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Recombinant Mouse Usp7 Protein, Myc/DDK-tagged

Cat.No. : Usp7-6882M
Product Overview : Purified recombinant protein of mouse full-length ubiquitin specific peptidase 7 (Usp7), with C-terminal MYC/DDK tag, expressed in HEK293T cells.
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Description : Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Deubiquitinates KMT2E preventing KMT2E proteasomal-mediated degradation. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions. Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex. Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo. Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function. Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins. Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells. Deubiquitinates SIRT7, inhibiting SIRT7 histone deacetylase activity and regulating gluconeogenesis.
Source : HEK293T
Species : Mouse
Tag : Myc/DDK
Molecular Mass : 128.9 kDa
Purity : > 80% as determined by SDS-PAGE and Coomassie blue staining
Stability : Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Storage : Store at -80 centigrade after receiving vials.
Concentration : >50 μg/mL as determined by microplate BCA method
Storage Buffer : 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol.
Gene Name : Usp7 ubiquitin specific peptidase 7 [ Mus musculus (house mouse) ]
Official Symbol : Usp7
Synonyms : USP7; ubiquitin specific peptidase 7; ubiquitin carboxyl-terminal hydrolase 7; mHAUSP; ubiquitin thioesterase 7; deubiquitinating enzyme 7; ubiquitin thiolesterase 7; ubiquitin specific protease 7; ubiquitin-specific-processing protease 7; herpesvirus-associated ubiquitin-specific protease; Hausp; C80752; AA409944; AA617399; AU019296; AW548146; 2210010O09Rik
Gene ID : 252870
mRNA Refseq : NM_001003918
Protein Refseq : NP_001003918
UniProt ID : Q6A4J8

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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