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IGFBP-3 peptide
Cat. No. PP-420
Structure:
H-Lys-Lys-Gly-Phe-Tyr-Lys-Lys-Lys-Gln-Cys-Arg-Pro-Ser-Lys-Gly-Arg-Lys-Arg-NH2
Other Names:
215-KKGFYKKKQCRPSKGRKR-232
Activity:
Blocks haluronan-CD44 signaling
IGFBP-3 peptide is a peptide derived from the nuclear localization sequence within the heparin-binding domain of insulin like growth factor binding protein-3 (IGFBP-3), and corresponds to amino acids 215–232 of the full length protein. Both this region and IGFBP-3 peptide bind to glycosaminoglycans including hyaluronan, and also have high affinity and specificity for the mitochondria derived peptide humanin, binding to it with a with a Kd of 120 nM compared with binding of 101 nM for the full-length protein. Both the IGFBP-3 protein and the synthetic IGFBP-3 peptide bind to hyaluronic acid and block its ability to interact with its receptor CD44, and using the synthetic IGFBP-3 peptide to bind hyaluronan inhibits viability of A549 lung cancer cells, an effect correlated with increased apoptosis.
Muterspaugh et al (2018) Interaction of Insulin-Like Growth Factor-Binding Protein 3 With Hyaluronan and Its Regulation by Humanin and CD44. Biochemistry 57(39) 5726 PMID: 30184438
Price et al (2020) IGFBP-3 Blocks Hyaluronan-CD44 Signaling, Leading to Increased Acetylcholinesterase Levels in A549 Cell Media and Apoptosis in a p53-Dependent Manner. Sci Rep. 10(1) 5083 PMID: 32193421
Al Khashali et al (2022) Opposing Roles of IGFBP-3 and Heparanase in Regulating A549 Lung Cancer Cell Survival. Cells 11(22) 3533 PMID: 36428962
Related areas
All peptides >
All protein-protein interaction modulators >
All cancer research categories >
Technical Data
| Structure | H-Lys-Lys-Gly-Phe-Tyr-Lys-Lys-Lys-Gln-Cys-Arg-Pro-Ser-Lys-Gly-Arg-Lys-Arg-NH2 |
| Molecular Weight | 2221.32 |
| Formula | C98H172N36O21S |
| Sequence | KKGFYKKKQCRPSKGRKR-NH2 |
| Modifications | C terminal amide |
Solubility and Storage
| Solubility | Soluble in water |
| Appearance | Freeze dried solid |
| Storage | Store dry, frozen and in the dark |
Batch Specific Data
| Purity | >95% by hplc |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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