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USP4 Antibody

Polyclonal antibody to detect USP4 (a DUB enzyme) in human samples.
Catalog #: 6131

Product Details

Cat # +Size 6131-50
Size 50 μg
Antibody Target USP4
Alternate Name Deubiquitinating enzyme 4, Ubiquitin carboxyl-terminal hydrolase 4, Ubiquitin-specific-processing, protease 4, Ubiquitin thioesterase 4, Ubiquitous nuclear protein homolog, UNP, Unph, UNPH, Ubiquitin-specific-processing protease 4.
Host Chicken
Antibody Type Polyclonal
Isotype Chicken IgG
Immunogen Recombinant full length protein
Accession # Q13107
Gene ID 7375
Appearance Colorless liquid
Formulation 50 µg of antibody in PBS containing 10% glycerol
Purification Purified from egg yolk
Species Reactivity Human
Application Western blot
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
Handling The antibody solution should be gently mixed before use.
Storage Conditions -20 °C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not For Use in Humans.


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. USP4 was originally identified during a survey of murine genes near the Mpv20 retroviral insertion site and initially referred to as Ubiquitous Nuclear Protein (UNP). Analysis of the mouse cDNA originally identified Usp4/Unp as a proto-oncogene related to the human tre-2/tre-17/USP6 proto-oncogene. Usp4/Unp was subsequently observed to contain the conserved Cys and His boxes of the UBP family as well as DUB activity. In a study of primary lung tumor tissue, it was observed that the human homolog of Usp4, USP4/UNPH, had elevated gene expression levels in small cell tumors and adenocarcinomas of the lung, suggesting a causative role for USP4 in neoplasia. Another recent study demonstrated overexpression of USP4 in several types of human cancer and that USP4 positively contributes to cell transformation by negatively regulating p53 levels. Both murine and human USP4 have been shown to interact with the Rb family of tumor suppressor proteins, providing additional mechanistic evidence of a role for USP4 in cellular transformation.

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