TRMT2A Recombinant Monoclonal Antibody

TRMT2A is a tRNA methyltransferase that catalyzes the formation of 5-methyluridine at specific positions in tRNA molecules, playing a fundamental role in post-transcriptional RNA modification. This enzyme, homologous to yeast TRM2, contributes to tRNA stability and translational fidelity, making it a relevant target for researchers investigating epitranscriptomic regulation and its connections to cellular function and disease states.

This recombinant monoclonal antibody, clone 5B1, offers the reproducibility and consistency that demanding experimental workflows require. Because it is generated from a defined sequence and produced in a controlled recombinant system, researchers can expect uniform performance across different lots, eliminating the variability often encountered with traditional hybridoma-derived antibodies. The rabbit IgG format and affinity-chromatography purification ensure high specificity for human TRMT2A.

Validation studies demonstrate reliable performance across multiple applications. In western blot analysis, the antibody detects TRMT2A in both MCF7 and HeLa whole cell lysates at dilutions ranging from 1:500 to 1:5000. The observed band appears at approximately 75 kDa, slightly higher than the predicted 69 kDa molecular weight, which likely reflects post-translational modifications such as glycosylation or other cellular processing events. Immunohistochemistry studies confirm robust staining in paraffin-embedded human stomach tissue and liver cancer specimens at 1:100 dilution using standard citrate buffer antigen retrieval. Additionally, immunofluorescence analysis in HeLa cells reveals clear cytoplasmic and nuclear localization patterns when counterstained with DAPI.

For researchers exploring epigenetics, nuclear signaling, or RNA modification biology, this antibody provides a versatile tool compatible with protein detection, tissue localization, and cellular imaging studies in human samples.