CXCL9(74-103) is a chemokine-derived peptide fragment retaining a key stretch of residues involved in receptor engagement and structural stabilization. Its sequence includes charged, polar, and aromatic components that influence β-sheet and loop formation typical of CXC chemokines. Researchers examine its conformational behavior using spectroscopic and computational tools. Applications include chemokine-receptor interaction studies, immune-signaling modeling, and motif-function analysis.
CAT No: R2795
CXCL9(74-103) is a synthetic peptide fragment corresponding to amino acids 74 through 103 of the human chemokine CXCL9, also known as monokine induced by gamma interferon (MIG). As a CXC chemokine, CXCL9 is involved in the regulation of immune cell trafficking, particularly the recruitment and activation of T lymphocytes via interaction with the CXCR3 receptor. The 74-103 fragment represents a functionally significant region of the full-length protein and is commonly utilized in studies probing chemokine-receptor interactions, immune modulation, and peptide structure-activity relationships. Its defined sequence and biochemical stability make it a valuable research tool for elucidating specific aspects of chemokine biology and peptide-mediated signaling.
Receptor Binding Studies: The CXCL9(74-103) peptide is widely employed in investigations of chemokine receptor interactions, particularly with CXCR3. By isolating this C-terminal segment, researchers can dissect the binding determinants responsible for receptor specificity and affinity. Such studies facilitate a deeper understanding of how truncated or modified chemokine fragments influence receptor activation, providing critical insights for mapping functional domains and designing receptor-targeted ligands.
Peptide Structure-Activity Relationship Analysis: In the context of peptide chemistry and molecular pharmacology, this fragment serves as a model system for structure-activity relationship (SAR) studies. Examining the biological and physicochemical properties of the 74-103 region allows for the identification of key residues that contribute to chemotactic activity, stability, or receptor engagement. Through systematic substitution or modification of amino acids within this sequence, researchers can delineate the structural features essential for activity, supporting the rational design of chemokine analogs or inhibitors.
Immunological Mechanism Elucidation: CXCL9(74-103) is frequently utilized to probe immune cell migration and activation pathways in vitro. By applying the peptide to cultured T cells or other immune populations, investigators can analyze downstream signaling events, cytokine release, and cellular responses triggered by chemokine engagement. These studies enable the dissection of molecular mechanisms underlying leukocyte recruitment and the role of chemokine fragments in modulating immune responses, advancing the field of immunology research.
Peptide-Based Assay Development: The defined sequence and biological relevance of CXCL9(74-103) make it suitable for use as a standard or probe in diverse biochemical assays. It can be incorporated into binding assays, competitive inhibition formats, or functional migration assays to evaluate the activity of chemokine receptors, screen for antagonists, or validate assay performance. The peptide's application in assay development supports high-throughput screening and mechanistic studies in academic and industrial research settings.
Synthetic Peptide Engineering: As a representative fragment of a biologically active chemokine, CXCL9(74-103) provides a template for synthetic modifications and peptide engineering efforts. Researchers leverage this sequence to generate analogs with altered receptor affinity, stability, or immunomodulatory properties, enabling the exploration of novel chemokine-based tools or probes. The peptide's modular nature supports the development of innovative reagents for biochemical, pharmacological, and immunological investigations, contributing to the advancement of peptide science and chemokine research.
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