Alpha 1-Microglobulin Protein, Human (P.pastoris, His)

Alpha 1-microglobulin has multiple antioxidant and repairing effects, with reductase, heme-binding and free radical scavenging activities. Within blood vessels, it regulates red blood cell homeostasis and prevents heme- and reactive oxygen species-induced cell damage. Alpha 1-Microglobulin Protein, Human (P.pastoris, His) is the recombinant human-derived Alpha 1-Microglobulin protein, expressed by P. pastoris , with N-His labeled tag. The total length of Alpha 1-Microglobulin Protein, Human (P.pastoris, His) is 143 a.a., with molecular weight of ~17.4 kDa.

The Alpha 1-Microglobulin protein serves as a multifaceted antioxidant and tissue repair agent, showcasing reductase, heme-binding, and radical-scavenging activities. Operating both intravascularly and extravascularly, it actively removes and shields against harmful oxidants, facilitating repair of macromolecules in various cellular compartments. Intravascularly, the protein plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage, safeguarding fetal and adult red blood cells from hemolysis. It also reduces extracellular methemoglobin, converting it back to the oxygen-carrying form deoxyhemoglobin. In instances of acute inflammation, it inhibits oxidation of low-density lipoprotein particles, thereby limiting vascular damage. Extravascularly, the protein protects against oxidation products on extracellular matrix structures and cell membranes, catalyzing the reduction of carbonyl groups on oxidized collagen fibers. Notably, it counteracts oxidative damage at the blood-placenta interface, preventing the leakage of free fetal hemoglobin into the maternal circulation. Intracellularly, the protein maintains mitochondrial redox homeostasis, preserving mitochondrial ATP synthesis and protecting renal tubule epithelial cells from heme-induced oxidative damage. Additionally, it exhibits chaperone activity in facilitating the correct folding of bikunin in the endoplasmic reticulum, and it acts as a Kunitz-type serine protease inhibitor and structural component of the extracellular matrix, contributing to extracellular space remodeling and cell adhesion. It further participates in the I-alpha-I complex, facilitating the transfer of heavy chains to hyaluronan in the presence of TNFAIP6, a process critical for extracellular matrix proteoglycan structure remodeling. The protein's diverse functions extend to inhibiting proteases involved in airway inflammation, cytotoxic responses, and matrix metalloproteinase activation, as well as playing a role in cumulus oophorus expansion during ovulation and inhibiting calcium oxalate crystallization.

Human

P. pastoris

N-His

P02760 (A206-L348)

259  [NCBI]

Approximately 17.4 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.