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A9041

Sigma-Aldrich

Arg-Gly-Asp-Ser

≥95% (HPLC)

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About This Item

Empirical Formula (Hill Notation):
C15H27N7O8
CAS Number:
Molecular Weight:
433.42
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.32

biological source

synthetic

Quality Level

Assay

≥95% (HPLC)

form

powder

composition

Peptide content, ~70%

technique(s)

cell culture | mammalian: suitable

storage temp.

−20°C

SMILES string

N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(O)=O

InChI

1S/C15H27N7O8/c16-7(2-1-3-19-15(17)18)12(27)20-5-10(24)21-8(4-11(25)26)13(28)22-9(6-23)14(29)30/h7-9,23H,1-6,16H2,(H,20,27)(H,21,24)(H,22,28)(H,25,26)(H,29,30)(H4,17,18,19)/t7-,8-,9-/m0/s1

InChI key

NNRFRJQMBSBXGO-CIUDSAMLSA-N

Gene Information

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Amino Acid Sequence

Arg-Gly-Asp-Ser

General description

The tetrapeptide Arg-Gly-Asp-Ser (RGDS) is a key component of the cell attachment domain of fibronectin. The RGDS sequence was found initially to promote the attachment of rat kidney fibroblasts (NRKcells) to fibronectin and synthetic fibronectin peptides coupled to protein-coated plastic. Further investigation indicated that the free RGDS peptide inhibited the attachment of NRK cells to fibronectin coated substrates. The RGDS sequence has been shown to occur in several other proteins, such as the λ receptor on E. coli and the Sindbis coat protein. RGDS is also a target sequence for spirochete adherence of the syphilis bacterium Treponema pallidum.

RGDS has been shown to block fibrinogen-induced aggregation of intact erythrocytes and specific binding of fibrinogen to erythrocyte membranes. The effect of RGDS on transforming growth factor ß1 (TGFß1) mRNA expression and secretion in cultured human mesangial cells has been investigated. RGDS has been utilized in a study of integrin-mediated signal transduction in cultured cells from the sponge Suberites domuncula. RGDS has been demonstrated
to mitigate the binding of Mycobacterium tuberculosis to murine alveolar macrophages

Application

Arg-Gly-Asp-Ser has been used:
  • to study its effects on cell attachment in rats
  • to analyse the interaction of fibrinogen with erythrocytes occurs through integrin related receptor
  • to pretreat the cells, to assess the role of integrin in the cell attachment process
  • to test its competition with platelet-secreted, nanosheet-adsorbed proteins for binding to glycoprotein IIIa (GPIIIa)

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Preparation Note

This product is soluble in water (1 mg/ml), yielding a
clear, colorless solution.

Other Notes

Lyophilized from 0.1% TFA in H2O

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Lian Leng et al.
Advanced materials (Deerfield Beach, Fla.), 24(27), 3650-3658 (2012-06-21)
The one-step, continuous formation of mosaic hydrogel sheets is presented. A microfluidic device allows controllable incorporation of secondary biopolymers within a flowing biopolymer sheet followed by a cross-linking step that retains the microscale composition. Information is encoded; mosaic stiffness and
Integrin-associated protein (CD47) is a putative mediator for soluble fibrinogen interaction with human red blood cells membrane
De OS, et al.
Biochimica et Biophysica Acta, 1818(3), 481-490 (2012)
A few immobilized thrombins are sufficient for platelet spreading
Okamura Y, et al.
Biophysical Journal, 100(2) (2011)
Toshiki Sawada et al.
Molecular bioSystems, 8(4), 1264-1274 (2012-02-02)
We obtained novel peptides that selectively bind to self-assembling peptide nanomaterials from a random peptide library displayed on phages. Affinity-dependent peptide screening gave phage clones displaying peptides with selective affinities against two kinds of highly networked nanofibers constructed of β-sheet
Sapun H Parekh et al.
Biomaterials, 32(9), 2256-2264 (2010-12-24)
Proliferation and differentiation of cells are known to be influenced by the physical properties of the extracellular environment. Previous studies examining biophysics underlying cell response to matrix stiffness utilized a two-dimensional (2D) culture format, which is not representative of the

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