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Key Documents

G1269

Sigma-Aldrich

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

≥97% (HPLC)

Synonym(s):

GRGDSPK

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About This Item

Empirical Formula (Hill Notation):
C28H49N11O11
CAS Number:
Molecular Weight:
715.76
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.32

biological source

human

Quality Level

Assay

≥97% (HPLC)

form

powder

technique(s)

blocking: suitable
ligand binding assay: suitable

storage temp.

−20°C

SMILES string

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

InChI key

ZRVZOBGMZWVJOS-VMXHOPILSA-N

Gene Information

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Amino Acid Sequence

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

General description

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. 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.

Application

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

Biochem/physiol Actions

Fibronectin analog that binds to integrins.

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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A M Moursi et al.
Journal of cell science, 109 ( Pt 6), 1369-1380 (1996-06-01)
The secretion of fibronectin by differentiating osteoblasts and its accumulation at sites of osteogenesis suggest that fibronectin participates in bone formation. To test this directly, we determined whether fibronectin-cell interactions regulate progressive differentiation of cultured fetal rat calvarial osteoblasts. Spatial
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
Che-Yi Chang et al.
International journal of nanomedicine, 12, 279-294 (2017-01-25)
Neovascularization (NV) of the cornea can disrupt visual function, causing ocular diseases, including blindness. Therefore, treatment of corneal NV has a high public health impact. Epigalloccatechin-3-gallate (EGCG), presenting antiangiogenesis effects, was chosen as an inhibitor to treat human vascular endothelial
E A Cowles et al.
Journal of biomedical materials research, 52(4), 725-737 (2000-10-18)
Since osteoblast proliferation is critical for bone development, the effect of bone extracellular matrix (ECM) proteins on osteoblast signaling and proliferation in serum-free medium was investigated. Proliferation was highest in primary rat calvarial osteoblasts cells grown on fibronectin but less
M R Custodio et al.
The Journal of eukaryotic microbiology, 42(6), 721-724 (1995-11-01)
Developmental processes in multicellular organisms require structural elements, such as adhesion molecules, to stabilize cells at functional positions. In vertebrates, a series of extracellular matrix proteins, e.g. fibronectin and laminin, are involved in cell adhesion. These proteins contain Arg-Gly-Asp [RGD]

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