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AB230922

Anti-HTF9C/TRMT2A antibody [1G8]

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(1 Publication)

Mouse Monoclonal HTF9C/TRMT2A antibody. Suitable for IHC-P, WB and reacts with Human, Transfected cell lysate samples. Cited in 1 publication. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human TRMT2A.

View Alternative Names

tRNA (uracil-5-)-methyltransferase homolog A, mRNA (uracil-5-)-methyltransferase TRMT2A, TRMT2A

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HTF9C/TRMT2A antibody [1G8] (AB230922)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-HTF9C/TRMT2A antibody [1G8] (AB230922)

Formalin-fixed, paraffin-embedded human testis tissue stained for HTF9C/TRMT2A using ab230922 at 10 μg/ml in immunohistochemical analysis.

Western blot - Anti-HTF9C/TRMT2A antibody [1G8] (AB230922)
  • WB

Supplier Data

Western blot - Anti-HTF9C/TRMT2A antibody [1G8] (AB230922)

All lanes:

Western blot - Anti-HTF9C/TRMT2A antibody [1G8] (ab230922) at 1/2000 dilution

Lane 1:

pCMV6-ENTRY control-transfected HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate at 5 µg

Lane 2:

pCMV6-ENTRY HTF9C/TRMT2A-transfected HEK-293T whole cell lysate at 5 µg

Predicted band size: 69 kDa

true

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

1G8

Isotype

IgG1

Carrier free

No

Applications

IHC-P, WB

applications

Immunogen

Recombinant Full Length Protein corresponding to Human TRMT2A.

Q8IZ69

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "10 µg/mL", "IHCP-species-notes": "<p></p>", "WB-species-checked": "guaranteed", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Transfected cell lysate": { "IHCP-species-checked": "notRecommended", "IHCP-species-dilution-info": "", "IHCP-species-notes": "", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2000", "WB-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A/G
Storage buffer
Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 1% BSA
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.

HTF9C also known as TRMT2A is a tRNA methyltransferase enzyme with a mass of approximately 57 kDa. Its primary function is to catalyze the methylation of tRNA specifically the modification of uridine at position 54 to 5-methyluridine. This modification is essential for maintaining the correct structure and function of tRNA which affects protein synthesis. The protein is ubiquitously expressed in various tissues suggesting it plays an important role in fundamental cellular processes.
Biological function summary

The enzyme influences accurate tRNA function affecting overall protein translation efficiency. HTF9C/TRMT2A contributes to the maturation of tRNA molecules an important step in the stability and proper functioning of the translation machinery. Although it functions largely as an independent enzyme it may transiently interact with other proteins in the tRNA modification pathway indicating its potential involvement in broader RNA processing complexes.

Pathways

HTF9C/TRMT2A plays a critical role in the tRNA modification pathway which is tightly linked to protein biosynthesis. Its function affects the fidelity of translation connecting it indirectly to the mTOR pathway which regulates cell growth and metabolism. The TRMT2A enzyme's activity is potentially interrelated with ribosomal proteins like RPLP0 which are important for the translation process reflecting its impact on cellular growth and proliferation.

Improper function of HTF9C/TRMT2A can contribute to the development of cancer due to dysregulated protein synthesis. Aberrant methylation patterns affecting tRNA can result in translation anomalies contributing to oncogenic transformation. Additionally its malfunction is thought to be connected to neurological disorders where precise protein translation is important for neural function. In these contexts HTF9C may interact with dysregulated proteins such as p53 involved in cell cycle control and tumor suppression further illustrating its role in disease mechanisms.
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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

S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine in tRNAs and some mRNAs (PubMed : 31361898, PubMed : 33799331, PubMed : 34556860). Mainly catalyzes the methylation of uridine at position 54 (m5U54) in cytosolic tRNAs (PubMed : 31361898, PubMed : 33799331). Also able to mediate the formation of 5-methyl-uridine in some mRNAs (PubMed : 34123281).
See full target information TRMT2A
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Publications (1)

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

Experimental hematology & oncology 12:4 PubMed36624493

2023

Alpha-B-Crystallin overexpression is sufficient to promote tumorigenesis and metastasis in mice.

Applications

Unspecified application

Species

Unspecified reactive species

Behnam Rashidieh,Amanda Louise Bain,Simon Manuel Tria,Sowmya Sharma,Cameron Allan Stewart,Jacinta Ley Simmons,Pirjo M Apaja,Pascal H G Duijf,John Finnie,Kum Kum Khanna
View all publications
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Product promise

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