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ELISA USP7 Antibody, HRP

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Quantity :50µg Clone Number: Aliases:Deubiquitinating enzyme 7 antibody; HAUSP antibody; Herpes virus associated ubiquitin specific protease antibody; Herpesvirus-associated ubiquitin-specific protease antibody; TEF 1 antibody; tef-1 antibody; TEF1 antibody; Ubiquitin carboxyl terminal hydrolase 7 antibody; Ubiquitin carboxyl-terminal hydrolase 7 antibody; Ubiquitin specific peptidase 7 (herpes virus associated) antibody; Ubiquitin specific peptidase 7 antibody; Ubiquitin specific peptidase 7 herpes virus associated antibody; Ubiquitin specific processing protease 7 antibody; Ubiquitin specific protease 7 (herpes virus associated) antibody; Ubiquitin specific protease 7 antibody; Ubiquitin specific protease 7 herpes virus associated antibody; Ubiquitin thioesterase 7 antibody; Ubiquitin thiolesterase 7 antibody; Ubiquitin-specific-processing protease 7 antibody; UBP 7 antibody; UBP-7 antibody; UBP7 antibody; UBP7_ antibody; USP 7 antibody; usp-7 antibody; Usp7 antibody; VMW110-ASSOCIATED PROTEIN, 135-KD antibody Product Type:Polyclonal Antibody Immunogen Species:Homo sapiens () UniProt ID:Q93009 Immunogen:Recombinant Ubiquitin carboxyl-terminal hydrolase 7 protein (302-394AA) Raised in:Rabbit Reactivity: Tested Applications:ELISA Background:Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148). 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 (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regµLation, cell growth repression and apoptosis (PubMed:25283148). 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 (PubMed:11923872). Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity (PubMed:16964248). 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 (PubMed:18716620). 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 (PubMed:22466611, PubMed:22466612). 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 (PubMed:21745816, PubMed:22411829). Acts as a chromatin regµLator via its association with the Polycomb group (PcG) mµLtiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (PubMed:20601937). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:20601937). Exhibits a preference towards \\\'Lys-48\\\'-linked ubiquitin chains (PubMed:22689415). Increases regµLatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). Clonality:Polyclonal Isotype:IgG Purification Method:>95%, Protein G purified Conjµgate:HRP Buffer:Preservative: 0.03% Proclin 300 Constituents: 50% Glycerol, 0.01M PBS, pH 7.4 Form:Liquid Stroage:Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Target Names:USP7 Research Areas:Epigenetics and Nuclear Signaling; Cancer; Cell biology; Microbiology

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Hieff NGS

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Garantie satisfait ou remboursé de 30 jours
Expédition : 2-3 jours ouvrables


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