Anti-USP42 Antibody detects endogenous levels of total USP42 protein.
Immunogen
The antiserum was produced against synthesized peptide derived from human USP42.
Immunogen Range: 251-300
Application
Anti-USP42 antibody produced in rabbit is suitable for indirect ELISA and western blot applications.
Biochem/physiol Actions
USP42 (ubiquitin specific peptidase 42) is a nuclear protein belonging to the ubiquitin-specific protease (USP) family. It is widely distributed in human tissues, especially in skeletal muscle and testis. It is involved in the regulation of ubiquitin-mediated pathways. It exerts deubiquitylating activity by cleaving ubiquitin from an ubiquitin-β-galactosidase fusion protein. It plays an important role in the regulation of p53 activity. It helps to stabilize p53 in response to stress and promotes early activation of p53.
Features and Benefits
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Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by the
The ubiquitin E3 ligase UBE3A has been widely reported to interact with the proteasome, but it is still unclear how this enzyme regulates by ubiquitination the different proteasomal subunits. The proteasome receptor DDI1 has been identified both in Drosophila photoreceptor
Biochemical and biophysical research communications, 314(1), 54-62 (2004-01-13)
We have identified and cloned 22 human cDNAs encoding novel members of the ubiquitin-specific protease (USP) family. Eighteen of the identified proteins contain all structural features characteristic of these cysteine proteinases, whereas four of them have been classified as non-peptidase
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