Recombinant human HAUSP / USP7 protein is a Human Full Length protein, in the 2 to 1102 aa range, expressed in Baculovirus infected Sf9, with >=66% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
Images
Key facts
- Purity
- >=66% SDS-PAGE
- Endotoxin level
- < 1 EU/µg
- Expression system
- Baculovirus infected Sf9 cells
- Tags
- His-DDDDK tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Amino acid sequence
M H H H H H H D Y K D D D D K N H Q Q Q Q Q Q Q K A G E Q Q L S E P E D M E M E A G D T D D P P R I T Q N P V I N G N V A L S D G H N T A E E D M E D D T S W R S E A T F Q F T V E R F S R L S E S V L S P P C F V R N L P W K I M V M P R F Y P D R P H Q K S V G F F L Q C N A E S D S T S W S C H A Q A V L K I I N Y R D D E K S F S R R I S H L F F H K E N D W G F S N F M A W S E V T D P E K G F I D D D K V T F E V F V Q A D A P H G V A W D S K K H T G Y V G L K N Q G A T C Y M N S L L Q T L F F T N Q L R K A V Y M M P T E G D D S S K S V P L A L Q R V F Y E L Q H S D K P V G T K K L T K S F G W E T L D S F M Q H D V Q E L C R V L L D N V E N K M K G T C V E G T I P K L F R G K M V S Y I Q C K E V D Y R S D R R E D Y Y D I Q L S I K G K K N I F E S F V D Y V A V E Q L D G D N K Y D A G E H G L Q E A E K G V K F L T L P P V L H L Q L M R F M Y D P Q T D Q N I K I N D R F E F P E Q L P L D E F L Q K T D P K D P A N Y I L H A V L V H S G D N H G G H Y V V Y L N P K G D G K W C K F D D D V V S R C T K E E A I E H N Y G G H D D D L S V R H C T N A Y M L V Y I R E S K L S E V L Q A V T D H D I P Q Q L V E R L Q E E K R I E A Q K R K E R Q E A H L Y M Q V Q I V A E D Q F C G H Q G N D M Y D E E K V K Y T V F K V L K N S S L A E F V Q S L S Q T M G F P Q D Q I R L W P M Q A R S N G T K R P A M L D N E A D G N K T M I E L S D N E N P W T I F L E T V D P E L A A S G A T L P K F D K D H D V M L F L K M Y D P K T R S L N Y C G H I Y T P I S C K I R D L L P V M C D R A G F I Q D T S L I L Y E E V K P N L T E R I Q D Y D V S L D K A L D E L M D G D I I V F Q K D D P E N D N S E L P T A K E Y F R D L Y H R V D V I F C D K T I P N D P G F V V T L S N R M N Y F Q V A K T V A Q R L N T D P M L L Q F F K S Q G Y R D G P G N P L R H N Y E G T L R D L L Q F F K P R Q P K K L Y Y Q Q L K M K I T D F E N R R S F K C I W L N S Q F R E E E I T L Y P D K H G C V R D L L E E C K K A V E L G E K A S G K L R L L E I V S Y K I I G V H Q E D E L L E C L S P A T S R T F R I E E I P L D Q V D I D K E N E M L V T V A H F H K E V F G T F G I P F L L R I H Q G E H F R E V M K R I Q S L L D I Q E K E F E K F K F A I V M M G R H Q Y I N E D E Y E V N L K D F E P Q P G N M S H P R P W L G L D H F N K A P K R S R Y T Y L E K A I K I H N
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Associated Products
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Target data
Function
Hydrolase that deubiquitinates target proteins such as FOXO4, DEPTOR, 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, PubMed:35216969). 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, PubMed:26786098). 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). Involved in the regulation of WASH-dependent actin polymerization at the surface of endosomes and the regulation of endosomal protein recycling (PubMed:26365382). It maintains optimal WASH complex activity and precise F-actin levels via deubiquitination of TRIM27 and WASHC1 (PubMed:26365382). Mediates the deubiquitination of phosphorylated DEPTOR, promoting its stability and leading to decreased mTORC1 signaling (PubMed:35216969). (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. (Microbial infection) Upon infection with Epstein-Barr virus, the interaction with viral EBNA1 increases the association of USP7 with PML proteins, which is required for the polyubiquitylation and degradation of PML.
Alternative names
HAUSP, USP7, Ubiquitin carboxyl-terminal hydrolase 7, Deubiquitinating enzyme 7, Herpesvirus-associated ubiquitin-specific protease, Ubiquitin thioesterase 7, Ubiquitin-specific-processing protease 7
Recommended products
Recombinant human HAUSP / USP7 protein is a Human Full Length protein, in the 2 to 1102 aa range, expressed in Baculovirus infected Sf9, with >=66% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >=66% SDS-PAGE
- Endotoxin level
- < 1 EU/µg
- Expression system
- Baculovirus infected Sf9 cells
- Tags
- His-DDDDK tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- Specific activity: 545 pmol/min/μg
Assay Conditions: Reaction was performed in 50 mM Tris pH 7.4, 1 mM DTT. 0.5 mM EDTA, and 500 nM Ub-AMC. Reaction was incubated at 37°C for 15 min. and fluorescent signal was measured at excitation of 340 nm, and emission at 460 nm. - Accession
- Q93009-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Preservative: 0.61% Imidazole
Constituents: 5% Glycerol (glycerin, glycerine), 0.76% Sodium chloride, 0.75% Tris HCl, 0.02% Potassium chloride
Sequence info
Amino acid sequence
- M H H H H H H D Y K D D D D K N H Q Q Q Q Q Q Q K A G E Q Q L S E P E D M E M E A G D T D D P P R I T Q N P V I N G N V A L S D G H N T A E E D M E D D T S W R S E A T F Q F T V E R F S R L S E S V L S P P C F V R N L P W K I M V M P R F Y P D R P H Q K S V G F F L Q C N A E S D S T S W S C H A Q A V L K I I N Y R D D E K S F S R R I S H L F F H K E N D W G F S N F M A W S E V T D P E K G F I D D D K V T F E V F V Q A D A P H G V A W D S K K H T G Y V G L K N Q G A T C Y M N S L L Q T L F F T N Q L R K A V Y M M P T E G D D S S K S V P L A L Q R V F Y E L Q H S D K P V G T K K L T K S F G W E T L D S F M Q H D V Q E L C R V L L D N V E N K M K G T C V E G T I P K L F R G K M V S Y I Q C K E V D Y R S D R R E D Y Y D I Q L S I K G K K N I F E S F V D Y V A V E Q L D G D N K Y D A G E H G L Q E A E K G V K F L T L P P V L H L Q L M R F M Y D P Q T D Q N I K I N D R F E F P E Q L P L D E F L Q K T D P K D P A N Y I L H A V L V H S G D N H G G H Y V V Y L N P K G D G K W C K F D D D V V S R C T K E E A I E H N Y G G H D D D L S V R H C T N A Y M L V Y I R E S K L S E V L Q A V T D H D I P Q Q L V E R L Q E E K R I E A Q K R K E R Q E A H L Y M Q V Q I V A E D Q F C G H Q G N D M Y D E E K V K Y T V F K V L K N S S L A E F V Q S L S Q T M G F P Q D Q I R L W P M Q A R S N G T K R P A M L D N E A D G N K T M I E L S D N E N P W T I F L E T V D P E L A A S G A T L P K F D K D H D V M L F L K M Y D P K T R S L N Y C G H I Y T P I S C K I R D L L P V M C D R A G F I Q D T S L I L Y E E V K P N L T E R I Q D Y D V S L D K A L D E L M D G D I I V F Q K D D P E N D N S E L P T A K E Y F R D L Y H R V D V I F C D K T I P N D P G F V V T L S N R M N Y F Q V A K T V A Q R L N T D P M L L Q F F K S Q G Y R D G P G N P L R H N Y E G T L R D L L Q F F K P R Q P K K L Y Y Q Q L K M K I T D F E N R R S F K C I W L N S Q F R E E E I T L Y P D K H G C V R D L L E E C K K A V E L G E K A S G K L R L L E I V S Y K I I G V H Q E D E L L E C L S P A T S R T F R I E E I P L D Q V D I D K E N E M L V T V A H F H K E V F G T F G I P F L L R I H Q G E H F R E V M K R I Q S L L D I Q E K E F E K F K F A I V M M G R H Q Y I N E D E Y E V N L K D F E P Q P G N M S H P R P W L G L D H F N K A P K R S R Y T Y L E K A I K I H N
- Accession
- Q93009
- Protein length
- Full Length
- Predicted molecular weight
- 130 kDa
- Amino acids
- 2 to 1102
- Nature
- Recombinant
- Tags
- His-DDDDK tag N-Terminus
Specifications
- Form
- Liquid
- Additional notes
Affinity purified.
General info
- Function
Hydrolase that deubiquitinates target proteins such as FOXO4, DEPTOR, 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, PubMed:35216969). 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, PubMed:26786098). 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). Involved in the regulation of WASH-dependent actin polymerization at the surface of endosomes and the regulation of endosomal protein recycling (PubMed:26365382). It maintains optimal WASH complex activity and precise F-actin levels via deubiquitination of TRIM27 and WASHC1 (PubMed:26365382). Mediates the deubiquitination of phosphorylated DEPTOR, promoting its stability and leading to decreased mTORC1 signaling (PubMed:35216969).
- Sequence similarities
Belongs to the peptidase C19 family.
- Post-translational modifications
Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated.
- Subcellular localisation
- Nucleus, PML body
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Storage information
- Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
HAUSP also known as USP7 is a deubiquitinating enzyme with a molecular mass of approximately 135 kDa. It functions by removing ubiquitin molecules from target proteins influencing their stability and activity. HAUSP is widely expressed in various human tissues with notable presence in the nucleus and cytoplasm. Its expression is essential for modulation of multiple signaling pathways. The enzyme's capacity to regulate protein ubiquitination dynamics makes it a significant player in cellular function.
- Biological function summary
HAUSP influences several critical cellular processes including DNA repair transcriptional regulation and cell cycle progression. It often interacts with other proteins such as p53 to modify their functions by altering their ubiquitination status. HAUSP does not function in isolation but forms part of larger protein complexes where it plays a role in processing substrate proteins. Its ability to activate or deactivate proteins through deubiquitination highlights its importance in maintaining cellular homeostasis.
- Pathways
Research identifies HAUSP as an important component in both the p53 pathway and the Wnt signaling pathway. Through the p53 pathway HAUSP directly interacts with the p53 tumor suppressor protein influencing cell cycle and apoptosis decisions. Its participation in the Wnt signaling pathway associates it with beta-catenin where it supports cellular proliferation and differentiation. These pathway interactions illustrate HAUSP's integral role in maintaining cellular function and responding to various signaling inputs.
- Associated diseases and disorders
HAUSP has implications in cancer and neurodegenerative diseases. Aberrant activity or expression of HAUSP has been linked to tumorigenesis particularly through its interaction with the proteins p53 and MDM2 affecting cell survival and proliferation. In neurodegenerative conditions altered HAUSP activity may impact protein homeostasis and degradation pathways contributing to disease progression. Its connection to these proteins and disease states highlights its potential as a therapeutic target in associated disorders.
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2 product images
Functional Studies - Recombinant human HAUSP / USP7 protein (ab198464)
Specific activity of ab198464
SDS-PAGE - Recombinant human HAUSP / USP7 protein (ab198464)
10% SDS-PAGE analysis of 2 μg ab198464 stained with Coomassie
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