The complement system is made up of a collection of proteins found in the bloodstream and is comprised of nine major complement proteins; complement C3 is one of them. The complement system is a crucial component of the cellular immune system because it kills unwanted bacteria and initiates inflammation. Within the complement system family of proteins, C3 is the most plentiful as well as most central protein, and consists of an alpha and a beta chain. The C3 activation step represents the convergence of the lectin, classical, and alternative complement activation pathways.
The CIP2A protein was originally identified as p90, a cytoplasmic auto-antigen from the serum of a cancer patient. It was later found to inhibit protein phosphatase 2A (PP2A) activity as well as interact with c-myc. CIP2A's inhibitory activity blocks c-myc phosphorylation and its subsequent proteolytic degradation, producing a stable c-myc that promotes aberrant cell growth and transformation. In addition to its role in c-Myc stabilization, CIP2A promotes anchorage-independent cell growth and in vivo tumor formation.
The enzyme S-adenosylmethionine synthetase, or MAT, catalyzes the formation of S- adenosylmethionine (AdoMet or SAMe) from methionine and ATP. AdoMet is the principal biological source of synthesized methyl, and is found in all cells but most prominently in the liver. In mammalian tissues, there are three distinct AdoMet synthases - the alpha, beta, and gamma isoforms. While the alpha and beta variants are uniquely expressed solely in the adult liver, gamma is more widely distributed in the extrahepatic tissues.
We at Novus Biologicals are constantly updating our antibody catalog in order to provide as comprehensive a database as possible for molecular biology researchers. Not all our antibodies are derived from proteins found in mammalian or human tissue. Some are derived from single-celled or non-eucaryotic organisms which produce harmful effects when introduced to humans or animals.
