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AB271783

Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus)

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Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) is a Human Fragment protein, in the 2 to 914 aa range, expressed in HEK 293 cells, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

KIAA1003, LSFR3A, VDU2, USP20, Ubiquitin carboxyl-terminal hydrolase 20, Deubiquitinating enzyme 20, Ubiquitin thioesterase 20, Ubiquitin-specific-processing protease 20, VHL-interacting deubiquitinating enzyme 2, hVDU2

2 Images
Functional Studies - Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) (AB271783)
  • FuncS

Supplier Data

Functional Studies - Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) (AB271783)

Functional studies analysis of ab271783 was 10 pmol/min/μg.

SDS-PAGE - Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) (AB271783)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human USP20 protein (6x His N-Terminus + DDDDK tag C-Terminus) (AB271783)

SDS-PAGE analysis of ab271783.

Key facts

Purity

>90% SDS-PAGE

Expression system

HEK 293 cells

Tags

6x His tag N-Terminus DDDDK tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific Activity: 10 pmol/min/μg

Assay Conditions: 50mM Tris-HCl, 0.5mM EDTA, 0.05% Tween 20, 1mM DTT, 500nM Ubiquitin-AMC. Incubate at room temperature for 30 minutes. Fluorescence intensity is measured at exc/em of 360nm/460nm using Tecan M1000 plate reader.

Accession

Q9Y2K6

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.02% Potassium chloride

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":"GDSRDLCPHLDSIGEVTKEDLLLKSKGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTFIKLNKAFQAEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSVAQPLGPENLHGEQKIEAETRAV","proteinLength":"Fragment","predictedMolecularWeight":"104 kDa","actualMolecularWeight":null,"aminoAcidEnd":914,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"Q9Y2K6","tags":[{"tag":"6x His","terminus":"N-Terminus"},{"tag":"DDDDK","terminus":"C-Terminus"}]}]

Properties and storage information

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
True

Supplementary information

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

USP20 also known as ubiquitin-specific peptidase 20 is an enzyme involved in removing ubiquitin molecules from proteins a process that regulates protein degradation and stabilization. The molecular mass of USP20 is approximately 97 kDa. USP20 is widely expressed in various tissues including brain heart and skeletal muscle indicating its versatile role in different cellular contexts. It deubiquitinates substrates impacting their protein stability and controlling their signal pathways.
Biological function summary

Removal of ubiquitin from protein substrates is an important function of USP20 which interacts with diverse protein complexes. USP20 modulates stability of multiple proteins by preventing their proteasomal degradation. It is involved in maintaining balance in cellular protein levels which affects cellular activities like cell cycle progression and response to stress. This activity can significantly influence the timing of protein turnover impacting how cells respond to changes.

Pathways

Deubiquitinating activities of USP20 significantly influence stress response and cellular signaling. USP20 functions within the NF-κB signaling pathway a critical mediator of immune response where it interacts with proteins such as IκBα stabilizing them by removing ubiquitin moieties. This regulatory mechanism is essential for proper NF-κB activation and immune response. Additionally USP20 plays a role in endoplasmic reticulum stress pathways by modulating GRP78 levels highlighting its involvement in protein folding and stress handling.

Dysregulation of USP20 is linked to several health conditions like cancer and neurodegenerative diseases. In cancer USP20 influences tumor progression by interacting with the protein MCL-1 an important factor in cell survival therefore affecting apoptosis. In neurodegenerative diseases disruptions in USP20 function or expression can lead to imbalance of protein homeostasis contributing to protein aggregation a common hallmark in diseases like Alzheimer's. Studying USP20 and its interconnected pathways and proteins offers insights into potential therapeutic strategies for these disorders.

Specifications

Form

Liquid

General info

Function

Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis (PubMed : 27801882, PubMed : 29487085). Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination (PubMed : 26839314). Promotes cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-linked ubiquitination of STING1 leading to its stabilization (PubMed : 27801882). Plays an essential role in autophagy induction by regulating the ULK1 stability through deubiquitination of ULK1 (PubMed : 29487085). Acts as a positive regulator for NF-kappa-B activation by TNF through deubiquitinating 'Lys-48'-linked polyubiquitination of SQSTM1, leading to its increased stability (PubMed : 32354117). Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2) (PubMed : 19424180). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2 (PubMed : 19424180). This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity (PubMed : 15776016). Deubiquitinates MCL1, a pivotal member of the anti-apoptotic Bcl-2 protein family to regulate its stability (PubMed : 35063767). Within the endoplasmic reticulum, participates with USP33 in the rescue of post-translationally targeted membrane proteins that are inappropriately ubiquitinated by the cytosolic protein quality control in the cytosol (PubMed : 33792613).

Sequence similarities

Belongs to the peptidase C19 family. USP20/USP33 subfamily.

Post-translational modifications

Ubiquitinated via a VHL-dependent pathway for proteasomal degradation.

Subcellular localisation

Cytoskeleton

Product protocols

Target data

Deubiquitinating enzyme that plays a role in many cellular processes including autophagy, cellular antiviral response or membrane protein biogenesis (PubMed : 27801882, PubMed : 29487085). Attenuates TLR4-mediated NF-kappa-B signaling by cooperating with beta-arrestin-2/ARRB2 and inhibiting TRAF6 autoubiquitination (PubMed : 26839314). Promotes cellular antiviral responses by deconjugating 'Lys-33' and 'Lys-48'-linked ubiquitination of STING1 leading to its stabilization (PubMed : 27801882). Plays an essential role in autophagy induction by regulating the ULK1 stability through deubiquitination of ULK1 (PubMed : 29487085). Acts as a positive regulator for NF-kappa-B activation by TNF through deubiquitinating 'Lys-48'-linked polyubiquitination of SQSTM1, leading to its increased stability (PubMed : 32354117). Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2) (PubMed : 19424180). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2 (PubMed : 19424180). This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity (PubMed : 15776016). Deubiquitinates MCL1, a pivotal member of the anti-apoptotic Bcl-2 protein family to regulate its stability (PubMed : 35063767). Within the endoplasmic reticulum, participates with USP33 in the rescue of post-translationally targeted membrane proteins that are inappropriately ubiquitinated by the cytosolic protein quality control in the cytosol (PubMed : 33792613).
See full target information USP20

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