The connecting segment 1 (CS-1) is a cell attachment domain located in the type III homology connecting segment (IIICS) of fibronectin. Fibronectin CS1 Peptide lacks the Arg-Gly-Asp-containing domain, actively inhibits tumor metastases in spontaneous and experimental metastasis models.
CAT No: R1354
CAS No:136466-51-8
Synonyms/Alias:Fibronectin CS1 Peptide;136466-51-8;(4S)-4-amino-5-[[(2S,3S)-1-[[(2S)-1-[[(2S)-3-carboxy-1-[[(2S)-1-[(2S)-2-[[(2S)-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-3-hydroxy-1-oxopropan-2-yl]carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-5-oxopentanoic acid;Glu-Ile-Leu-Asp-Val-Pro-Ser-Thr;Fibronectin CS-1 Fragment (1978-1985) trifluoroacetate salt;Fibronectin cs-1 peptide;SCHEMBL8937022;CHEMBL3220763;HY-P1816;NCGC00167252-01;DA-63439;FF108601;Fibronectin cs-1 fragment(1978-1985);CS-0096031;H-Glu-Ile-Leu-Asp-Val-Pro-Ser-Thr-OH; H-EILDVPST-OH;(3S,6S,9S,12S,15S)-15-amino-12-sec-butyl-3-((S)-2-((S)-1-((1S,2R)-1-carboxy-2-hydroxypropylamino)-3-hydroxy-1-oxopropan-2-ylcarbamoyl)pyrrolidine-1-carbonyl)-6-(carboxymethyl)-9-isobutyl-2-methyl-5,8,11,14-tetraoxo-4,7,10,13-tetraazaoctadecan-18-oic acid;
Fibronectin CS1 Peptide is a synthetic peptide fragment derived from the alternatively spliced connecting segment 1 (CS1) region of human fibronectin, an essential extracellular matrix glycoprotein. The CS1 domain plays a pivotal role in mediating cell adhesion, migration, and signaling events by interacting specifically with integrin receptors, such as α4β1 (VLA-4). Due to its defined sequence and biological relevance, this peptide serves as a valuable molecular tool for dissecting cell-extracellular matrix interactions, understanding integrin-mediated processes, and advancing studies in cell biology, tissue engineering, and biomaterials research.
Cell Adhesion Studies: Utilization of the Fibronectin CS1 Peptide enables precise investigation of integrin-mediated cell adhesion mechanisms. By coating culture surfaces or biomaterials with this peptide, researchers can selectively engage α4β1 integrins on various cell types, including lymphocytes, fibroblasts, and stem cells. This targeted approach facilitates the analysis of integrin specificity, affinity, and downstream signaling pathways, providing critical insights into how cellular attachment and spreading are regulated by extracellular matrix cues.
Migration and Invasion Assays: The CS1 motif is instrumental in modulating cell migration, particularly in immune cells and mesenchymal lineages. Incorporating the peptide into in vitro migration or invasion assays allows researchers to evaluate the contribution of the CS1-integrin interaction to cell motility. This application is especially relevant in studies of wound healing, immune cell trafficking, and cancer metastasis, where controlled manipulation of the migratory environment is essential for elucidating underlying molecular mechanisms.
Biomaterials and Tissue Engineering: Integration of the Fibronectin CS1 Peptide into synthetic scaffolds or hydrogels enhances the bioactivity of engineered materials by providing cell-adhesive motifs that mimic native extracellular matrix signals. Functionalization with this sequence supports selective cell attachment, proliferation, and organization, which are crucial for the development of advanced tissue constructs and regenerative medicine platforms. By modulating cellular responses at the biomaterial interface, the peptide contributes to the design of more physiologically relevant and responsive tissue models.
Signal Transduction Research: The interaction between the CS1 sequence and integrin receptors initiates a cascade of intracellular signaling events that influence cell survival, differentiation, and cytoskeletal organization. Employing the peptide in cell culture or biochemical assays enables detailed analysis of these signaling pathways, including the activation of focal adhesion kinases and downstream effectors. Such studies are fundamental for deciphering how extracellular matrix components orchestrate cellular behavior through integrin-mediated signaling.
Competitive Binding and Receptor Blocking: The Fibronectin CS1 Peptide is frequently used as a competitive inhibitor in binding assays to disrupt native fibronectin-integrin interactions. By introducing the peptide into experimental systems, researchers can selectively block the CS1 binding site, thereby delineating the functional role of specific integrin subunits in adhesion and migration processes. This approach is invaluable for validating receptor-ligand specificity and for mapping the contributions of individual extracellular matrix domains to cell function.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More