Hemopexin from Human Plasma – Native Protein (Research Use Only)

Hemopexin from Human Plasma (Catalog #B2014954) is a high-purity native 57 kDa glycoprotein supplied as 500 µg of low-endotoxin lyophilized powder. Hemopexin is the primary heme-binding protein in human plasma with the highest known affinity for free heme. It sequesters heme released during hemolysis or tissue injury, preventing oxidative damage and facilitating safe transport and catabolism in the liver via receptor-mediated endocytosis. This native human hemopexin is an excellent research tool for studies of heme metabolism, oxidative stress protection, acute-phase responses, hemolysis, and related pathologies.

Scientific Overview

Hemopexin is a 57 kDa plasma glycoprotein that binds free heme with extremely high affinity, protecting cells and tissues from heme-catalyzed formation of reactive oxygen species and lipid peroxidation. The heme–hemopexin complex is recognized by the CD91/LRP1 receptor on hepatocytes and macrophages, leading to internalization and degradation of heme by heme oxygenase-1 while recycling apo-hemopexin. This native human hemopexin (low endotoxin) is widely used in functional studies of heme scavenging, oxidative stress, acute-phase responses, hemolytic disorders, intracerebral hemorrhage, sickle cell disease, and cancer-related heme biology.

Key research applications include:

• Heme-binding affinity and transport assays
• Oxidative stress and cytoprotection studies
• Acute-phase inflammatory response models
• Heme-mediated toxicity and detoxification research
• Development of heme-related biomarkers and therapeutic strategies

Usage & Handling Guidance

Store the lyophilized powder at -20 °C. Reconstitute in sterile ultrapure water, PBS, or appropriate assay buffer to the desired concentration. Prepare single-use aliquots to avoid repeated freeze–thaw cycles. The protein remains stable under standard laboratory conditions when handled with protease-free reagents.

• Recommended applications: Heme-binding assays, oxidative stress studies, cell culture supplementation, and in vivo heme-scavenging experiments
• Working concentration: Typically 0.1–10 µM (optimize empirically for your assay)
• Stability: Lyophilized form is stable for long-term storage at -20 °C; reconstituted solutions should be used fresh or stored frozen in aliquots
• Handling notes: Low endotoxin level makes it suitable for sensitive cell-based or in vivo studies

What You Get

• 500 µg native Hemopexin from Human Plasma as lyophilized powder
• High-purity 57 kDa glycoprotein with intact heme-binding activity
• Low endotoxin level suitable for functional and cell-based studies
• Convenient quantity for multiple experiments and method optimization
• For research use only (RUO)

Why Researchers Choose It

• Native human hemopexin for physiologically relevant studies
• Low endotoxin preparation ideal for cell culture and in vivo experiments
• Excellent tool for heme scavenging, oxidative stress, and acute-phase response research
• Well-characterized protein with extensive literature support in human heme biology
• Reliable source of high-purity hemopexin for biochemical and functional assays

Frequently Asked Questions (FAQ)

• What is the primary function of hemopexin?
  Hemopexin binds free heme with extremely high affinity, preventing oxidative damage and facilitating safe heme recycling in the liver.
• Why is low endotoxin important?
  It minimizes unwanted inflammatory responses in cell culture or in vivo studies, making it suitable for sensitive functional assays.
• How should I reconstitute the powder?
  Dissolve in sterile ultrapure water or PBS to the desired concentration. Prepare aliquots and store at -20 °C.
• Can this be used in cell culture?
  Yes. The low endotoxin level makes it appropriate for serum-free or low-serum media in heme-related cellular studies.
• What storage conditions are recommended?
  Store the lyophilized powder at -20 °C for long-term stability.

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References

• Jung JY, Kwak YH, Kim KS, Kwon WY, Suh GJ. Change of hemopexin level is associated with the severity of sepsis in endotoxemic rat model and the outcome of septic patients. J Crit Care. 2015 Jun;30(3):525-30.
• Chang CH, Lin JY, Lo WY, Lee TH. Hypothermal stress induced differential expression profiles of the immune response gene, warm-temperature-acclimation associated 65-kDa protein (Wap65), in the liver of fresh water and seawater milkfish, Chanos chanos. Fish Shellfish Immunol. 2017 Nov;70:174-184.
• Stanley LA, Adams DJ, Lindsay R, Meehan RR, Liao W, Wolf CR. Potentiation and suppression of mouse liver cytochrome P-450 isozymes during the acute-phase response induced by bacterial endotoxin. Eur J Biochem. 1988 May 16;174(1):31-6.
• Liu W, Lu L, Pan H, He X, Zhang M, Wang N, Zhu J, Yi H, Tang S. Heme oxygenase-1 and hemopexin gene polymorphisms and the risk of anti-tuberculosis drug-induced hepatotoxicity in China. Pharmacogenomics. 2022 May;23(7):431-441.
• Fan X, Zhang X, Liu LC, Zhang S, Pelger CB, Lughmani HY, Haller ST, Gunning WT 3rd, Cooper CJ, Gong R, Dworkin LD, Gupta R. Hemopexin accumulates in kidneys and worsens acute kidney injury by causing hemoglobin deposition and exacerbation of iron toxicity in proximal tubules. Kidney Int. 2022 Dec;102(6):1320-1330.
• Muller-Eberhard U. Hemopexin. Methods Enzymol. 1988;163:536-65.
• Fiorito V, Tolosano E. Hemopexin and Cancer. Int J Mol Sci. 2022 Jan 17;23(2):997.
• Ashouri R, Fangman M, Burris A, Ezenwa MO, Wilkie DJ, Doré S. Critical Role of Hemopexin Mediated Cytoprotection in the Pathophysiology of Sickle Cell Disease. Int J Mol Sci. 2021 Jun 15;22(12):6408.
• Delanghe JR, Langlois MR. Hemopexin: a review of biological aspects and the role in laboratory medicine. Clin Chim Acta. 2001 Oct;312(1-2):13-23.
• Piccard H, Van den Steen PE, Opdenakker G. Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. J Leukoc Biol. 2007 Apr;81(4):870-92.