Synthetic peptide directed towards the C terminal region of human Anxa6
Biochem/physiol Actions
ANXA6 is a calcium-dependent, phospholipid-binding protein that belongs to the annexin family. It inhibits the activity of cytoplasmic phospholipase A2 and prevenst the transport of caveolin-1 from the Golgi complex. ANXA6 has been reported to regulate mitochondrial homeostasis by inhibiting Drp1 and blocking mitochondrial fission.
Sequence
Synthetic peptide located within the following region: SDTSGHFRRILISLATGHREEGGENLDQAREDAQVAAEILEIADTPSGDK
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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Mitochondrial homeostasis is critical in meeting cellular energy demands, shaping calcium signals and determining susceptibility to apoptosis. Here we report a role for anxA6 in the regulation of mitochondrial morphogenesis, and show that in cells lacking anxA6 mitochondria are fragmented
The Journal of biological chemistry, 283(15), 10174-10183 (2008-02-05)
The molecular mechanisms regulating the exit of caveolin from the Golgi complex are not fully understood. Cholesterol and sphingolipid availability affects Golgi vesiculation events and involves the activity of cytoplasmic phospholipase A(2) (cPLA(2)). We recently demonstrated that high expression levels
Eukaryotic cells contain various Ca(2+)-effector proteins that mediate cellular responses to changes in intracellular Ca(2+) levels. A unique class of these proteins - annexins - can bind to certain membrane phospholipids in a Ca(2+)-dependent manner, providing a link between Ca(2+)
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