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p16
Cat. No. AC-020
Structure:
H-Thr-His-Phe-Gly-Val-Leu-Met-Asp-Leu-Pro-Arg-Ser-Ala-Ser-Gln-Leu-OH
Activity:
GPR126 activator
p16 is a peptide derived from the C-terminal domain sequence at the GPCR proteolysis cleavage site of GPR126. p16 specifically activates both wild type GPR126 and generated chimeric P2Y12-ΔGPS-CTF(GPR126) receptors. In vivo p16 serves as an agonist for endogenous Gpr126 using zebrafish posterior lateral line nerve (PLLn) myelin basic protein expression as an assay. p16 is highly selective for GPR126, and is a short tethered sequence (the Stachel sequence) within the ectodomain of GPR126, demonstating that tethered peptide activation is a common signaling mechanism for adhesion GPCRs.
Liebscher et al (2014) A tethered agonist within the ectodomain activates the adhesion G protein-coupled receptors GPR126 and GPR133. Cell Rep. 9(6) 2018 PMID: 25533341
Related areas
Technical Data
| Structure | H-Thr-His-Phe-Gly-Val-Leu-Met-Asp-Leu-Pro-Arg-Ser-Ala-Ser-Gln-Leu-OH |
| Molecular Weight | 1770.91 |
| Formula | C78H126N22O23S |
| Sequence | THFGVLMDLPRSASQL |
| Modifications | None |
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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