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AB86220

Anti-TRIP12/ULF antibody

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(5 Publications)

Rabbit Polyclonal TRIP12/ULF antibody. Suitable for IP, WB and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Synthetic Peptide within Human TRIP12.

View Alternative Names

KIAA0045, ULF, TRIP12, E3 ubiquitin-protein ligase TRIP12, E3 ubiquitin-protein ligase for Arf, HECT-type E3 ubiquitin transferase TRIP12, Thyroid receptor-interacting protein 12, TR-interacting protein 12, TRIP-12

2 Images
Immunoprecipitation - Anti-TRIP12/ULF antibody (AB86220)
  • IP

Unknown

Immunoprecipitation - Anti-TRIP12/ULF antibody (AB86220)

Detection of human TRIP12/ULF in Immunoprecipitates of HeLa whole cell lysate (1 mg lysate for IP, 20% of IP loaded) using ab86220 at 3 μg/mg lysate for IP, and at 0.1 μg/ml for subsequent Western blot.

Detection : Chemiluminescence with an exposure time of 10 seconds.

All lanes:

Immunoprecipitation - Anti-TRIP12/ULF antibody (ab86220)

Predicted band size: 220 kDa

false

Western blot - Anti-TRIP12/ULF antibody (AB86220)
  • WB

Unknown

Western blot - Anti-TRIP12/ULF antibody (AB86220)

All lanes:

Western blot - Anti-TRIP12/ULF antibody (ab86220) at 0.04 µg/mL

Lane 1:

HeLa whole cell lysate at 5 µg

Lane 2:

HeLa whole cell lysate at 1.5 µg

Lane 3:

HeLa whole cell lysate at 0.5 µg

Predicted band size: 220 kDa

true

Exposure time: 3min

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB, IP

applications

Immunogen

Synthetic Peptide within Human TRIP12. The exact immunogen used to generate this antibody is proprietary information.

Q14669

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IP-species-checked": "testedAndGuaranteed", "IP-species-dilution-info": "2-5 µg/mg of lysate", "IP-species-notes": "<p></p>", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2000 - 1/10000", "WB-species-notes": "<p></p>" }, "Camel": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Chimpanzee": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Dog": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Elephant": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Gorilla": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Guinea pig": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Orangutan": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Pig": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Rhesus monkey": { "IP-species-checked": "predicted", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 6.8 - 7.4 Preservative: 0.09% Sodium azide Constituents: Tris buffered saline, 0.1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle|Do Not Freeze

Supplementary information

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

TRIP12 also known as Thyroid Hormone Receptor Interactor 12 or ULF (Ubiquitin Ligase for FBW7) is an E3 ubiquitin ligase. Mechanically TRIP12 facilitates the ubiquitination and subsequent proteasomal degradation of specific proteins. It has an approximate mass of 220 kDa. This protein is expressed in various tissues including the brain and liver. TRIP12 often interacts with other proteins through its ARM and HECT domains playing an important role in regulating protein stability.
Biological function summary

TRIP12 functions as a regulator of protein turnover impacting processes such as cell cycle progression and DNA damage responses. It is not part of a larger complex but operates independently to exert its influence. The target specifically targets proteins like p53 and FBW7 for degradation allowing cells to maintain homeostasis and adapt to changing conditions. This regulation ensures cells respond appropriately to DNA damage by either promoting repair pathways or facilitating apoptosis when repair is not feasible.

Pathways

TRIP12 plays a role in the ubiquitin-proteasome system and the p53 signaling pathway. In the ubiquitin-proteasome system TRIP12 works alongside other E3 ligases to regulate protein degradation ensuring proteins that are damaged or no longer needed are efficiently removed. Within the p53 signaling pathway TRIP12 influences the stability and activity of the tumor suppressor protein p53 helping control cell cycle arrest and apoptosis. TRIP12's relationship with FBW7 further connects it to pathways involved in cancer as FBW7 targets many oncoproteins.

TRIP12 has links to cancer and neurodevelopmental disorders. Alterations in the activity or expression of TRIP12 can lead to the accumulation of proteins like p53 which may contribute to tumorigenesis. Mutations in TRIP12 have also been associated with neurodevelopmental disorders where disrupted protein turnover impacts neural development. Its interaction with proteins such as p53 and FBW7 highlights its potential role in disease mechanisms making it a target of interest for therapeutic intervention.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair (PubMed : 19028681, PubMed : 22884692). Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins (PubMed : 19028681). Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed : 22884692). In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress (PubMed : 20208519). In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation (PubMed : 20208519). Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A (PubMed : 20208519). Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation (PubMed : 18627766). Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins (PubMed : 20829358). Mediates ubiquitination of ASXL1 : following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex (PubMed : 30982744).
See full target information TRIP12

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Cancer research 82:916-928 PubMed34965932

2021

p16 Represses DNA Damage Repair via a Novel Ubiquitin-Dependent Signaling Cascade.

Applications

Unspecified application

Species

Unspecified reactive species

David P Molkentine,Jessica M Molkentine,Kathleen A Bridges,David R Valdecanas,Annika Dhawan,Reshub Bahri,Andrew J Hefner,Manish Kumar,Liangpeng Yang,Mohamed Abdelhakiem,Phillip M Pifer,Vlad Sandulache,Aakash Sheth,Beth M Beadle,Howard D Thames,Kathryn A Mason,Curtis R Pickering,Raymond E Meyn,Heath D Skinner

The Journal of biological chemistry 296:100246 PubMed33853758

2021

The deubiquitinase TRABID stabilizes the K29/K48-specific E3 ubiquitin ligase HECTD1.

Applications

Unspecified application

Species

Unspecified reactive species

Lee D Harris,Janic Le Pen,Nico Scholz,Juliusz Mieszczanek,Natalie Vaughan,Simon Davis,Georgina Berridge,Benedikt M Kessler,Mariann Bienz,Julien D F Licchesi

Nucleic acids research 47:11268-11283 PubMed31586398

2019

UBR5 interacts with the replication fork and protects DNA replication from DNA polymerase η toxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Lina Cipolla,Federica Bertoletti,Antonio Maffia,Chih-Chao Liang,Alan R Lehmann,Martin A Cohn,Simone Sabbioneda

Molecular cell 67:181-193.e5 PubMed28689657

2017

Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the HECT E3 Ubiquitin Ligase Hyd/UBR5.

Applications

Unspecified application

Species

Unspecified reactive species

Joshua E Flack,Juliusz Mieszczanek,Nikola Novcic,Mariann Bienz

eLife 5: PubMed27183006

2016

ERG signaling in prostate cancer is driven through PRMT5-dependent methylation of the Androgen Receptor.

Applications

WB

Species

Unspecified reactive species

Zineb Mounir,Joshua M Korn,Thomas Westerling,Fallon Lin,Christina A Kirby,Markus Schirle,Gregg McAllister,Greg Hoffman,Nadire Ramadan,Anke Hartung,Yan Feng,David Randal Kipp,Christopher Quinn,Michelle Fodor,Jason Baird,Marie Schoumacher,Ronald Meyer,James Deeds,Gilles Buchwalter,Travis Stams,Nicholas Keen,William R Sellers,Myles Brown,Raymond A Pagliarini
View all publications

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