Human AMBP preproprotein gene encodes a complex glycoprotein secreted in plasma. The precursor is proteolytically processed into distinct functioning proteins: alpha-1-microglobulin (A1M), which belongs to the superfamily of lipocalin transport proteins and may play a role in the regulation of inflammatory processes, and bikunin, which is a urinary trypsin inhibitor belonging to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes. AMBP binds and degrades heme, is a radical scavenger as well as a reductase. A model has been proposed in which A1M is described as a circulating “waste bin” which continuously removes free radicals and oxidizing agents, particularly heme, from the tissues. It is subsequently transported to the kidneys, where it is broken down. The protein is therefore believed to protect cells and tissues against the damage that is induced by abnormally high concentrations of free hemoglobin and/or reactive oxygen species (also called “oxidative stress”).

Full-length human Alpha-1 microglobulin (A1M) cDNA (20-203aa) was constructed with codon optimization gene synthesis technology and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein was expressed in E. coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro A1M mediated radical scavenger pathway regulation study for various cells by intracellular delivery of this protein with protein-delivery reagent such as ProFectin Reagent Kit.

2. May be used for protein-protein interaction interaction assay.

3. As substrate protein for various proteases assay.

4. Potential diagnostic protein, which may be used for preeclampsia application.

5. As immunogen for specific antibody production.