This rabbit IgG1 polyclonal antiobody was generated against a synthetic peptide (TARRSRAASSQRAEEC) and recognizes mammalian forms of Phospho Charged multi vesicular protein 4c.
Borealin interacts directly with Snf7/Shrb/CHMP4 components in both Drosophila and human cells and the two proteins colocalize at the midbody in late cytokinesis. Aurora B phosphorylates CHMP4C at three serine residues located in its C-terminal linker region, a part of the protein known to regulate its ability to form polymers and interact with the membrane. Over-expression of CHMP4C variants mutated in these three residues caused cytokinesis failure, suggesting that Aurora B inhibits CHMP4C activity during cytokinesis. It is proposed that CPC controls abscission timing in both flies and human cells by regulating the function of ESCRT-III Snf7 proteins during cytokinesis through the interaction of its Borealin component with the N-terminus of Shrb/CHMP4 proteins and Aurora B-mediated phosphorylation of the CHMP4C regulatory linker tail.
From a laboratory at Cancer Research Technology.
Part of The Investigator's Annexe program.
|Antigen:||Phospho Charged multi vesicular protein 4c|
|Molecular Weight:||Approx. 30kDa|
|Immunogen:||Synthetic peptide (TARRSRAASSQRAEEC)|
|Buffer:||PBS, 0.09% NaN3|
|Positive Control:||Synchronised HeLa cell extracts. Signals are absent in a twin blot that had been pre-incubated with lambda-phosphatase, indicating that the antibody specifically recognizes a phosphorylated form of CHMP4C.|
|Comments:||Staining Pattern: CHMP4C is predominantly cytoplasmic and partially colocalizes with Borealin during late cytokinesis, and during abscission CHMP4 is found at the midbody.|
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