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Key Documents

A9041

Sigma-Aldrich

Arg-Gly-Asp-Ser

≥95% (HPLC)

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About This Item

Formule empirique (notation de Hill):
C15H27N7O8
Numéro CAS:
Poids moléculaire :
433.42
Numéro MDL:
Code UNSPSC :
12352209
ID de substance PubChem :
Nomenclature NACRES :
NA.32

Source biologique

synthetic

Niveau de qualité

Pureté

≥95% (HPLC)

Forme

powder

Composition

Peptide content, ~70%

Technique(s)

cell culture | mammalian: suitable

Température de stockage

−20°C

Chaîne SMILES 

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

Clé InChI

NNRFRJQMBSBXGO-CIUDSAMLSA-N

Informations sur le gène

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Amino Acid Sequence

Arg-Gly-Asp-Ser

Description générale

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)

Conditionnement

Bottomless glass bottle. Contents are inside inserted fused cone.

Notes préparatoires

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

Autres remarques

Lyophilized from 0.1% TFA in H2O

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

A few immobilized thrombins are sufficient for platelet spreading
Okamura Y, et al.
Biophysical Journal, 100(2) (2011)
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)
Valeria S Mouguelar et al.
Reproduction (Cambridge, England), 141(5), 581-593 (2011-02-23)
Integrins are cell adhesion molecules that are thought to be involved in sperm-oocyte interaction. Nevertheless, their function in mammalian fertilization is still controversial, as different species behave differently. In amphibians, their role is mainly supported by Xenopus laevis studies, where
Bartley J Gill et al.
Cancer research, 72(22), 6013-6023 (2012-09-07)
Better understanding of the biophysical and biochemical cues of the tumor extracellular matrix environment that influence metastasis may have important implications for new cancer therapeutics. Initial exploration into this question has used naturally derived protein matrices that suffer from variability

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