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AB134902

Anti-NOP10 antibody [EPR8857]

5

(2 Reviews)

|

(11 Publications)

Rabbit Recombinant Monoclonal NOP10 antibody. Suitable for IHC-P, WB and reacts with Human, Mouse, Rat samples. Cited in 11 publications.

View Alternative Names

NOLA3, NOP10, H/ACA ribonucleoprotein complex subunit 3, Nucleolar protein 10, Nucleolar protein family A member 3, snoRNP protein NOP10

4 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-NOP10 antibody [EPR8857] (AB134902)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-NOP10 antibody [EPR8857] (AB134902)

Immunohistochemical analysis of paraffin-embedded Human kidney tissue labelling NOP10 with ab134902 at 1/250 dilution.

Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-NOP10 antibody [EPR8857] (AB134902)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-NOP10 antibody [EPR8857] (AB134902)

Immunohistochemical analysis of paraffin-embedded Human breast tissue labelling NOP10 with ab134902 at 1/250 dilution.

Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.

Western blot - Anti-NOP10 antibody [EPR8857] (AB134902)
  • WB

Unknown

Western blot - Anti-NOP10 antibody [EPR8857] (AB134902)

All lanes:

Western blot - Anti-NOP10 antibody [EPR8857] (ab134902) at 1/10000 dilution

Lane 1:

293T (Human embryonic kidney epithelial cell) cell lysate at 10 µg

Lane 2:

HeLa cell lysate at 10 µg

Lane 3:

Jurkat cell lysate at 10 µg

Lane 4:

HuT-78 cell lysate at 10 µg

Lane 5:

Caco 2 cell lysate at 10 µg

Secondary

All lanes:

HRP-conjugated goat anti-rabbit polyclonal IgG at 1/2000 dilution

Predicted band size: 7 kDa

Observed band size: 8 kDa

false

OI-RD Scanning - Anti-NOP10 antibody [EPR8857] (AB134902)
  • OI-RD Scanning

Unknown

OI-RD Scanning - Anti-NOP10 antibody [EPR8857] (AB134902)

We have systematically measured KD (the equilibrium dissociation constant between the antibody and its antigen), of more than 840 recombinant antibodies to assess not only their individual KD values but also to see the average affinity of antibody. Based on the comparison with published literature values for mouse monoclonal antibodies, Recombinant antibodies appear to be on average 1-2 order of magnitude higher affinity.

  • Carrier free

    Anti-NOP10 antibody [EPR8857] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR8857

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

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

NOP10 also known as Nucleolar Protein 10 is a small protein component with a molecular weight of approximately 7 kDa. It is an essential part of the H/ACA ribonucleoprotein complexes responsible for guiding the isomerization of uridine to pseudouridine in ribosomal RNA (rRNA). NOP10 is expressed in the nucleolus where it interacts closely with other core proteins such as NHP2 NOP58 and the catalytic subunit dyskerin also known as DKC1.
Biological function summary

NOP10 plays a critical role in ribosome biogenesis by taking part in H/ACA snoRNP complexes that facilitate the processing and modification of rRNA which is necessary for proper ribosome function. The protein forms a complex with the other core proteins and small nucleolar RNAs (snoRNAs) essential for the chemical alteration and folding of rRNA. By supporting the formation and stability of these complexes NOP10 ensures the fidelity of ribosomal assembly and cellular protein synthesis.

Pathways

The protein contributes significantly to the ribosome biogenesis and RNA modification pathways. It directly influences the ribosome biogenesis process which determines the production of ribosomes essential for protein translation in cells. In this pathway NOP10 interacts with proteins such as GAR1 and dyskerin which assist in assembling the complete ribosomal subunits. These interactions help sustain the delicate balance of rRNA modifications required for functional ribosome activity during protein synthesis.

NOP10 is associated with conditions like dyskeratosis congenita and some forms of cancer. Dyskeratosis congenita a genetic disorder characterized by bone marrow failure and skin abnormalities is linked to mutations in components of the H/ACA snoRNP complex including NOP10. In cancer altered expression or functionality of NOP10 can influence the process of ribosome biogenesis leading to increased cellular proliferation. Dyskerin another key member of the complex is also implicated in these conditions highlighting the intertwined role of these proteins in maintaining cellular homeostasis and their potential disruption in disease states.

Product protocols

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

Target data

Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA (PubMed : 32554502). This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.
See full target information NOP10

Publications (11)

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

Genome biology 26:39 PubMed40001124

2025

Mapping snoRNA-target RNA interactions in an RNA-binding protein-dependent manner with chimeric eCLIP.

Applications

Unspecified application

Species

Unspecified reactive species

Zhuoyi Song,Bongmin Bae,Simon Schnabl,Fei Yuan,Thareendra De Zoysa,Maureen V Akinyi,Charlotte A Le Roux,Karine Choquet,Amanda J Whipple,Eric L Van Nostrand

Human molecular genetics 32:2901-2912 PubMed37440454

2023

Novel pathological variants of NHP2 affect N-terminal domain flexibility, protein stability, H/ACA Ribonucleoprotein (RNP) complex formation and telomerase activity.

Applications

Unspecified application

Species

Unspecified reactive species

Bartosz Maliński,Jacopo Vertemara,Elena Faustini,Claes Ladenvall,Anna Norberg,Yuming Zhang,Eleonore von Castelmur,Panagiotis Baliakas,Renata Tisi,Jörg Cammenga,Francisca Lottersberger

Nucleic acids research 51:3357-3374 PubMed36869663

2023

Proteomic analyses reveal new features of the box H/ACA RNP biogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Florence Schlotter,Salim Mérouani,Justine Flayac,Valentyne Kogey,Amani Issa,Maxime Dodré,Alexandra Huttin,Christiane Branlant,Edouard Bertrand,Stéphane Labialle,Franck Vandermoere,Céline Verheggen,Séverine Massenet

Cells 11: PubMed36497038

2022

Evidences for Mutant Huntingtin Inducing Musculoskeletal and Brain Growth Impairments via Disturbing Testosterone Biosynthesis in Male Huntington Disease Animals.

Applications

Unspecified application

Species

Unspecified reactive species

Libo Yu-Taeger,Arianna Novati,Jonasz Jeremiasz Weber,Elisabeth Singer-Mikosch,Ann-Sophie Pabst,Fubo Cheng,Carsten Saft,Jennifer Koenig,Gisa Ellrichmann,Taneli Heikkinen,Mahmoud A Pouladi,Olaf Riess,Huu Phuc Nguyen

iScience 24:103396 PubMed34825148

2021

Proteostasis regulated by testis-specific ribosomal protein RPL39L maintains mouse spermatogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Qianxing Zou,Lele Yang,Ruona Shi,Yuling Qi,Xiaofei Zhang,Huayu Qi

Cancers 13: PubMed34638246

2021

Analysis of Telomere Maintenance Related Genes Reveals as a New Metastatic-Risk Marker in Pheochromocytoma/Paraganglioma.

Applications

Unspecified application

Species

Unspecified reactive species

María Monteagudo,Paula Martínez,Luis J Leandro-García,Ángel M Martínez-Montes,Bruna Calsina,Marta Pulgarín-Alfaro,Alberto Díaz-Talavera,Sara Mellid,Rocío Letón,Eduardo Gil,Manuel Pérez-Martínez,Diego Megías,Raúl Torres-Ruiz,Sandra Rodriguez-Perales,Patricia González,Eduardo Caleiras,Scherezade Jiménez-Villa,Giovanna Roncador,Cristina Álvarez-Escolá,Rita M Regojo,María Calatayud,Sonsoles Guadalix,Maria Currás-Freixes,Elena Rapizzi,Letizia Canu,Svenja Nölting,Hanna Remde,Martin Fassnacht,Nicole Bechmann,Graeme Eisenhofer,Massimo Mannelli,Felix Beuschlein,Marcus Quinkler,Cristina Rodríguez-Antona,Alberto Cascón,María A Blasco,Cristina Montero-Conde,Mercedes Robledo

EMBO reports 22:e50684 PubMed33852194

2021

The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Hyunju Ryu,Xiao-Xin Sun,Yingxiao Chen,Yanping Li,Xiaoyan Wang,Roselyn S Dai,Hong-Ming Zhu,John Klimek,Larry David,Lev M Fedorov,Yoshiaki Azuma,Rosalie C Sears,Mu-Shui Dai

Molecular and cellular biology 41: PubMed33526451

2021

SUMOylation- and GAR1-Dependent Regulation of Dyskerin Nuclear and Subnuclear Localization.

Applications

Unspecified application

Species

Unspecified reactive species

D E MacNeil,P Lambert-Lanteigne,J Qin,F P McManus,E Bonneil,P Thibault,C Autexier

Proceedings of the National Academy of Sciences of 117:15137-15147 PubMed32554502

2020

Pseudouridylation defect due to and mutations causes nephrotic syndrome with cataracts, hearing impairment, and enterocolitis.

Applications

Unspecified application

Species

Unspecified reactive species

Eszter Balogh,Jennifer C Chandler,Máté Varga,Mona Tahoun,Dóra K Menyhárd,Gusztáv Schay,Tomas Goncalves,Renáta Hamar,Regina Légrádi,Ákos Szekeres,Olivier Gribouval,Robert Kleta,Horia Stanescu,Detlef Bockenhauer,Andrea Kerti,Hywel Williams,Veronica Kinsler,Wei-Li Di,David Curtis,Maria Kolatsi-Joannou,Hafsa Hammid,Anna Szőcs,Kristóf Perczel,Erika Maka,Gergely Toldi,Florentina Sava,Christelle Arrondel,Magdolna Kardos,Attila Fintha,Ahmed Hossain,Felipe D'Arco,Mario Kaliakatsos,Jutta Koeglmeier,William Mifsud,Mariya Moosajee,Ana Faro,Eszter Jávorszky,Gábor Rudas,Marwa H Saied,Salah Marzouk,Kata Kelen,Judit Götze,George Reusz,Tivadar Tulassay,François Dragon,Géraldine Mollet,Susanne Motameny,Holger Thiele,Guillaume Dorval,Peter Nürnberg,András Perczel,Attila J Szabó,David A Long,Kazunori Tomita,Corinne Antignac,Aoife M Waters,Kálmán Tory

Cell death & disease 11:238 PubMed32303682

2020

Biallelic mutations in WRAP53 result in dysfunctional telomeres, Cajal bodies and DNA repair, thereby causing Hoyeraal-Hreidarsson syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Sofie Bergstrand,Stefanie Böhm,Helena Malmgren,Anna Norberg,Mikael Sundin,Ann Nordgren,Marianne Farnebo
View all publications

Product promise

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