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G1269

Sigma-Aldrich

Gly-Arg-Gly-Asp-Ser-Pro-Lys

≥97% (HPLC)

Sinonimo/i:

GRGDSPK

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CHF 281.00

About This Item

Formula empirica (notazione di Hill):
C28H49N11O11
Numero CAS:
Peso molecolare:
715.76
Numero MDL:
Codice UNSPSC:
12352209
ID PubChem:
NACRES:
NA.32

CHF 281.00


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Origine biologica

human

Livello qualitativo

Saggio

≥97% (HPLC)

Stato

powder

tecniche

blocking: suitable
ligand binding assay: suitable

Temperatura di conservazione

−20°C

Stringa SMILE

NCCCC[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CCCNC(N)=N)NC(=O)CN)C(O)=O

InChI

1S/C28H49N11O11/c29-8-2-1-5-16(27(49)50)37-25(47)19-7-4-10-39(19)26(48)18(14-40)38-24(46)17(11-22(43)44)36-21(42)13-34-23(45)15(35-20(41)12-30)6-3-9-33-28(31)32/h15-19,40H,1-14,29-30H2,(H,34,45)(H,35,41)(H,36,42)(H,37,47)(H,38,46)(H,43,44)(H,49,50)(H4,31,32,33)/t15-,16-,17-,18-,19-/m0/s1
ZRVZOBGMZWVJOS-VMXHOPILSA-N

Informazioni sul gene

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Amino Acid Sequence

Gly-Arg-Gly-Asp-Ser-Pro-Lys

Descrizione generale

Gly-Arg-Gly-Asp-Ser-Pro-Lys is a RGD peptide. Naturally occurring RGD peptides, present in the ECM (extracellalar matrix) proteins, are involved in facilitating integrin-mediated cell adhesion to matrix proteins.[1] RGD peptide is present as repeats in cell-adhesion protein, such as fibronectin and vitronectin. This tripeptide is recognized by cells by specific integrins (e.g. β1 , β3 , and β5 subunits), present on the cell surface and associated with the actin filament via the FA (focal adhesion)-complex.[2]

Applicazioni

Gly-Arg-Gly-Asp-Ser-Pro-Lys (RGD peptide) has been used-
  • as a blocking peptide to inhibit integrin-fibronectin binding[3]
  • in adhesion assay performed on porcine trophectoderm to study the influence of TGFβ (transforming growth factor) on cell adhesion[4]
  • for incubation of MC3T3-E1 osteoblast cells to determine its effect on cell adhesion measured by AFM (atomic force microscopy)[2]
  • for the preparation of RGD.Flt23k.NR nanoparticles[5]
  • to determine the involvement of RGD-integrin bonding in cell adhesion process[6]

Azioni biochim/fisiol

Fibronectin analog that binds to integrins.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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Pierre-Henri Puech et al.
Journal of cell science, 118(Pt 18), 4199-4206 (2005-09-13)
During vertebrate gastrulation, progenitor cells of different germ layers acquire specific adhesive properties that contribute to germ layer formation and separation. Wnt signals have been suggested to function in this process by modulating the different levels of adhesion between the
Christine Selhuber-Unkel et al.
Biophysical journal, 95(11), 5424-5431 (2008-08-12)
We have studied the initial phase of cell adhesion as a function of the lateral organization of individual integrin molecules with single-cell force microscopy. Nanostructures, consisting of hexagonally ordered gold dots, were prepared with diblock-copolymer micelle lithography and functionalized with
Yang Kyung Cho et al.
Investigative ophthalmology & visual science, 53(4), 2328-2336 (2012-03-20)
To determine if nanoparticles delivering plasmids expressing Flt23k (an anti-VEGF intraceptor) can enhance murine cornea transplant survival and whether their effect is synergistic with steroid therapy. Biodegradable PLGA Flt23k loaded or blank nanoparticles were prepared using the emulsion solvent evaporation
J Holland et al.
Biomaterials, 17(22), 2147-2156 (1996-11-01)
A synthetic peptide, Gly-Arg-Gly-Asp-Ser-Pro-Lys (GRGDSPK), which includes the cell-adhesive region of fibronectin, Arg-Gly-Asp (RGD), was covalently bound to a dialdehyde starch (DAS) coating on a polymer surface by reductive amination. The GRGDSPK/DAS-coated surface was characterized by atomic force microscopy (AFM)
E J Filardo et al.
The Journal of cell biology, 130(2), 441-450 (1995-07-01)
The NPXY sequence is highly conserved among integrin beta subunit cytoplasmic tails, suggesting that it plays a fundamental role in regulating integrin-mediated function. Evidence is provided that the NPXY structural motif within the beta 3 subunit, comprising residues 744-747, is

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