C14orf49 protein (221-232)

C14orf49 protein (221-232) is a synthetic peptide corresponding to amino acid residues 221 through 232 of the human C14orf49 protein sequence. As a peptide fragment derived from a less-characterized open reading frame, it represents a valuable molecular tool for probing the structure, function, and biological interactions of the parent protein within cellular systems. The region encompassed by residues 221-232 may harbor structural motifs or functional determinants relevant to the activity or localization of C14orf49, making this peptide fragment particularly useful for research aiming to elucidate the molecular underpinnings of this protein's role in cellular physiology. Its defined sequence and manageable length facilitate diverse biochemical and analytical applications, supporting both targeted and exploratory studies in protein science.

Epitope mapping: The C14orf49 (221-232) peptide is well-suited for use in epitope mapping experiments, enabling researchers to define antibody recognition sites within the parent protein. By incorporating this peptide into immunoassays such as ELISA or Western blotting, investigators can assess antibody specificity and affinity for this particular region. This approach aids in the characterization of polyclonal or monoclonal antibodies generated against C14orf49, supporting the development of reliable immunological detection reagents for downstream applications in cell biology and proteomics.

Protein interaction studies: As a discrete segment of the C14orf49 sequence, this peptide can be employed in binding assays to investigate potential interaction partners that recognize the 221-232 motif. Pull-down assays, peptide arrays, or surface plasmon resonance experiments utilizing this fragment can reveal direct binding events with other proteins, nucleic acids, or small molecules. Such studies contribute to the identification of molecular networks and signaling pathways involving C14orf49, providing mechanistic insights into its cellular functions.

Phosphorylation and post-translational modification analysis: The defined sequence of the (221-232) peptide allows for targeted investigation of post-translational modifications, such as phosphorylation, that may occur within this region of C14orf49. Synthetic peptides serve as effective substrates in in vitro kinase assays or mass spectrometry-based workflows, facilitating the identification and characterization of modification sites. This application supports efforts to unravel regulatory mechanisms that modulate C14orf49 activity and its integration into broader signaling cascades.

Structural and conformational studies: The C14orf49 (221-232) peptide provides a tractable model for biophysical analyses aimed at deciphering the secondary structure or folding propensity of this protein segment. Techniques such as circular dichroism spectroscopy, NMR, or X-ray crystallography can be applied to the peptide to gain insights into local structural features. These data inform broader structural studies of the full-length protein, guiding mutagenesis strategies or functional assays targeting this region.

Peptide-based assay development: Owing to its defined sequence and biochemical relevance, the peptide is a suitable standard or reagent in the development and optimization of quantitative assays. It can serve as a calibration standard in mass spectrometry workflows or as a positive control in immunoassays, ensuring assay reliability and reproducibility. Such applications are critical for advancing quantitative proteomics, biomarker discovery, and the validation of analytical platforms in basic and translational research settings.

1. Crystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural Features

2. Uncarboxylated osteocalcin decreases insulin-stimulated glucose uptake without affecting insulin signaling and regulators of mitochondrial biogenesis in myotubes

3. C-peptide and its C-terminal fragments improve erythrocyte deformability in type 1 diabetes patients

4. Cationic cell-penetrating peptides are potent furin inhibitors

5. The effect of B-type allatostatin neuropeptides on crosstalk between the insect immune response and cold tolerance