Recombinant Proteins
Product List
Hemopexin Human
Hemopexin Human Recombinant
Hemopexin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Hemopexin Human, Sf9
Hemopexin Human Recombinant, Sf9
Hemopexin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 448 amino acids (24-462a.a.) and having a molecular mass of 50.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
Hemopexin is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Introduction
Key Biological Properties: Hemopexin is a 60-kDa plasma glycoprotein with a high binding affinity to heme in an equimolar ratio . It plays a major protective role against oxidative stress through its heme-scavenging activities .
Expression Patterns and Tissue Distribution: Hemopexin is primarily expressed in the liver but is also found in other tissues such as the nervous system, skeletal muscle, retina, and kidney . It is an acute-phase protein whose synthesis is induced after an inflammatory event .
Primary Biological Functions: Hemopexin’s main function is to scavenge heme released or lost by the turnover of heme proteins such as hemoglobin, thus protecting the body from oxidative damage . It also plays a role in recycling the iron bound to heme molecules .
Role in Immune Responses and Pathogen Recognition: Hemopexin is pivotal in the immune defense against hemolytic stress. It serves as an effective antagonist against heme toxicity resulting from severe acute or chronic hemolysis .
Mechanisms with Other Molecules and Cells: Hemopexin binds free heme and forms a complex that is transported to hepatocytes and macrophages via receptors such as CD91 . This binding prevents heme’s pro-oxidant and pro-inflammatory effects and promotes its detoxification .
Binding Partners and Downstream Signaling Cascades: Hemopexin interacts with CD91 to release its bound ligand for internalization . The heme-HPX complex is phagocytosed by macrophages and broken down inside the cells, leading to the formation of bilirubin, carbon monoxide, and iron .
Regulatory Mechanisms Controlling Expression and Activity: The expression of hemopexin is regulated at multiple levels, including developmental control, tissue-specific control, and modulation during the acute phase reaction . Post-translational modifications also play a role in regulating its activity .
Biomedical Research: Hemopexin is used in research to understand its role in hemolytic diseases and its potential as a biomarker for assessing disease progression and prognosis .
Diagnostic Tools and Therapeutic Strategies: Hemopexin-based therapies are being developed to mitigate toxic heme exposure in conditions such as sickle cell disease, transfusion-induced hemolysis, and sepsis . It is also being explored as a diagnostic tool for various hematological disorders .
Role Throughout the Life Cycle: Hemopexin plays a crucial role in protecting the body from oxidative damage throughout the life cycle, from development to aging and disease . Its levels and activity can be indicative of various pathological conditions, making it a valuable marker in clinical settings .
