Obtustatin is a highly potent and selective inhibitor of the binding of α1β1 integrin to collagen IV, however, does not show inhibitory activity toward other integrins, including α2β1, αIIbβ3, αvβ3, α4β1, α5β1, α6β1, and α9β1, α4β7 integrins. It displays antitumor efficacy.
CAT No: R0985
Obtustatin is a disintegrin peptide originally isolated from the venom of the Vipera lebetina obtusa snake, recognized for its capacity to selectively inhibit integrin function. As a member of the disintegrin family, it features a distinctive amino acid sequence that enables precise interaction with integrin α1β1, a collagen-binding receptor crucial to various cellular adhesion and migration processes. Its specificity and high affinity for this integrin subtype have positioned obtustatin as a valuable biochemical tool for dissecting integrin-mediated mechanisms in cell biology, vascular research, and extracellular matrix studies. The compound's well-characterized structure and functional selectivity make it a preferred reagent for researchers investigating cell-matrix interactions and the molecular basis of integrin signaling.
Integrin inhibition studies: Obtustatin is widely employed in integrin inhibition assays, particularly for elucidating the roles of α1β1 integrin in cell adhesion, migration, and signaling. By competitively binding to integrin receptors, it disrupts the interaction between cells and collagen substrates, enabling researchers to investigate the downstream effects of integrin blockade in various cellular contexts. Such studies are critical for understanding the molecular pathways governing tissue remodeling, angiogenesis, and cell motility, especially in models where integrin α1β1 is implicated.
Extracellular matrix research: The peptide's selectivity for collagen-binding integrins makes it an effective probe in extracellular matrix (ECM) biology. It is frequently utilized to dissect the contributions of specific integrins to cell-ECM adhesion, matrix remodeling, and the regulation of cellular phenotype in response to microenvironmental cues. By modulating cell attachment and signaling, obtustatin assists in clarifying the complex interplay between ECM components and integrin receptors, facilitating studies on tissue development, fibrosis, and wound healing at the molecular level.
Angiogenesis modeling: In vitro and ex vivo angiogenesis assays often incorporate obtustatin to selectively inhibit endothelial cell interactions with collagen, thereby assessing the impact of integrin α1β1 on new blood vessel formation. Its application in these models enables precise evaluation of the integrin's role in endothelial cell migration, tube formation, and vascular stability. Such targeted inhibition is instrumental in distinguishing integrin-dependent mechanisms from other regulatory factors in angiogenic processes.
Peptide-functional studies: As a structurally defined disintegrin, obtustatin serves as a reference molecule in peptide structure-activity relationship (SAR) analyses and integrin-binding studies. Researchers utilize it to benchmark the activity of synthetic peptide analogs, assess the impact of sequence modifications, and explore the determinants of integrin selectivity. These investigations contribute to the broader understanding of peptide-based modulation of protein-protein interactions and inform the design of novel integrin-targeting compounds.
Cell signaling pathway analysis: The ability of obtustatin to modulate integrin engagement provides a valuable means to study downstream signaling cascades activated by cell-matrix adhesion. By selectively disrupting integrin-mediated signaling, investigators can delineate the roles of pathways such as focal adhesion kinase (FAK), MAPK, and PI3K in cellular responses to the extracellular environment. This approach enhances mechanistic insights into how integrin interactions influence cell survival, proliferation, and differentiation, supporting advanced research in cell biology and molecular signaling.
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