Insulin-like growth factor-II mRNA binding protein 3 (515-523)

Insulin-like growth factor-II mRNA binding protein 3 (515-523) is a synthetic peptide fragment corresponding to amino acids 515 through 523 of the IGF2BP3 protein, a well-characterized RNA-binding protein involved in the post-transcriptional regulation of gene expression. This peptide sequence is derived from a biologically significant region of IGF2BP3, which has been implicated in the modulation of mRNA stability, localization, and translational control, particularly in the context of cellular growth, differentiation, and development. The availability of this defined peptide fragment enables researchers to investigate the functional domains of IGF2BP3, dissect protein-protein or protein-RNA interactions, and explore the molecular mechanisms underlying RNA regulatory networks.

Epitope mapping: The 515-523 peptide serves as a valuable tool for epitope mapping studies, allowing researchers to identify and characterize antibody binding sites within the IGF2BP3 protein. By employing this peptide in immunoassays such as ELISA or Western blotting, investigators can determine the specificity of monoclonal or polyclonal antibodies, validate antibody reagents for research use, and facilitate the development of highly selective immunodetection protocols targeting IGF2BP3 or its associated protein complexes.

Protein-protein interaction analysis: The defined sequence of this peptide enables its use in probing direct and indirect interactions between IGF2BP3 and other cellular proteins. By incorporating the peptide into pull-down assays, surface plasmon resonance experiments, or other biophysical binding studies, researchers can elucidate the binding affinities, interaction partners, and functional consequences of domain-specific contacts. Such analyses contribute to a deeper understanding of the modular architecture of IGF2BP3 and its role in multimeric protein assemblies.

Peptide-based inhibitor screening: The 515-523 fragment can be utilized as a competitive ligand or template in high-throughput screening platforms designed to identify small molecules or peptides that modulate IGF2BP3 activity. By mimicking a functional domain of the full-length protein, the peptide provides a molecular scaffold for evaluating the efficacy of candidate inhibitors, mapping inhibitory epitopes, and guiding structure-activity relationship studies aimed at dissecting the regulatory mechanisms of IGF2BP3-mediated mRNA binding.

Phosphorylation and post-translational modification studies: As the IGF2BP3 protein is subject to complex regulation through post-translational modifications, synthetic peptides corresponding to specific regions such as 515-523 facilitate detailed investigations into phosphorylation events or other covalent modifications. Researchers can employ this peptide in kinase assays, mass spectrometry workflows, or antibody development efforts to monitor modification status, map modification sites, and assess the impact of such changes on protein function.

Immunogenicity assessment: The 515-523 peptide may be used to evaluate the immunogenic potential of specific IGF2BP3 regions in animal models or in vitro immune assays. Such studies are relevant for the generation and characterization of peptide-specific antibodies, the assessment of immune responses to defined protein segments, and the optimization of antigen design for research applications. By leveraging the unique sequence of this peptide, investigators can systematically explore the immunological properties of IGF2BP3 and its relevance in various biological contexts.

1. Oleic acid and glucose regulate glucagon-like peptide 1 receptor expression in a rat pancreatic ductal cell line

2. The spatiotemporal control of signalling and trafficking of the GLP-1R

3. TMEM16F and dynamins control expansive plasma membrane reservoirs

4. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

5. Application of human liver organoids as a patient-derived primary model for HBV infection and related hepatocellular carcinoma