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AB269121

Recombinant human USP28 protein (Active)

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Recombinant human USP28 protein (Active) is a Human Fragment protein, in the 155 to 675 aa range, expressed in Escherichia coli, with >70%, suitable for SDS-PAGE, FuncS.

View Alternative Names

KIAA1515, USP28, Ubiquitin carboxyl-terminal hydrolase 28, Deubiquitinating enzyme 28, Ubiquitin thioesterase 28, Ubiquitin-specific-processing protease 28

2 Images
Functional Studies - Recombinant human USP28 protein (Active) (AB269121)
  • FuncS

Supplier Data

Functional Studies - Recombinant human USP28 protein (Active) (AB269121)

The specific activity of ab269121 was 499 nmol/min/mg in a DUB assay using ubiquitin-based proluciferin substrate.

SDS-PAGE - Recombinant human USP28 protein (Active) (AB269121)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human USP28 protein (Active) (AB269121)

SDS-PAGE analysis of ab269121.

Key facts

Purity

>70% SDS-PAGE

Expression system

Escherichia coli

Tags

GST tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

The specific activity of ab269121 was 499 nmol/min/mg in a DUB assay using ubiquitin-based proluciferin substrate.

Accession

Q96RU2

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF

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>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"RRVDGWPVGLKNVGNTCWFSAVIQSLFQLPEFRRLVLSYSLPQNVLENCRSHTEKRNIMFMQELQYLFALMMGSNRKFVDPSAALDLLKGAFRSSEEQQQDVSEFTHKLLDWLEDAFQLAVNVNSPRNKSENPMVQLFYGTFLTEGVREGKPFCNNETFGQYPLQVNGYRNLDECLEGAMVEGDVELLPSDHSVKYGQERWFTKLPPVLTFELSRFEFNQSLGQPEKIHNKLEFPQIIYMDRYMYRSKELIRNKRECIRKLKEEIKILQQKLERYVKYGSGPARFPLPDMLKYVIEFASTKPASESCPPESDTHMTLPLSSVHCSVSDQTSKESTSTESSSQDVESTFSSPEDSLPKSKPLTSSRSSMEMPSQPAPRTVTDEEINFVKTCLQRWRSEIEQDIQDLKTCIASTTQTIEQMYCDPLLRQVPYRLHAVLVHEGQANAGHYWAYIYNQPRQSWLKYNDISVTESSWEEVERDSYGGLRNVSAYCLMYINDKLPYFNAEAAPTESDQMSEVEALSV","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":675,"aminoAcidStart":155,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96RU2","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

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

USP28 also known as Ubiquitin Specific Peptidase 28 is a deubiquitinating enzyme responsible for removing ubiquitin from protein substrates. It belongs to the cysteine protease family and has a molecular mass of approximately 120 kDa. USP28 is mainly expressed in the nucleus and cytoplasm of cells and appears in various tissues including the lung liver and gastrointestinal tract. It plays a role in regulating protein stability by counteracting ubiquitination an important process for protein degradation.
Biological function summary

This deubiquitinase regulates several cellular processes such as DNA damage response cell cycle progression and apoptosis. USP28 influences protein stability by directly associating with components of the c-MYC signaling pathway. It is known to interact with and stabilize Fbw7 which is part of the ubiquitin ligase complex thereby affecting the turnover of proteins like c-MYC and cyclin E. Through these interactions USP28 helps maintain normal levels of these important regulators for healthy cellular functions.

Pathways

The enzyme plays an important part in the DNA damage response and MAPK signaling pathways. These pathways ensure proper genomic integrity and cell proliferation. USP28 enhances the stability of the key regulatory protein c-MYC in the p53 pathway emphasizing its role in cell cycle regulation. Its interaction with other proteins like Fbw7 and c-MYC allows it to modulate the rate of cell growth and division indicating its importance in controlled cellular pathways.

USP28 has connections to cancer and neurodegenerative diseases. Its interactions with c-MYC are implicated in tumorigenesis particularly in colorectal and breast cancers due to the stabilization of oncogenic proteins that promote uncontrollable cell proliferation. Additionally USP28 might contribute to neurodegenerative disorders by affecting protein aggregates commonly seen in such diseases although studies are less established in this area. The enzyme's strong connection with proteins like Fbw7 and c-MYC highlights its relevance in these disease situations making it a potential target for therapeutic intervention.

Specifications

Form

Liquid

General info

Function

Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome : acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells (PubMed : 24623306).

Sequence similarities

Belongs to the peptidase C19 family. USP28 subfamily.

Post-translational modifications

Degraded upon nickel ion level or hypoxia exposure.. Phosphorylated upon DNA damage at Ser-67 and Ser-714, by ATM or ATR (PubMed:16901786). Phosphorylated by PRKD1 (PubMed:24623306).

Subcellular localisation

Nucleus

Product protocols

Target data

Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome : acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus. Deubiquitinates ZNF304, hence preventing ZNF304 degradation by the proteasome and leading to the activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) in a subset of colorectal cancers (CRC) cells (PubMed : 24623306).
See full target information USP28

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