Adiponectin Protein (NBP1-46038) (0.025 mg)

Adiponectin is a member of the 'adipocytokines' that are cytokines that are expressed from adipose tissues. Its general functions include regulation of energy homeostasis, hematopoiesis, inflammation and immunity. Adiponectin also plays an important role in fat metabolism, feeding behaviour, insulin sensitivity and is a negative regulator of hematopoiesis and immune responses. Adiponectin has been shown to suppress the expression of a number of membrane bound proteins involved in the infiltration of cells to sites of inflammation, including, vascular cell adhesion molecule 1 (VCAM-1), E-Selectin, and intercellular adhesion molecule-1 (ICAM-1). Furthermore adiponectin suppresses TNF induced adhesion of monocytes to endothelial cells through a mechanism involving the suppression of TNF-alpha induced I-kappa-B-alpha phosphorylation. Adiponectin also inhibits phagocytosis and bacterial lipopolysaccharideinduced production of TNF-alpha in mature macrophages. Conversely, TNF-alpha reduces the expression and secretion of adiponectin in differentiating primary human pre-adipocytes. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible.