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AB217069

Anti-UBR2 antibody

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(6 Publications)

Rabbit Polyclonal UBR2 antibody. Suitable for IP, WB and reacts with Human, Mouse samples. Cited in 6 publications. Immunogen corresponding to Synthetic Peptide within Human UBR2 aa 1700 to C-terminus.

View Alternative Names

C6orf133, KIAA0349, UBR2, E3 ubiquitin-protein ligase UBR2, N-recognin-2, Ubiquitin-protein ligase E3-alpha-2, Ubiquitin-protein ligase E3-alpha-II

2 Images
Immunoprecipitation - Anti-UBR2 antibody (AB217069)
  • IP

Supplier Data

Immunoprecipitation - Anti-UBR2 antibody (AB217069)

Detection of UBR2 in immunoprecipitates of Jurkat whole cell lysate prepared using NETN lysis buffer (0.5 or 1 mg for IP, 20% of IP loaded). ab217069 was used at 6 μg/mg lysate for IP (Lane 1), and at 1 μg/ml for subsequent Western blot detection. Lane 2 represents control IgG IP. Detection : chemiluminescence with an exposure time of 30 seconds.

All lanes:

Immunoprecipitation - Anti-UBR2 antibody (ab217069)

Predicted band size: 201 kDa

false

Western blot - Anti-UBR2 antibody (AB217069)
  • WB

Supplier Data

Western blot - Anti-UBR2 antibody (AB217069)

All lanes:

Western blot - Anti-UBR2 antibody (ab217069) at 0.1 µg/mL

Lane 1:

HeLa whole cell lysate at 50 µg

Lane 2:

293T whole cell lysate at 50 µg

Lane 3:

Jurkat whole cell lysate at 50 µg

Lane 4:

mouse TCMK1 whole cell lysate at 50 µg

Lane 5:

mouse NIH 3T3 whole cell lysate at 50 µg

Predicted band size: 201 kDa

true

Exposure time: 75s

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

WB, IP

applications

Immunogen

Synthetic Peptide within Human UBR2 aa 1700 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q8IWV8

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": "2-10 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>" }, "Mouse": { "IP-species-checked": "guaranteed", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2000 - 1/10000", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Purification notes
ab217069 was affinity purified using an epitope specific to UBR2 immobilized on solid support.
Storage buffer
pH: 7 - 8 Preservative: 0.09% Sodium azide Constituents: 99% Tris citrate/phosphate
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
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

Supplementary information

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

UBR2 also known as E3 ubiquitin-protein ligase UBR2 acts as a component of the N-end rule pathway that recognizes proteins with destabilizing N-terminal residues. This recognition leads to ubiquitination and proteasomal degradation. UBR2 has a molecular mass of about 200 kDa. It is expressed in various tissues with significant expression levels found in the testes heart skeletal muscle and brain. UBR2's ability to tag proteins for degradation makes it an important player in regulating protein quality and quantity within cells.
Biological function summary

UBR2 plays an important role in the cellular processes such as meiosis and DNA damage repair. During meiosis UBR2 associates with the synaptonemal complex a critical structure for chromosome pairing and segregation. It interacts with proteins like RAD18 and influences the post-replicative DNA damage repair. In addition UBR2 participates in the turnover of proteins involved in DNA metabolic processes indicating its broad regulatory impact on genome integrity and cellular homeostasis.

Pathways

UBR2 integrates into the ubiquitin-proteasome system and the DNA repair pathways. It functions in the N-end rule pathway influencing protein degradation and consequently cell cycle and apoptosis. UBR2 interacts with other proteins such as UBR1 and ATE1 linking it to several key cellular pathways affecting growth and response to stress conditions. In the context of DNA damage response UBR2's role in promoting repair through its action on repair proteins highlights its importance in maintaining cellular stability.

UBR2 associates with infertility and cancer. Mutations or dysregulation of UBR2 can lead to reproductive issues due to its critical role in meiotic chromosome segregation aligning it with infertility concerns. Furthermore abnormal UBR2 expression or function can also contribute to tumorigenesis. It impacts the degradation of proteins like p53 a well-known tumor suppressor indicating its potential link to cancer development when pathways involving UBR2 are disrupted. Understanding UBR2's involvement in these diseases opens pathways for novel therapeutic interventions targeting its regulatory mechanisms.

Product protocols

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

Target data

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (PubMed : 15548684, PubMed : 20835242, PubMed : 28392261). Recognizes and binds to proteins bearing specific N-terminal residues (N-degrons) that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (PubMed : 20835242, PubMed : 28392261). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed : 20835242, PubMed : 28392261). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed : 20835242). In contrast, it strongly binds methylated N-degrons (PubMed : 28392261). Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A (By similarity). Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (PubMed : 20298436). Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis (By similarity). Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retrotransposon mobilization (By similarity). Catalyzes ubiquitination and degradation of the N-terminal part of NLRP1 following NLRP1 activation by pathogens and other damage-associated signals : ubiquitination promotes degradation of the N-terminal part and subsequent release of the cleaved C-terminal part of NLRP1, which polymerizes and forms the NLRP1 inflammasome followed by host cell pyroptosis (By similarity). Plays a role in T-cell receptor signaling by inducing 'Lys-63'-linked ubiquitination of lymphocyte cell-specific kinase LCK (PubMed : 38225265). This activity is regulated by DUSP22, which induces 'Lys-48'-linked ubiquitination of UBR2, leading to its proteasomal degradation by SCF E3 ubiquitin-protein ligase complex (PubMed : 38225265).
See full target information UBR2

Publications (6)

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

The Journal of biological chemistry 301:110449 PubMed40615042

2025

Targeted degradation of α-synuclein by arginine-based PROTACs.

Applications

Unspecified application

Species

Unspecified reactive species

Linjing Shen,Jianchao Zhang,Zhaoran Wang,Yaxuan Liu,Shengjin Cui,Hai Rao

Nature communications 16:4491 PubMed40368919

2025

Inherited deficiency of DIAPH1 identifies a DNA double strand break repair pathway regulated by γ-actin.

Applications

Unspecified application

Species

Unspecified reactive species

Beth L Woodward,Sudipta Lahiri,Anoop S Chauhan,Marcos Rios Garcia,Lucy E Goodley,Thomas L Clarke,Mohinder Pal,Angelo Agathanggelou,Satpal S Jhujh,Anil N Ganesh,Fay M Hollins,Valentina Galassi Deforie,Reza Maroofian,Stephanie Efthymiou,Andrea Meinhardt,Christopher G Mathew,Michael A Simpson,Heather C Mefford,Eissa A Faqeih,Sergio D Rosenzweig,Stefano Volpi,Gigliola Di Matteo,Caterina Cancrini,Annarita Scardamaglia,Fiona Shackley,E Graham Davies,Shahnaz Ibrahim,Peter D Arkwright,Maha S Zaki,Tatjana Stankovic,A Malcolm R Taylor,Antonina J Mazur,Nataliya Di Donato,Henry Houlden,Eli Rothenberg,Grant S Stewart

Cell reports 44:115434 PubMed40131931

2025

SOD2 is a regulator of proteasomal degradation promoting an adaptive cellular starvation response.

Applications

Unspecified application

Species

Unspecified reactive species

Nurul Khalida Ibrahim,Sabine Schreek,Buesra Cinar,Anna Sophie Stasche,Su Hyun Lee,Andre Zeug,Tim Dolgner,Julia Niessen,Evgeni Ponimaskin,Halyna Shcherbata,Beate Fehlhaber,Jean-Pierre Bourquin,Beat Bornhauser,Martin Stanulla,Andreas Pich,Alejandro Gutierrez,Laura Hinze

Autophagy 21:1019-1038 PubMed39723606

2024

Regulation of N-degron recognin-mediated autophagy by the SARS-CoV-2 PLpro ubiquitin deconjugase.

Applications

Unspecified application

Species

Unspecified reactive species

Carlos Ayala-Torres,Jiangnan Liu,Nico P Dantuma,Maria G Masucci

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 12:e2404107 PubMed39555688

2024

WAC Facilitates Mitophagy-mediated MSC Osteogenesis and New Bone Formation via Protecting PINK1 from Ubiquitination-Dependent Degradation.

Applications

Unspecified application

Species

Unspecified reactive species

Shuai Fan,Jinteng Li,Guan Zheng,Ziyue Ma,Xiaoshuai Peng,Zhongyu Xie,Wenjie Liu,Wenhui Yu,Jiajie Lin,Zepeng Su,Peitao Xu,Peng Wang,Yanfeng Wu,Huiyong Shen,Guiwen Ye

Nature communications 14:6774 PubMed37891180

2023

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.

Applications

Unspecified application

Species

Unspecified reactive species

Sylvia Varland,Rui Duarte Silva,Ine Kjosås,Alexandra Faustino,Annelies Bogaert,Maximilian Billmann,Hadi Boukhatmi,Barbara Kellen,Michael Costanzo,Adrian Drazic,Camilla Osberg,Katherine Chan,Xiang Zhang,Amy Hin Yan Tong,Simonetta Andreazza,Juliette J Lee,Lyudmila Nedyalkova,Matej Ušaj,Alexander J Whitworth,Brenda J Andrews,Jason Moffat,Chad L Myers,Kris Gevaert,Charles Boone,Rui Gonçalo Martinho,Thomas Arnesen
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