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MW: 57,000
Extinction Coefficient: 1.97
Lyophilized from 11.9 mM phosphate, 137 mM NaCl, 2.7 mM KCl, pH 7.4.
Hemopexin is a single-chain protein belonging to the family of blood transport proteins. It binds to heme released into the bloodstream during the degradation process. Recent studies have demonstrated that hemopexin acts as an extracellular antioxidant against hemoglobin-mediated damage in inflammation. Hemopexin protects against heme toxicity and conserves and recycles iron. Abnormal levels of hemopexin are associated with hemolytic anemia, chronic neuromuscular disease, and acute intermittent porphyria.
Storage: -20°C
Purity: >=95% by SDS-PAGE.
Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests.
Lab products are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research use only.
Product Citations:
Chen, Grace, et al. "Heme-induced neutrophil extracellular traps contribute to the pathogenesis of sickle cell disease."?Blood?(2014): blood-2013.
Lipiski, Miriam, et al. "Human Hp1-1 and Hp2-2 phenotype-specific haptoglobin therapeutics are both effective in vitro and in guinea pigs to attenuate hemoglobin toxicity."?Antioxidants & redox signaling?19, no. 14 (2013): 1619-1633.
Zager, Richard A., Ali CM Johnson, and Kirsten Becker. "Renal cortical hemopexin accumulation in response to acute kidney injury."?American Journal of Physiology-Renal Physiology?303, no. 10 (2012): F1460-F1472.
Sakamoto K, et al. IL-22 Controls Iron-Dependent Nutritional Immunity Against Systemic Bacterial Infections. Sci Immunol. 2017 Feb;2(8). pii: eaai8371. doi: 10.1126/sciimmunol.aai8371. Epub 2017 Feb 3.
Kozlik P, Goldman R, Sanda M. Study of structure-dependent chromatographic behavior of glycopeptides using reversed phase nanoLC.
Electrophoresis. 2017 Apr 26. doi: 10.1002/elps.201600547. [Epub ahead of print].
Kozlik P, Sanda M, Goldman R. Nano reversed phase versus nano hydrophilic interaction liquid chromatography on a chip in the analysis of the hemopexin glycopeptides. J Chromatogr A. 2017 Oct 13;1519:152-155. doi: 10.1016/j.chroma.2017.08.066. Epub 2017 Aug 26.
Kassa T, Jana S, Meng F Alayash AI. Differential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase‐1. FEBS Open Bio. 2016 Aug 8;6(9):876-84. doi: 10.1002/2211-5463.12103. eCollection 2016 Sep.
Lin T, Liu J, Huang F, Van Engelen TS, et. al. Purified and recombinant hemopexin: protease activity and effect on neutrophil chemotaxis.
Mol Med. 2016 Jan 8. doi: 10.2119/molmed.2016.00006. [Epub ahead of print]
Aggarwal S, Lam A, Bolisetty S, Carlisle MA, et al. Heme Attenuation Ameliorates Irritant Gas Inhalation-Induced Acute Lung Injury.
Antioxid Redox Signal. 2016 Jan 10;24(2):99-112. doi: 10.1089/ars.2015.6347. Epub 2015 Dec 14.
Mehta NU, Grijalva V, Hama S, Wagner A, Navab M, Fogelman AM, Reddy ST.
Apolipoprotein E-/- Mice Lacking Hemopexin Develop Increased Atherosclerosis via Mechanisms That Include Oxidative Stress and Altered Macrophage Function. Arterioscler Thromb Vasc Biol. 2016 Jun;36(6):1152-63. doi: 10.1161/ATVBAHA.115.306991. Epub 2016 Apr 14.
Kassa T, et al. Sickle Cell Hemoglobin in the Ferryl State Promotes βCys-93 Oxidation and Mitochondrial Dysfunction in Epithelial Lung Cells (E10). J Biol Chem. 2015 Nov 13;290(46):27939-58. doi: 10.1074/jbc.M115.651257. Epub 2015 Sep 22.
Ref:
Strop, P., et al. 1981. J. Chromat. 214, 317; Miller, Y.I., et al. 1996. Biochem. 35, 13112.
