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QK
Cat. No. RT-040
Structure:
Other Names:
Activity:
QK is a peptide derived from the 17–25 α-helical region of vascular endothelial growth factor (VEGF), which is the region of VEGF involved when binding to its receptor Flt-1 (VEGFR-1), QK acts as a VEGF mimetic and agonist and can reproduce the biological activity of VEGF while retaining its bioactivity much longer in vivo than the full-length protein. QK promotes proliferation and angiogenic differentiation of endothelial cells and can promote microvascularization in vitro and in vivo. QK can be used as a VEGF mimetic agent in reparative angiogenesis and has been synthesised as a nanoparticle for enhanced stability, in this form it has been used to prevent the occurrence of bisphosphonate-related osteonecrosis of the jaw (BRONJ).
D'Andrea (2005) Targeting angiogenesis: structural characterization and biological properties of a de novo engineered VEGF mimicking peptide. Proc Natl Acad Sci U S A 102(40) 14215 PMID: 16186493
Finetti (2012) Functional and pharmacological characterization of a VEGF mimetic peptide on reparative angiogenesis. Biochem Pharmacol. 84(3) 303 PMID: 22554565
Nair et al (2021) Light-Regulated Angiogenesis via a Phototriggerable VEGF Peptidomimetic. Adv Healthc Mater 10(14): e2100488 PMID: 34110713
Zhao (2022) Tetrahedral framework nucleic acid carrying angiogenic peptide prevents bisphosphonate-related osteonecrosis of the jaw by promoting angiogenesis. Int J Oral Sci. 14(1) 23 PMID: 35477924
Related areas
All peptides >
All receptor tyrosine kinase modulators >
All immunology research categories >
Technical Data
Structure | Ac-Lys-Leu-Thr-Trp-Gln-Glu-Leu-Tyr-Gln-Leu-Lys-Tyr-Lys-Gly-Ile-NH2 |
Molecular Weight | 1951.09 |
Formula | C94H146N22O23 |
Sequence | Ac-KLTWQELYQLKYKGI-NH2 |
Modifications | N terminal acetyl, 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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