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Q14
Cat. No. PI-280
Structure:
Other Names:
Activity:
Q14 is a peptide derived from the transmembrane domain of the mitochondrial anchored deubiquitinating enzyme USP30 (ubiquitin specific peptidase 30). Q14 can easily cross the cell membrane, bind to mitochondrial anchored USP30 directly, degrade outer mitochondrial membrane (OMM) proteins, promote mitochondrial fission, and trigger mitophagy. Q14 increases mitophagy through two distinct mechanisms, autoinhibition of USP30, and accelerated autophagosome formation through the LC3-interacting region (LIR) of Q14, synergistically enhancing mitophagy. USP30 antagonises PRKN/parkin-mediated mitophagy, making it a potential target for treating Parkinsons disease.
Qin X (2022) Identification of an autoinhibitory, mitophagy-inducing peptide derived from the transmembrane domain of USP30. Autophagy 1-20 PMID: 34989313
Related areas
All peptides >
All deubiquitinating enzyme modulators >
All regulated cell death research areas >
All neuroscience areas >
Technical Data
Structure | H-Gly-Ile-Tyr-Val-Ile-Trp-Gly-Pro-Ile-Thr-Glu-Arg-Lys-Lys-Arg-Arg-Lys-Gly-NH2 |
Molecular Weight | 2156.60 |
Formula | C99H166N32O22 |
Sequence | GIYVIWGPITERKKRRKG-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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