JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB157086

Recombinant human OTUB1 protein

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant human OTUB1 protein is a Human Full Length protein, in the 1 to 271 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.

View Alternative Names

OTB1, OTU1, HSPC263, OTUB1, Ubiquitin thioesterase OTUB1, Deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, Otubain-1, Ubiquitin-specific-processing protease OTUB1, hOTU1

2 Images
Functional Studies - Recombinant human OTUB1 protein (AB157086)
  • FuncS

Unknown

Functional Studies - Recombinant human OTUB1 protein (AB157086)

Deubiquitinylation assay : Western Blot showing polyubiquitin chains (K48-linked; K63-linked) incubated with (+) or without (-) ab157086 detected with ubiquitin polyclonal antibody at 1/1000 dilution.

SDS-PAGE - Recombinant human OTUB1 protein (AB157086)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human OTUB1 protein (AB157086)

SDS-PAGE analysis of ab157086 stained with Coomassie (8µg).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Deubiquitinylation assay: Western Blot showing polyubiquitin chains (K48-linked; K63-linked) incubated with (+) or without (-) ab157086 detected with ubiquitin polyclonal antibody at 1/1000 dilution.

Accession

Q96FW1

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Constituents: 0.79% Tris HCl, 0.29% Sodium chloride, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

style
left-column

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>" } } }
style
left-column
style
left-column

Sequence info

[{"sequence":"MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK","proteinLength":"Full Length","predictedMolecularWeight":"33 kDa","actualMolecularWeight":null,"aminoAcidEnd":271,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96FW1","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
style
left-column

Properties and storage information

Shipped at conditions
Blue 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
style
left-column

Supplementary information

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

The OTUB1 protein also known as OTU domain-containing ubiquitin aldehyde-binding protein 1 plays an important role in the removal of ubiquitin from proteins. This process is important for regulating protein stability and function within the cell. OTUB1 has a mass of approximately 32 kDa and is expressed ubiquitously across various tissues indicating its essential nature in cellular functions.
Biological function summary

OTUB1 functions as a deubiquitinating enzyme that cleaves ubiquitin from substrates influencing various cellular processes. It acts independently or as part of larger protein complexes. By controlling protein degradation pathways OTUB1 impacts protein turnover and cellular homeostasis. Interactions with other proteins allow OTUB1 to exert influence on different signaling pathways and cellular stress responses.

Pathways

OTUB1 holds a significant position in the regulation of the ubiquitin-proteasome system and DNA damage repair pathway. It closely interacts with proteins such as UBE2N affecting the DNA damage response. Additionally OTUB1 regulates processes through modulating pathways like NF-kB by interacting with and stabilizing specific protein factors involved.

OTUB1’s function connects it to various pathological states like cancer and neurodegenerative diseases. Aberrant expression or mutations in OTUB1 can lead to disruptions in cell cycle regulation and apoptosis contributing to oncogenesis. In the context of neurodegenerative diseases OTUB1 is related to tau stabilization with proteins such as HSP90 playing a role in the same regulatory mechanisms highlighting its relevance in these disorders.
style
left-column

Specifications

Form

Liquid

style
left-column

General info

Function

Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation (PubMed : 12401499, PubMed : 12704427, PubMed : 14661020, PubMed : 23827681). Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen (PubMed : 14661020). Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy (PubMed : 14661020). Isoform 1 destabilizes RNF128, leading to prevent anergy (PubMed : 14661020). In contrast, isoform 2 stabilizes RNF128 and promotes anergy (PubMed : 14661020). Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 (PubMed : 14661020). Deubiquitinates estrogen receptor alpha (ESR1) (PubMed : 19383985). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (PubMed : 18954305, PubMed : 19211026, PubMed : 23827681). Not able to cleave di-ubiquitin (PubMed : 18954305, PubMed : 23827681). Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (PubMed : 18954305, PubMed : 23827681).. Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites (PubMed : 20725033, PubMed : 22325355). Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks (PubMed : 20725033, PubMed : 22325355). Inhibition occurs by binding to free ubiquitin : free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1 (PubMed : 20725033, PubMed : 22325355). The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain (PubMed : 20725033, PubMed : 22325355). Acts as a regulator of mTORC1 and mTORC2 complexes (PubMed : 29382726, PubMed : 35927303). When phosphorylated at Tyr-26, acts as an activator of the mTORC1 complex by mediating deubiquitination of RPTOR via a non-catalytic process : acts by binding and inhibiting the activity of the ubiquitin-conjugating enzyme E2 (UBE2D1/UBCH5A, UBE2W/UBC16 and UBE2N/UBC13), thereby preventing ubiquitination of RPTOR (PubMed : 35927303). Can also act as an inhibitor of the mTORC1 and mTORC2 complexes in response to amino acids by mediating non-catalytic deubiquitination of DEPTOR (PubMed : 29382726).

Sequence similarities

Belongs to the peptidase C65 family.

Post-translational modifications

Phosphorylation at Tyr-26 by SRC and SRMS promotes deubiquitination of RPTOR via a non-catalytic process.

style
left-column

Product protocols

style
left-column

Target data

Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation (PubMed : 12401499, PubMed : 12704427, PubMed : 14661020, PubMed : 23827681). Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen (PubMed : 14661020). Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy (PubMed : 14661020). Isoform 1 destabilizes RNF128, leading to prevent anergy (PubMed : 14661020). In contrast, isoform 2 stabilizes RNF128 and promotes anergy (PubMed : 14661020). Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 (PubMed : 14661020). Deubiquitinates estrogen receptor alpha (ESR1) (PubMed : 19383985). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (PubMed : 18954305, PubMed : 19211026, PubMed : 23827681). Not able to cleave di-ubiquitin (PubMed : 18954305, PubMed : 23827681). Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin (PubMed : 18954305, PubMed : 23827681).. Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites (PubMed : 20725033, PubMed : 22325355). Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks (PubMed : 20725033, PubMed : 22325355). Inhibition occurs by binding to free ubiquitin : free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1 (PubMed : 20725033, PubMed : 22325355). The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain (PubMed : 20725033, PubMed : 22325355). Acts as a regulator of mTORC1 and mTORC2 complexes (PubMed : 29382726, PubMed : 35927303). When phosphorylated at Tyr-26, acts as an activator of the mTORC1 complex by mediating deubiquitination of RPTOR via a non-catalytic process : acts by binding and inhibiting the activity of the ubiquitin-conjugating enzyme E2 (UBE2D1/UBCH5A, UBE2W/UBC16 and UBE2N/UBC13), thereby preventing ubiquitination of RPTOR (PubMed : 35927303). Can also act as an inhibitor of the mTORC1 and mTORC2 complexes in response to amino acids by mediating non-catalytic deubiquitination of DEPTOR (PubMed : 29382726).
See full target information OTUB1
style
left-column
style
left-column
style
right-column

Complementary Products

Primary Antibodies

AB175200

Anti-OTUB1 antibody [EPR13028(B)]

RabMAb|Recombinant|KO Validated

Western blot - Anti-OTUB1 antibody [EPR13028(B)] (AB175200)

  • 5
  • 3
Proteins & Peptides

AB269124

Recombinant human USP5 protein (Active)

Functional Studies - Recombinant human USP5 protein (Active) (AB269124)

  • 0
  • 0
Primary Antibodies

AB40810

Anti-Glycogen synthase 1/GYS1 antibody [EP817Y]

RabMAb|Recombinant|KO Validated

Flow Cytometry (Intracellular) - Anti-Glycogen synthase 1/GYS1 antibody [EP817Y] (AB40810)

  • 4
  • 6
Cell Lines & Lysates

AB257569

Human OTUB1 knockout HEK-293T cell lysate

Western blot - Human OTUB1 knockout HEK-293T cell lysate (AB257569)

  • 0
  • 0

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com