96426-21-0

Basic information

• Product Name: GLY-ARG-GLY-ASP-SER
• Synonyms: GRGDS;GRGDS 1/2ACOH 2H2O;GRGDS, FIBRONECTIN ATTACHMENT PEPTIDE;GLY-ARG-GLY-ASP-SER;GLY-ARG-GLY-ASP-SER 1/2ACOH 2H2O;H-GLY-ARG-GLY-ASP-SER-OH;glycyl-arginyl-glycyl-aspartyl-serine;GLY-ARG-GLY-ASP-SER ACETATE
• CAS NO: 96426-21-0
• Molecular Formula: C₁₇H₃₀N₈O₉
• Molecular Weight: 490.47
• Product Categories: Cell Signaling Enzymes;ECM Related Proteins and PeptidesCytoskeleton and Extracellular Matrix;Extracellular Matrix;Extracellular Matrix Peptides (ECM);Extracellular Matrix Peptides and ProteinsPeptides for Cell Biology;Fibronectin Fragments and Analogs;Matrix Metalloproteinases Products;peptide
• Mol File: 96426-21-0.mol

Chemical Properties

• Appearance: solid
• Density: 1.66 g/cm³
• Refractive Index: 1.664
• Storage Temp.: −20°C
• PKA: 2.85±0.10(Predicted)
• CAS DataBase Reference: GLY-ARG-GLY-ASP-SER(CAS DataBase Reference)
• NIST Chemistry Reference: GLY-ARG-GLY-ASP-SER(96426-21-0)
• EPA Substance Registry System: GLY-ARG-GLY-ASP-SER(96426-21-0)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 96426-21-0(Hazardous Substances Data)

Usage

Uses

Used in Immunology Research:
GLY-ARG-GLY-ASP-SER is used as an antigen to determine whether integrin α4 or α5 hinders the adhesion of day 3 postirradiation thymocytes to thymic epithelial cells in mice. This helps in understanding the role of specific integrins in immune cell interactions and adhesion processes.
Used in Cell Biology Research:
GLY-ARG-GLY-ASP-SER is used for the treatment of collagen IV-coated dishes to study the role of integrins α1, αv, β1, and β3 in Sca-1+ progenitor cell differentiation into smooth muscle cells (SMCs). This application aids in investigating the influence of specific integrins on cell differentiation and development.
Used in Microbiology Research:
GLY-ARG-GLY-ASP-SER is used as a blocking peptide for the pre-incubation of Nisseria meningitides strains, to perform blocking experiments to study the interactions between these bacterial strains and fibronectin. This helps in understanding the molecular mechanisms of bacterial attachment and invasion.
Used in Virology Research:
GLY-ARG-GLY-ASP-SER is used for the pre-treatment of EL-4 cells infected by AdCMV-GFP (cytomegalovirus-green fluorescent protein), to study whether interaction with cellular integrins is essential for the transduction of adenovirus. This application contributes to the understanding of viral entry mechanisms and the development of antiviral strategies.

Biochem/physiol Actions

Antagonist of integrin function

InChI:InChI=1/C17H30N8O9/c18-5-11(27)23-8(2-1-3-21-17(19)20)14(31)22-6-12(28)24-9(4-13(29)30)15(32)25-10(7-26)16(33)34/h8-10,26H,1-7,18H2,(H,22,31)(H,23,27)(H,24,28)(H,25,32)(H,29,30)(H,33,34)(H4,19,20,21)/t8-,9-,10-/m0/s1

Upstream product

• 132304-03-1 C₃₉H₅₆N₈O₁₁S 
• 132304-04-2 Boc-Gly-Arg(Mts)-Gly-Asp-Ser(Bzl)-OPse 
• 132304-02-0 Boc-Gly-Arg(Mts)-Gly-Asp(OCHx)-Ser(Bzl)-OPse 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 136083-57-3 N-α-9-fluorenylmethoxycarbonyl-aspartic acid 
• 73724-45-5 N-(9H-fluoren-9-ylmethoxycarbonyl)-L-serine 
• 91000-69-0 Fmoc-L-Arg-OH 

Relevant articles and documents

Peptide microarrays for the discovery of bioactive surfaces that guide cellular processes: A single step azide-alkyne click chemistry approach

Cell behavior in vivo is guided by a complex microenvironment containing many different molecules including extracellular matrix (ECM) proteins, growth factors, and proteoglycans. Controlling the interaction between these various components at the cell-material interface will be invaluable in developing new materials for biomedical devices and tissue engineering applications. We report a single step approach to forming mixed peptide conjugated self-assembled monolayers on gold using copper-catalyzed azide-alkyne cycloaddition chemistry to study the combinatorial effects of different peptide ligands on cellular processes. We synthesized ECM adhesion peptides (YIGSR, GRGDS), a bone morphogenetic protein 7 (BMP-7) derived peptide (KPSSAPTQLN), and a heparin binding peptide (KRSR), and arrayed them, alone and in combination, onto gold coated coverslips. SAMs were characterized by X-ray photoelectron spectroscopy (XPS) and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry, and arrayed peptide combinations were seen to differentially bind to adipose derived stem cells (ADSCs) and mouse embryonic fibroblasts (MEFs). We further investigated the osteogenesis of ADSCs on SAMs containing combinations of adhesion peptide and BMP-7 peptide in both standard culture and osteogenic differentiation media. We demonstrate enhanced expression of osteogenic markers Runx2 and osteopontin when ADSCs are adherent to BMP-7 derived peptide alone or in combination with ECM adhesion peptides. The platform presented here enables immobilization of multiple peptides in a single step using a commercially available microarray spotter which will prove useful in fabricating biomolecule interfaces for cell biology studies and biochemical assays. This journal is the Partner Organisations 2014.

PROCESSES FOR REMOVING DIBENZOFULVENE

A dibenzofulvene amine adduct is removed by contacting a reaction mixture containing the dibenzofulvene amine adduct, which is obtained by reacting, for deprotection, an amino acid compound protected with an Fmoc group with an amine compound wherein a nit

Fibrinogen-coated particles for therapeutic use

The invention provides a particle comprising fibrinogen bound on the surface of an albumin matrix, wherein said particle is capable of coaggregation with platelet, and of aggregation in a solution containing soluble fibrinogen at a concentration of soluble fibrinogen not capable by it self of formation of a clot upon activation by thrombin.

Non-crosslinked protein particles for therapeutic and diagnostic use

Albumin particles in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolubilization without the aid of a crosslinking agent and without denaturation, by the incorporation of a stabilizing agent in the particle composition. Particles which are primarily albumin in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolublization by the incorporation of a reducing agent, oxidizing agent, hydrogen-accepting molecule, high molecular weight polymer, sulfur-containing ring compound or combinations thereof.

Non-crosslinked protein particles for therapeutic and diagnostic use

Albumin particles in the nanometer and micrometer size range in an aqueous suspension are rendered stable against resolubilization without the aid of a crosslinking agent and without denaturation, by the incorporation of hemoglobin in the particle composition. Particles which are primarily hemoglobin in the nanometer and micrometer size range in an aqueous suspension are rendered stable against aggregation by the incorporation of either albumin, surface active agents or gelatin.