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AB127482

Recombinant Human USP12 protein

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Recombinant Human USP12 protein is a Human Fragment protein, in the 165 to 370 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

UBH1, USP12L1, USP12, Ubiquitin carboxyl-terminal hydrolase 12, Deubiquitinating enzyme 12, Ubiquitin specific peptidase 12, Ubiquitin thioesterase 12, Ubiquitin-hydrolyzing enzyme 1, Ubiquitin-specific-processing protease 12

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His-DHFR tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

O75317

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

Reactivity data

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

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"24 kDa","actualMolecularWeight":null,"aminoAcidEnd":370,"aminoAcidStart":165,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"O75317","tags":[{"tag":"His-DHFR","terminus":"N-Terminus"}]}]

Properties and storage information

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

Supplementary information

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

USP12 also known as Ubiquitin Specific Protease 12 is an enzyme that functions as a deubiquitinating enzyme. It possesses a mass of approximately 43 kDa. Mechanically USP12 removes ubiquitin moieties from protein substrates influencing their stability localization and function. This target is expressed in several tissues including the brain skeletal muscle and testis with a significant presence in cellular components implicated in ubiquitin-dependent processes.
Biological function summary

USP12 regulates protein degradation and turnover in cells affecting pathways involved in maintaining protein homeostasis. It forms a complex with WDR20 and UAF1 enhancing its enzymatic activity. This complex allows for precise regulation of substrate specificity and function in various cellular contexts. Through its deubiquitinating activity USP12 plays a role in cellular signaling and stress response.

Pathways

USP12 participates in the ubiquitin-proteasome pathway and the DNA damage response pathway. Its activity influences the turnover of proteins that participate in these processes such as androgen receptor and MDM2. The interaction with these proteins highlights USP12's involvement in pathways that are important for cellular responses to damage and the regulation of gene expression.

USP12 is associated with cancer and neurodegenerative diseases. Abnormal regulation of USP12 or its substrates can contribute to tumorigenesis due to uncontrolled cell proliferation or impaired apoptosis. Additionally its connection with proteins like AR and MDM2 places USP12 in the context of prostate cancer as alterations can disrupt androgen receptor signaling. Studies also suggest a role for USP12 in neurodegenerative disorders where protein misfolding and aggregation play significant roles but additional research is needed to clarify its impact.

Specifications

Form

Lyophilized

Additional notes

Purified via His tag

General info

Function

Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation (PubMed : 19075014, PubMed : 27373336). During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane (PubMed : 26811477). Plays an essential role in the selective LPS-induced macrophage response through the activation of NF-kappa-B pathway (PubMed : 28063927). In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation (PubMed : 37410794). Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation (PubMed : 31899788). Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF-kappa-B signaling pathway through deubiquitinating and stabilizing B-cell lymphoma/leukemia 10/BCL10 (By similarity). In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA (By similarity). Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process (PubMed : 36361894). Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes (PubMed : 22778262). Protects neurons against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux (PubMed : 30266909). This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex (By similarity). In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability (PubMed : 24145035).. (Microbial infection) Forms a complex with Epstein-Barr virus protein EBNA3 which is an active deubiquitinase activity that may select specific substrates to promote B-lymphocyte transformation.

Sequence similarities

Belongs to the peptidase C19 family. USP12/USP46 subfamily.

Product protocols

Target data

Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation (PubMed : 19075014, PubMed : 27373336). During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane (PubMed : 26811477). Plays an essential role in the selective LPS-induced macrophage response through the activation of NF-kappa-B pathway (PubMed : 28063927). In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation (PubMed : 37410794). Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation (PubMed : 31899788). Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF-kappa-B signaling pathway through deubiquitinating and stabilizing B-cell lymphoma/leukemia 10/BCL10 (By similarity). In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA (By similarity). Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process (PubMed : 36361894). Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes (PubMed : 22778262). Protects neurons against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux (PubMed : 30266909). This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex (By similarity). In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability (PubMed : 24145035).. (Microbial infection) Forms a complex with Epstein-Barr virus protein EBNA3 which is an active deubiquitinase activity that may select specific substrates to promote B-lymphocyte transformation.
See full target information USP12

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