LSKL, Inhibitor of Thrombospondin (TSP-1) is a peptide derived from the latency-associated peptide, inhibits thrombospondin (TSP-1) activation of TGF-β and prevents the progression of hepatic damage and fibrosis.
CAT No: R1490
CAS No:283609-79-0
Synonyms/Alias:283609-79-0;H-Leu-Ser-Lys-Leu-NH2;LSKL, Inhibitor of Thrombospondin (TSP-1);(2S)-6-amino-N-[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]-2-[[(2S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]hexanamide;H-Leu-Ser-Lys-Leu-NH2 trifluoroacetate salt;L-Leucyl-L-seryl-L-lysyl-L-leucinamide;LSKL-NH2;Leu-Ser-Lys-Leu peptide;leucyl-seryl-lysyl-leucyl peptide;LSKL;H-Leu-Ser-Lys-Leu-NH;TSP-1 inhibitor peptide LSKL;HY-P0299;Inhibitor of Thrombospondin ;TSP-1;AC-31401;DA-74214;FL109362;MS-28396;PD078448;Leu-Ser-Lys-Leu-NH2, >=95% (HPLC);G13182;LSKL, Inhibitor of Thrombospondin (TSP-1) (TFA) LSKL;
Chemical Name:(2S)-6-amino-N-[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]-2-[[(2S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]hexanamide
LSKL, Inhibitor of Thrombospondin TSP-1, is a synthetic tetrapeptide recognized for its role as a selective antagonist of thrombospondin-1 (TSP-1) mediated signaling. As a peptide compound, LSKL is widely utilized in biochemical and cell biology research to dissect the complex interactions between TSP-1 and its downstream effectors, particularly those involved in the regulation of transforming growth factor-beta (TGF-β) activation. Its defined sequence and inhibitory properties make it an indispensable tool for studies aiming to elucidate extracellular matrix dynamics, cell signaling pathways, and the modulation of cellular responses to environmental cues.
Signal transduction research: LSKL peptide serves as a valuable probe for investigating the molecular mechanisms underlying TSP-1-mediated activation of latent TGF-β. By competitively inhibiting the interaction between TSP-1 and the latency-associated peptide (LAP) of TGF-β, it allows researchers to delineate the specific contribution of TSP-1 in TGF-β signaling cascades. This application is particularly relevant for studies exploring the regulation of cellular proliferation, differentiation, and extracellular matrix remodeling, where TGF-β plays a pivotal role.
Fibrosis modeling: In experimental models of tissue fibrosis, the LSKL peptide is frequently utilized to assess the involvement of TSP-1-driven TGF-β activation in fibrotic progression. By attenuating TSP-1 activity, it provides a means to characterize the molecular events leading to excessive extracellular matrix deposition and fibroblast activation. This approach enables a more precise evaluation of antifibrotic strategies and the identification of key regulatory checkpoints within fibrogenic pathways.
Extracellular matrix biology: The use of LSKL as a TSP-1 inhibitor facilitates the study of extracellular matrix (ECM) composition and turnover, especially in systems where TSP-1 modulates matrix assembly and degradation. Researchers employ this peptide to investigate how TSP-1 influences collagen fibrillogenesis, matrix metalloproteinase activity, and cell-ECM interactions. Insights gained from these studies advance the understanding of tissue homeostasis, repair mechanisms, and pathological remodeling.
Cell culture and functional assays: In vitro, LSKL is incorporated into cell culture systems to modulate TSP-1-dependent cellular behaviors, including migration, adhesion, and differentiation. Its use allows for the controlled inhibition of TSP-1 signaling, enabling the dissection of autocrine and paracrine effects on various cell types. This application is particularly useful in studies of endothelial cells, fibroblasts, and immune cell populations where TSP-1 exerts regulatory influence.
Angiogenesis research: The peptide is also applied in angiogenesis assays to interrogate the role of TSP-1 in vascular development and remodeling. By blocking TSP-1 activity, LSKL enables the examination of endothelial cell proliferation, tube formation, and vessel stabilization in response to altered microenvironmental cues. This facilitates the identification of TSP-1-dependent checkpoints in neovascularization processes and supports the development of targeted modulators of angiogenic signaling.
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