Hemopexin [9013-71-2]
16-16-080513
Protein IDP02790
Product group Proteins / Signaling Molecules
Overview
- SupplierAthens Research
- Product NameHemopexin [9013-71-2]
- Delivery Days Customer9
- Applications SupplierIn Vitro Diagnostic, Glycosylation, Oxidative Damage, Lung Injury, Infection, Inflammation, Neurogenesis, Kidney Injury, Stroke, bèta-thalassemia, Sickle Cell Anemia, Epilepsy
- CertificationResearch Use Only
- Estimated Purity≥95% by SDS-PAGE
- Protein IDP02790
- Protein NameHemopexin
- Scientific DescriptionHemopexin is a plasma glycoprotein with the highest known binding affinity for free heme, functioning as a critical scavenger during intravascular hemolysis or cellular injury. Structurally, it comprises two bèta-propeller domains that form a high-affinity heme-binding pocket, enabling it to neutralize heme's oxidative toxicity and facilitate its transport to the liver for iron recycling via CD163 receptors. As an acute-phase reactant, hemopexin synthesis increases during inflammation, though chronic hemolysis often depletes its levels, exacerbating tissue damage. Deficiencies or dysfunction in hemopexin are implicated in hemolytic anemias such as sickle cell disease and bèta-thalassemia, where unbound heme drives endothelial activation, vaso-occlusion, and organ damage. It also correlates with neurologic complications in familial epilepsy due to impaired heme clearance in neural tissues and contributes to sepsis-related mortality by failing to counteract hemoglobin-mediated inflammation. Therapeutically, hemopexin supplementation shows promise in preclinical models, reducing cardiovascular dysfunction in sickle cell mice by 50% and mitigating renal injury in hemolysis. It serves as both a biomarker for hemolytic severity and a potential therapeutic agent to attenuate heme toxicity in transfusion medicine, atherosclerosis, and acute porphyrias.
- Shelf life instructionmore then 1 year
- SourceSource human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
- Storage Instruction-20C
- UNSPSC41116100
References
- Okubo, K., et al., (2018), 'Macrophage extracellular trap formation promoted by platelet activation is a key mediator of rhabdomyolysisinduced acute kidney injury', Nature Medicine, 24: pp 232–238.Read this paper
- Sakamoto, K., et al., (2021), 'IL-22 Controls Iron-Dependent Nutritional Immunity Against Systemic Bacterial Infections', Sci Immunol., 2(8): eaai8371.Read this paper
- Bateman, T. J., et al., (2021), 'A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii', NATURE COMMUNICATIONS., 12: pp 6270.Read this paper
- Aggarwal, S. et al., (2020), 'Heme attenuates beta-endorphin levels in leukocytes of HIV positive individuals with chronic widespread pain', Redox Biology 36: pp 101684.Read this paper
- Madyaningrana, K., et al., (2021), 'Alpha1-antitrypsin counteracts heme-induced endothelial cell inflammatory activation, autophagy dysfunction and death', Redox Biology 46: pp 102060.Read this paper