39S ribosomal protein L34, mitochondrial (58-66)

39S ribosomal protein L34, mitochondrial

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: ta-070

Synonyms/Alias:39S ribosomal protein L34, mitochondrial (58-66)

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  • IND and NDA support
  • Drug master files (DMF) filing
Sequence
IKRKNKHGW
Areas of Interest
Antigen-presenting Cells; Cancer Research

39S ribosomal protein L34, mitochondrial (58-66) is a synthetic peptide fragment derived from the mitochondrial ribosomal protein L34, specifically encompassing amino acid residues 58 to 66. As a segment of the mitochondrial large ribosomal subunit, this peptide is of significant interest in mitochondrial biology, protein synthesis research, and studies of ribosomal structure and function. Its defined sequence and origin from a key mitochondrial ribosomal protein make it a valuable tool for probing the molecular mechanisms underlying mitochondrial translation and the biogenesis of mitochondrial ribosomes. Researchers utilize such peptide fragments to dissect protein-protein interactions, investigate post-translational modifications, and develop analytical methods relevant to mitochondrial function and pathology.

Peptide mapping: The 39S ribosomal protein L34, mitochondrial (58-66) fragment serves as a precise standard for peptide mapping experiments aimed at characterizing mitochondrial ribosomal proteins. By enabling the identification and confirmation of peptide sequences within larger protein digests, it supports mass spectrometry-based proteomic workflows. This application is particularly valuable for validating protein expression, monitoring post-translational modifications, and ensuring the accuracy of mitochondrial ribosomal protein identification in complex biological samples.

Antibody generation: As an antigenic determinant, this peptide fragment can be employed to generate sequence-specific antibodies against the mitochondrial ribosomal protein L34. These antibodies are instrumental in immunodetection assays such as Western blotting, immunoprecipitation, and immunofluorescence, facilitating the study of protein localization, expression dynamics, and interaction networks within mitochondria. The use of a well-defined peptide epitope enhances the specificity and sensitivity of antibody-based detection strategies.

Protein interaction studies: The defined sequence of this peptide enables its use in in vitro assays designed to probe protein-protein interactions involving mitochondrial ribosomal proteins. By serving as a binding partner or competitive inhibitor in affinity assays, it helps elucidate the molecular interfaces governing ribosome assembly, stability, and function. Insights gained from such studies contribute to a deeper understanding of mitochondrial translation regulation and the coordination of ribosomal components.

Structural analysis: Synthetic peptides like this mitochondrial L34 fragment are valuable in structural biology, providing model systems for high-resolution techniques such as nuclear magnetic resonance (NMR) spectroscopy or X-ray crystallography. Researchers utilize these defined fragments to investigate secondary structure propensities, folding behaviors, and conformational dynamics, which inform on the structural features critical to ribosomal protein function and ribosome assembly within mitochondria.

Analytical method development: The availability of a synthetic peptide corresponding to a specific region of a mitochondrial ribosomal protein supports the development and validation of analytical methods for mitochondrial proteomics. It can be used as a calibration standard, internal control, or spike-in reference in quantitative assays, ensuring robust performance of liquid chromatography-mass spectrometry (LC-MS) workflows. Such applications enhance the reproducibility, sensitivity, and accuracy of mitochondrial protein quantification in both basic and applied research contexts.

Source#
Homo sapiens (human)
Epitope
58-66
Restricting HLA
HLA-A2
References
Ramila Philip; J Proteome Res 2007

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