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AB229351

Anti-TRUB1 antibody

1

(1 Review)

|

(1 Publication)

Rabbit Polyclonal TRUB1 antibody. Suitable for ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human TRUB1.

View Alternative Names

PUS4, TRUB1, Pseudouridylate synthase TRUB1, TruB pseudouridine synthase homolog 1, tRNA pseudouridine 55 synthase TRUB1, Psi55 synthase TRUB1

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-TRUB1 antibody (AB229351)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-TRUB1 antibody (AB229351)

NT2/D1 cells stained for TRUB1 (green) using ab229351 (1/500 dilution) in ICC/IF. Cells were fixed in 4% paraformaldehyde at RT for 15 minutes.

Nuclear counterstain : Hoechst 33342 (blue).

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF

applications

Immunogen

Recombinant Fragment Protein within Human TRUB1. The exact immunogen used to generate this antibody is proprietary information.

Q8WWH5

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/100 - 1/1000", "ICCIF-species-notes": "<p></p>" }, "Mouse": { "ICCIF-species-checked": "predicted", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "" }, "Rat": { "ICCIF-species-checked": "predicted", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "" }, "Rhesus monkey": { "ICCIF-species-checked": "predicted", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS, 20% Glycerol (glycerin, glycerine)
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
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

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

TRUB1 also known as TruB pseudouridine synthase family member 1 is an enzyme with a molecular mass of approximately 58 kDa. It is primarily involved in the pseudouridylation of RNA molecules which is a process where uridine residues in RNA are converted to pseudouridine. This protein shows expression in various tissues with notable presence in the nucleolus of eukaryotic cells where it performs its functions on RNA. TRUB1 has homologs across different species indicating a conserved role in RNA processing.
Biological function summary

TRUB1 interacts with components of the ribonucleoprotein complex playing a role in the maturation and structural modification of ribosomal RNA. This modification helps improve the stability and functionality of RNA molecules enhancing their ability to participate in translation. TRUB1 achieves its function by recognizing specific sequences in RNA substrate and performing the enzymatic conversion to pseudouridine thereby impacting RNA stability and translation fidelity across various cell types.

Pathways

RNA modifications where TRUB1 is involved play a critical role in cellular translation mechanisms. It participates in pathways that include the ribosome biogenesis pathway and RNA modification pathways. Other proteins that are part of these pathways such as dyskerin and fibrillarin share similar sites of action in the nucleolus and work collaboratively to support the proper formation of ribosomal RNA allowing TRUB1 to be intricately linked with these processes.

TRUB1 has been implicated in ribosomopathies which are disorders caused by defects in ribosome function and certain cancers where alteration in RNA processing pathways is observed. Its association with dyskerin another pseudouridine synthase highlights a potential connection to diseases like dyskeratosis congenita. These diseases manifest through defects in ribosome assembly and function where TRUB1's role in pseudouridylation may directly influence cellular protein synthesis contributing to the disease pathology.
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Product protocols

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

Pseudouridine synthase that catalyzes pseudouridylation of mRNAs and tRNAs (PubMed : 28073919, PubMed : 31477916, PubMed : 32926445). Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure (PubMed : 28073919, PubMed : 31477916). Constitutes the major pseudouridine synthase acting on mRNAs (PubMed : 28073919). Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs (PubMed : 32926445, PubMed : 33023933). Promotes the processing of pri-let-7 microRNAs (pri-miRNAs) independently of its RNA pseudouridylate synthase activity (PubMed : 32926445). Acts by binding to the stem-loop structure on pri-let-7, preventing LIN28-binding (LIN28A and/or LIN28B), thereby enhancing the interaction between pri-let-7 and the microprocessor DGCR8, which mediates miRNA maturation (PubMed : 32926445).
See full target information TRUB1
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Publications (1)

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

Nature communications 16:1313 PubMed39900921

2025

USP5 stabilizes YTHDF1 to control cancer immune surveillance through mTORC1-mediated phosphorylation.

Applications

Unspecified application

Species

Unspecified reactive species

Na Shao,Lei Xi,Yangfan Lv,Muhammad Idris,Lin Zhang,Ya Cao,Jingyi Xiang,Xi Xu,Belinda X Ong,Qiongyi Zhang,Xu Peng,Xiaoyan Yue,Feng Xu,Chungang Liu
View all publications
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