Midkine, a heparin-binding growth factor, contains 121 amino acid residues with 5 disulfide bonds. It promotes the growth, survival, and migration of various cells, and plays roles in neurogenesis and epithelial mesenchymal interactions during organogenesis. The C-terminal portion contains the heparin-binding domain and the antigenicity and neurite-promoting sequences. Both the C- and N-terminals are necessary for the moleculeμs neurotrophic effects.
Midkine Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids and having a molecular mass of 13.4kDa.
The Midkine is purified by proprietary chromatographic techniques.
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.
