Hyaluronan mediated motility receptor (165-173)

Hyaluronan mediated motility receptor (165-173) is a synthetic peptide fragment derived from the hyaluronan-mediated motility receptor (HMMR), a protein implicated in cell motility, cell division, and interactions with the extracellular matrix. As a defined peptide sequence corresponding to residues 165 through 173 of HMMR, it serves as a valuable research tool for investigating the molecular mechanisms governing cell migration, signaling pathways, and protein-protein interactions involving hyaluronan and its binding partners. The unique sequence and structural features of this peptide provide a focused approach for dissecting the functional domains of HMMR and their roles in cellular processes relevant to tissue remodeling, development, and disease models.

Peptide-protein interaction studies: The 165-173 fragment of HMMR is widely utilized to probe specific binding interactions between hyaluronan and its receptor, as well as to map domains critical for receptor-ligand recognition. By employing this peptide in binding assays, researchers can delineate the contribution of this motif to hyaluronan affinity and receptor specificity, thereby clarifying the molecular determinants of extracellular matrix engagement and downstream signaling events. Such studies enhance the understanding of cell adhesion and migration mechanisms at a molecular level.

Signal transduction research: As a functional segment of HMMR, this peptide is instrumental in dissecting intracellular signaling cascades initiated by hyaluronan binding. It is commonly applied in cell-based assays and biochemical systems to evaluate its impact on the activation of signaling pathways such as ERK, PI3K/Akt, or Rho GTPases, which are central to motility and cytoskeletal reorganization. The ability to introduce this defined sequence allows for targeted interrogation of pathway modulation and the identification of sequence-specific effects on cellular responses.

Peptide inhibitor design and screening: The defined sequence of the 165-173 region enables its use as a template for developing peptide-based inhibitors or mimetics that modulate HMMR function. By incorporating this fragment into competitive binding or functional screening assays, researchers can assess its capacity to block hyaluronan-receptor interactions, thereby informing the design of novel molecular tools or probes. Such applications are critical for the validation of therapeutic targets and the exploration of structure-activity relationships within the HMMR protein family.

Structural and conformational analysis: The peptide serves as a model system for studying the secondary structure and conformational dynamics of HMMR functional domains. Through techniques such as NMR spectroscopy, circular dichroism, or molecular modeling, investigators can elucidate the folding properties and structural motifs present within the 165-173 region. These insights contribute to a deeper understanding of how structural features correlate with receptor activity and biological function.

Antibody epitope mapping: The HMMR (165-173) peptide is frequently employed as an epitope in immunological studies aimed at generating or characterizing antibodies specific to this domain. By using the peptide as an immunogen or as a probe in binding assays, researchers can map antibody recognition sites, validate antibody specificity, and develop reagents for detecting HMMR expression in various experimental systems. This application supports the development of highly selective immunoassays and enhances the precision of analytical tools used in cell biology and molecular research.

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