Description
Human IL-6 Recombinant Protein Tag Free Lyophilized has been recombinantly produced in E Coli.
Cytokines of the IL6/GCSF/MGF family are glycoproteins of about 170 to 180 amino acid residues that contain four conserved cysteine residues involved in two disulfide bonds. They have a compact, globular fold (similar to other interleukins), stabilized by the 2 disulfide bonds. One half of the structure is dominated by a 4 alpha-helix bundle with a left-handed twist; the helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet. The fourth alpha helix is important to the biological activity of the molecule. Interleukin-6 (IL-6) is an important proinflammatory and immunoregulatory cytokine expressed by various cells. Interleukin-6 has been shown to inhibit the growth of early sTage and to promote the proliferation of advanced sTage melanoma cells in vitro.
This recombinant protein can be used for biological assays