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|Author:||Cheng Zhiyong Z|
Foxo1 integrates insulin signaling with mitochondrial function in the liver.
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Dynamitin is a 50 kDa protein containing a calmodulin binding domain, a putative ATPase domain and MacMARCKS-binding domain. This protein is a part of the dynactin complex believed to link the dynactin complex to membrane compartments. Its functions are tightly associated with dynein motor protein, thus extend to vesicle trafficking and membrane integrity. Dynamitin was named so because its overexpression causes dynactin complex which contains 10 subunits, to disassemble. Its N terminal 58 amino acid is for MacMARCKS binding and residues 59-83 is responsible for calmodulin binding. This antibody is is against the N terminal 59aa of full length p50 dynamitin.