Recombinant Human Ubiquitin carboxyl-terminal hydrolase 7 (USP7), partial

Code CSB-YP849973HU
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Source Yeast
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Code CSB-EP849973HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP849973HU
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Source Baculovirus
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Code CSB-MP849973HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
USP7
Uniprot No.
Alternative Names
Deubiquitinating enzyme 7; HAUSP; Herpes virus associated ubiquitin specific protease; Herpesvirus-associated ubiquitin-specific protease; TEF 1; tef-1; TEF1; Ubiquitin carboxyl terminal hydrolase 7; Ubiquitin carboxyl-terminal hydrolase 7; Ubiquitin specific peptidase 7 (herpes virus associated); Ubiquitin specific peptidase 7; Ubiquitin specific peptidase 7 herpes virus associated; Ubiquitin specific processing protease 7; Ubiquitin specific protease 7 (herpes virus associated); Ubiquitin specific protease 7; Ubiquitin specific protease 7 herpes virus associated; Ubiquitin thioesterase 7; Ubiquitin thiolesterase 7; Ubiquitin-specific-processing protease 7; UBP 7; UBP-7; UBP7; UBP7_HUMAN; USP 7; usp-7; Usp7; VMW110-ASSOCIATED PROTEIN, 135-KD
Species
Homo sapiens (Human)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 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/MLL5 preventing KMT2E/MLL5 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.; (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.
Gene References into Functions
  1. Full kinetic analysis and multiple X-ray crystal structures indicate that electrostatic interactions in the distal ''switching loop'' region and local packing in the hydrophobic core mediate subtle but significant conformational changes that modulate USP7 activation. PMID: 29249604
  2. show that BRE facilitates deubiquitylation of CDC25A by recruiting ubiquitin-specific-processing protease 7 (USP7) in the presence of DNA damage PMID: 29416040
  3. High expression of USP7 is frequent in HCC tissues, which promotes tumor proliferation and invasion, and is correlated with a poor overall survival. PMID: 29574466
  4. REVIEW: USP7 plays crucial roles in diverse array of cellular and biological processes including tumour suppression, cell cycle, DNA repair, chromatin remodelling, and epigenetic regulation. PMID: 29781103
  5. USP7 depletion in APC-mutated colorectal cancer inhibits Wnt activation by restoring beta-catenin ubiquitination, drives differentiation, and suppresses xenograft tumor growth. PMID: 29045831
  6. USP7 is RNF169 interacting protein.Expression of USP7 and RNF169 positively correlated in breast cancer. PMID: 28325877
  7. protein deubiquitinase USP7 is an essential player in osteogenic differentiation of Human adipose-derived stem cells. PMID: 28807012
  8. ubiquitin-specific protease 7 (USP7) deubiquitinase targeting by vIRF-3 (in addition to previously reported USP7 binding by vIRF-1 and vIRF-4); the importance of vIRF-1 and vIRF-3 interactions with USP7 for latent PEL cell growth and viability; and the positive and negative contributions, respectively, of USP7 targeting by vIRF-1 and vIRF-3 to HHV-8 productive replication. PMID: 29343584
  9. demonstrate that both USP7 and various USP7 substrates are subjected to Lys48-mediated ubiquitin modification, consistent with increased proteasomal degradation of these proteins because of USP7 inhibition PMID: 29236775
  10. Here we study the transition between USP7 states. We provide a crystal structure of USP7(CD123) and show that catalytic domain CD and the first 3 Ubl domains Ubl123 are connected via an extended charged alpha helix. Mutational analysis is used to determine whether the charge and rigidity of this 'connector helix' are important for full USP7 activity PMID: 27183903
  11. the overexpression of USP7 might promote cell proliferation by deubiquitinating Ki-67 protein PMID: 27590858
  12. these data identify DUB3 and USP7 as factors that regulate DNA replication by controlling Geminin protein stability, and suggest that USP7 may be involved in Geminin dysregulation during breast cancer progression. PMID: 28288134
  13. Molecular mechanisms of USP7 substrate recognition and C-terminal activation have been described. PMID: 27452404
  14. USP7 promotes breast carcinogenesis by stabilizing PHF8 and upregulating cyclin A2. and the interaction between USP7 and PHF8 is augmented during DNA damage. PMID: 27183383
  15. Data suggest that SIRT7 undergoes Lys-63 polyubiquitination, later removed by USP7 to repress enzymatic activity of SIRT7; USP7 and SIRT7 regulate gluconeogenesis via expression of glucose-6-phosphatase catalytic subunit (G6PC); SIRT7 targets G6PC promoter through ELK4. (SIRT7 = sirtuin 7; USP7 = ubiquitin specific peptidase 7; G6PC = glucose-6-phosphatase catalytic subunit; ELK4 = transcription factor ELK4) PMID: 28655758
  16. USP7 is overexpressed and regulates homologous recombination repair in chronic lymphocytic leukemia cells. PMID: 28495793
  17. Findings demonstrate a crucial role of HAUSP in regulating N-Myc function in neuroblastoma in vivo and suggest that HAUSP inhibition is a potential therapy for MYCN-amplified tumors. PMID: 27618649
  18. findings suggest that Usp7 is important for MB cell proliferation and metastasis by activating Shh pathway, and is a putative therapeutic target for MBs PMID: 28137592
  19. Data suggest that HIV-1 (human immunodeficiency virus type 1) Tat gene product is stabilized by host cell deubiquitinase USP7, leading to enhanced viral production; HIV-1 in turn up-regulates the USP7 protein expression in human T-lymphocytes. PMID: 28280111
  20. modulatory role for Trip12 in the USP7-dependent DNA damage response PMID: 27800609
  21. WDR79 colocalized and interacted with USP7 in the nucleus of non-small cell lung cancer cells. This event, in turn, reduced the ubiquitination of Mdm2 and p53, thereby increasing the stability and extending the half-life of the two proteins. PMID: 28406480
  22. USP7 and MARCH7 are involved in the progression of Epithelial ovarian cancer. PMID: 27302477
  23. The present study identified USP7 and TDP-43 as the regulators of CRY1 and CRY2, underscoring the significance of the stability control process of CRY proteins for period determination in the mammalian circadian clockwork. PMID: 27123980
  24. We also uncovered the suppression of the p53 signaling pathway that mediated the activity of USP7 and LSD1. Furthermore, USP7 and LSD1 expression levels were higher in the 150 glioma patients than these levels in normal brain tissues and were correlated with glioma progression. PMID: 27632941
  25. USP7 forms a trimeric complex with MDM2 protein and suppressor of variegation 3-9 homolog 1 protein, independent of DNA, and modulates MDM2 protein-dependent suppressor of variegation 3-9 homolog 1 protein ubiquitination. PMID: 26971997
  26. stabilization of UVSSA by interaction with USP7 is essential for Transcription-coupled Nucleotide Excision Repair PMID: 27129218
  27. USP7 suppresses H2O2-induced mutagenesis involving cell-cycle-independent processes such as DNA repair. PMID: 26673319
  28. This study identified USP7 as a replisome-enriched SUMO deubiquitinase that is essential for DNA replication. PMID: 26950370
  29. We now report the identification of a novel molecular function of STIP that links USP7 to the p53-Mdm2 pathway PMID: 26460617
  30. USP7 interacts with vIRF1 in U2OS cells. PMID: 26786098
  31. HAUSP-nucleolin interaction is regulated by p53-Mdm2 complex in response to DNA damage. PMID: 26238070
  32. USP7-mediated de-ubiquitylation protects Rad18 from proteasomal degradation and is necessary for the integrity of the specialized translesion synthesis pathway PMID: 25961918
  33. USP7 allosterically regulates the conformational states of UHRF1 and affects chromatin association of UHRF1. PMID: 26299963
  34. Taken together, our results reveal that oxidative and ER stress, rather than the Mdm2-p53 axis, mainly contributes to USP7 inhibitor-mediated apoptosis in cancer cells. PMID: 26768359
  35. Data suggest that ubiquitin thioesterase 7 (HAUSP) may act as an oncogenic protein that can modulate c-MYC protein expression via transformation-transcription domain-associated protein (TRRAP). PMID: 25925205
  36. microRNA205 (miR205) may negatively regulate UPS7 protein levels through targeting its 3'untranslated region in hepatocellular carcinoma cells. PMID: 26129839
  37. These studies reveal that USP7-mediated stabilization of DNMT1 is regulated by acetylation and provide a structural basis for the design of inhibitors. PMID: 25960197
  38. Results reveal an important role of USP7 in regulating ubiquitin-dependent signaling via stabilization of RNF168. PMID: 25894431
  39. USP7 demonstrated that USP7 bound to both ASXL1-WT and ASXL1-MT PMID: 25836587
  40. In conclusion, the results of the present study indicated that the FOXO6/USP7 molecular network has an important role in the regulation of lung cancer development. PMID: 25695151
  41. The stress-responsive gene ATF3 regulates the histone acetyltransferase Tip60 stability by promoting USP7-mediated deubiquitination of Tip60. PMID: 25865756
  42. Annexin-1 regulated by HAUSP is essential for UV-induced damage response PMID: 25695607
  43. The USP7 deubiquitinating enzyme is an integral component of the MAGE-L2-TRIM27 ligase and is essential for WASH-mediated endosomal actin assembly and protein recycling. PMID: 26365382
  44. This observation suggests that HAUSP behaves as a shuttling protein in CML. PMID: 25082234
  45. USP7 directly binds ICP0 via its C-terminal UBL1-2 domains and mapped the USP7-binding site for ICP0. PMID: 26224631
  46. our findings reveal a modulatory role of USP7 in PCNA ubiquitination-mediated stress-tolerance pathways by fine-tuning Poleta turnover. PMID: 25435364
  47. USP7 associates with AR in an androgen-dependent manner and mediates AR deubiquitination. PMID: 26175158
  48. The ability of MBD4 to directly interact with and recruit USP7 to chromocenters implicates it as an additional factor that can potentially regulate Dnmt1 activity during cell proliferation. PMID: 25358258
  49. USP7 directly regulates Chk1 protein levels by cleavage of the poly-ubiquitination chain. PMID: 25483066
  50. USP7 overexpression significantly correlated with malignant phenotype. PMID: 25519684

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Subcellular Location
Nucleus. Cytoplasm. Nucleus, PML body. Chromosome. Note=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.
Protein Families
Peptidase C19 family
Tissue Specificity
Expressed in neural progenitor cells (at protein level). Widely expressed. Overexpressed in prostate cancer.
Database Links

HGNC: 12630

OMIM: 602519

KEGG: hsa:7874

STRING: 9606.ENSP00000343535

UniGene: Hs.386939

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