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Human Hemopexin
Native Whole Molecule
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Proteins Synonyms: HPX, HX, Beta-1B-glycoprotein Source: Human Plasma Purity: ≥ 95% by SDS-PAGE Physical State: Lyophilized from 11.9 mM phosphate, 137 mM NaCl, 2.7 mM KCl, pH 7.4. Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
HPX, HX, Beta-1B-glycoprotein
Description of Human Hemopexin
Human Hemopexin is a 57 kDa protein. Hemopexin 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 β-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 β-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.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human Hemopexin at -20°C.
Applications
In Vitro Diagnostic, Glycosylation, Oxidative Damage, Lung Injury, Infection, Inflammation, Neurogenesis, Kidney Injury, Stroke, β-thalassemia, Sickle Cell Anemia, Epilepsy.
Citations/Publications
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. Available at: doi:10.1038/nm.4462
Sakamoto, K., et al., (2021), 'IL-22 Controls Iron-Dependent Nutritional Immunity Against Systemic Bacterial Infections', Sci Immunol., 2(8): eaai8371. Available at: doi:10.1126/sciimmunol.aai8371.
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. Available at: https://doi.org/10.1038/s41467-021-26545-9
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. Available at: https://doi.org/10.1016/j.redox.2020.101684
Madyaningrana, K., et al., (2021), 'Alpha1-antitrypsin counteracts heme-induced endothelial cell inflammatory activation, autophagy dysfunction and death', Redox Biology 46: pp 102060. Available at: https://doi.org/10.1016/j.redox.2021.102060
NCBI: https://www.ncbi.nlm.nih.gov/protein/P02790/
Shipped with ice packs
Gel Scan of Human Hemopexin
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
Paying by bank transfer
