Similar to calgizzarin; similar to PID:g3115349 (40-49)

Similar to calgizzarin; similar to PID:g3115349 (40-49) is a synthetic peptide fragment modeled after a specific region of the human calgizzarin (S100A11) protein, corresponding to amino acids 40 to 49. Calgizzarin is a member of the S100 protein family, which is known for its role in calcium-binding and regulation of various cellular processes, including cell growth, differentiation, and intracellular signaling. By focusing on a defined peptide sequence, this analog provides a targeted tool for dissecting the structural and functional properties of the parent protein, enabling researchers to investigate the role of specific domains in protein-protein interactions, signaling pathways, and cellular physiology.

Peptide mapping: As a well-defined peptide fragment, this product serves as a valuable standard in peptide mapping studies. It can be employed to verify proteolytic cleavage sites or to confirm the identity of calgizzarin-derived peptides in mass spectrometry-based proteomic analyses. By matching the synthetic peptide's retention time and fragmentation pattern, researchers can confidently annotate peptide spectra and improve the accuracy of protein identification in complex biological samples.

Protein interaction research: This peptide is instrumental in probing the interaction interfaces of S100A11 with its binding partners. By incorporating the fragment into binding assays, surface plasmon resonance experiments, or pull-down studies, investigators can delineate the contribution of the 40-49 region to molecular recognition events. Such studies are essential for mapping functional epitopes, characterizing binding affinities, and understanding the molecular basis of calgizzarin-mediated signaling.

Antibody epitope characterization: The defined sequence of this peptide makes it an effective tool for antibody development and specificity testing. It can be used as an immunogen for generating sequence-specific antibodies, or as a competitive inhibitor in ELISA and immunoblot assays to confirm antibody binding to the target epitope. These approaches facilitate the validation of antibody reagents and support the development of sensitive and selective detection methods for S100A11.

Signal transduction studies: By introducing the peptide into cell-based or in vitro systems, researchers can assess its influence on calcium-dependent signaling pathways regulated by S100A11. The fragment may act as a competitive inhibitor or modulator of protein-protein interactions, enabling functional dissection of signaling cascades. Such experiments provide mechanistic insights into the role of specific calgizzarin domains in cellular calcium homeostasis and downstream responses.

Peptide structure-function analysis: The synthetic nature of the peptide allows for detailed biophysical and structural studies, such as circular dichroism spectroscopy or nuclear magnetic resonance analysis. These investigations can reveal the conformational properties of the 40-49 region, its propensity for secondary structure formation, and its stability under various conditions. Insights gained from such studies contribute to the broader understanding of S100 protein folding, domain organization, and functional dynamics.

1. Implications of ligand-receptor binding kinetics on GLP-1R signalling

2. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis

3. Spatiotemporal delivery of nanoformulated liraglutide for cardiac regeneration after myocardial infarction

4. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

5. cRGD-functionalized, DOX-conjugated, and 64Cu-labeled superparamagnetic iron oxide nanoparticles for targeted anticancer drug delivery and PET/MR imaging