10) and hepatocellular carcinoma (11,12).
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