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AB127142

Recombinant Human USP3 protein

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Recombinant Human USP3 protein is a Human Fragment protein, in the 313 to 520 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

Ubiquitin carboxyl-terminal hydrolase 3, Deubiquitinating enzyme 3, Ubiquitin thioesterase 3, Ubiquitin-specific-processing protease 3, USP3

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His-DHFR tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9Y6I4

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.58% Sodium chloride, 0.32% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"23.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":520,"aminoAcidStart":313,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9Y6I4","tags":[{"tag":"His-DHFR","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

USP3 also known as Ubiquitin Specific Peptidase 3 is an enzyme that functions as a deubiquitinating enzyme (DUB). This protein plays a role in removing ubiquitin moieties from polyubiquitinated protein substrates. By regulating ubiquitination USP3 controls protein degradation. The full-length human USP3 protein has a molecular mass of approximately 109 kDa. Scientists have found USP3 expression in various tissues including the liver lungs and kidneys indicating its widespread biological significance.
Biological function summary

USP3 influences the regulation of the cell cycle and genome maintenance. It does not function alone; USP3 can associate with other proteins to form complexes that modulate these intracellular processes. Its activity in deubiquitination contributes to chromatin remodeling by stabilizing or activating proteins involved in cellular division and DNA repair. Therefore USP3 plays a role in maintaining cellular integrity and preventing genomic instability.

Pathways

Deubiquitination events involving USP3 impact key regulatory circuits like the DNA damage response and cell cycle checkpoints. Within these pathways USP3 collaborates with proteins such as H2A and H2AX where it maintains their stability by deubiquitinating them. By influencing these pathways USP3 ensures the proper execution of cell cycle transitions and the DNA damage response preventing errors during replication and division.

USP3 has implications in both cancer and neurodegenerative diseases. Its dysregulation contributes to abnormal cell proliferation and defective DNA repair mechanisms which are hallmarks of various cancers including breast cancer. USP3 is also connected to Rett syndrome where it affects the stability of proteins like MECP2 involved in neuronal function. Understanding USP3's role in these diseases highlights its potential as a therapeutic target for improving treatment strategies.
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Specifications

Form

Lyophilized

Additional notes

Purified via His tag

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General info

Function

Deubiquitinase that plays a role in several cellular processes including transcriptional regulation, cell cycle progression or innate immunity. In response to DNA damage, deubiquitinates monoubiquitinated target proteins such as histone H2A and H2AX and thereby counteracts RNF168- and RNF8-mediated ubiquitination. In turn, participates in the recruitment of DNA damage repair factors to DNA break sites (PubMed : 24196443). Required for proper progression through S phase and subsequent mitotic entry (PubMed : 17980597). Acts as a positive regulator of TP53 by deubiquitinating and stabilizing it to promote normal cell proliferation and transformation (PubMed : 28807825). Participates in establishing tolerance innate immune memory through non-transcriptional feedback. Mechanistically, negatively regulates TLR-induced NF-kappa-B signaling by targeting and removing the 'Lys-63'-linked polyubiquitin chains on MYD88 (PubMed : 37971847). Negatively regulates the activation of type I interferon signaling by mediating 'Lys-63'-linked polyubiquitin chains on RIGI and IFIH1 (PubMed : 24366338). Deubiquitinates also ASC/PYCARD, the central adapter mediating the assembly and activation of most inflammasomes, and thereby promotes inflammasome activation (PubMed : 36050480).

Sequence similarities

Belongs to the peptidase C19 family. USP3 subfamily.

Subcellular localisation

Nucleus

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Product protocols

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Target data

Deubiquitinase that plays a role in several cellular processes including transcriptional regulation, cell cycle progression or innate immunity. In response to DNA damage, deubiquitinates monoubiquitinated target proteins such as histone H2A and H2AX and thereby counteracts RNF168- and RNF8-mediated ubiquitination. In turn, participates in the recruitment of DNA damage repair factors to DNA break sites (PubMed : 24196443). Required for proper progression through S phase and subsequent mitotic entry (PubMed : 17980597). Acts as a positive regulator of TP53 by deubiquitinating and stabilizing it to promote normal cell proliferation and transformation (PubMed : 28807825). Participates in establishing tolerance innate immune memory through non-transcriptional feedback. Mechanistically, negatively regulates TLR-induced NF-kappa-B signaling by targeting and removing the 'Lys-63'-linked polyubiquitin chains on MYD88 (PubMed : 37971847). Negatively regulates the activation of type I interferon signaling by mediating 'Lys-63'-linked polyubiquitin chains on RIGI and IFIH1 (PubMed : 24366338). Deubiquitinates also ASC/PYCARD, the central adapter mediating the assembly and activation of most inflammasomes, and thereby promotes inflammasome activation (PubMed : 36050480).
See full target information USP3
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