Mouse Anti-USP7 Recombinant Antibody (CBT664) (V2LY-0625-LY3361)

Mouse

Human

CBT664

IgG

WB, ELISA

Purified recombinant fragment of human HAUSP expressed in E. Coli.

Mouse

Human

IgG

Monoclonal Antibody

Supernatant

BSA, Glycerol

Sodium azide

Batch dependent

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Hydrolase that deubiquitinates target proteins such as FOXO4, KAT5, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:25865756, PubMed:26678539, PubMed:28655758).

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 regulation, 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).

Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation (PubMed:26678539).

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).

Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111).

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 (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 regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222).

Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins (PubMed:27123980).

Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells (PubMed:21258371).

Deubiquitinates SIRT7, inhibiting SIRT7 histone deacetylase activity and regulating gluconeogenesis (PubMed:28655758).

(Microbial infection) Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection.

Histone H2B conserved C-terminal lysine deubiquitination Source: UniProtKB
Maintenance of DNA methylation Source: UniProtKB
Monoubiquitinated protein deubiquitination Source: MGI
Negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
Negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Positive regulation of DNA demethylation Source: UniProtKB
Protein deubiquitination Source: UniProtKB
Protein K63-linked deubiquitination Source: UniProtKB
Protein stabilization Source: UniProtKB
Protein ubiquitination Source: Reactome
Regulation of circadian rhythm Source: UniProtKB
Regulation of DNA-binding transcription factor activity Source: UniProtKB
Regulation of gluconeogenesis Source: UniProtKB
Regulation of protein stability Source: UniProtKB
Regulation of retrograde transport, endosome to Golgi Source: UniProtKB
Regulation of signal transduction by p53 class mediator Source: Reactome
Regulation of telomere capping Source: BHF-UCL
Rhythmic process Source: UniProtKB-KW
Transcription-coupled nucleotide-excision repair Source: UniProtKB
Ubiquitin-dependent protein catabolic process Source: InterPro

Nucleus; PML body; Cytoplasm; Chromosome. Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies.

Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated.1 Publication
Isoform 1: Polyneddylated. Isoform 2: Not Polyneddylated.
Isoform 1 and isoform 2: Not sumoylated.
Isoform 1 and isoform 2: Polyubiquitinated by herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110; leading to its subsequent proteasomal degradation. Isoform 1: Ubiquitinated at Lys-869.