| Description | 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 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.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.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... Read More | Inquire | IFN-αs are proteins secreted by leukocyte. They are mainly involved in innate immune response against viral infection. The IFN-α family has 13 subtypes and 23 different variants. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166IFN-αs are proteins secreted by leukocyte. They are mainly involved in innate immune response against viral infection. The IFN-α family has 13 subtypes and 23 different variants. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end... Read More | Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by recruiting leukocytes to acute and chronic inflammation sites. Alternatively-spliced forms are known to occur, but the most common form is a type I transmembrane protein with a 674 aa extracellular domain (ECD) that includes seven C2-type immunoglobulin domains, a 22 aa transmembrane segment, and a 19 amino acid (aa) cytoplasmic tail. Within the ECD, human VCAM-1 shares 75% and 76% aa sequence identity with the mouse and rat VCAM-1, respectively. VCAM-1 binds to leukocyte integrins alpha 4 beta 1 (VLA-4) and alpha 4 beta 7. During the inflammatory adhesion mechanism, activated integrins halt rolling leukocytes and attach them firmly to the vascular endothelium. The VCAM-1:VLA-4/ alpha 4 beta 7 interaction is also thought to be involved in the extravasation of white blood cells through the blood vessel wall to sites of inflammation. ELISA techniques have shown that detectable levels of soluble VCAM-1 are present in the biological fluids of apparently normal individuals, but elevated levels of serum VCAM-1 are indicative of future Atrial Fibrillation incident as well as liver disease. Tumor cells use overexpression of VCAM-1 as means of escaping immune surveillance.Post-translational modifications:Sialoglycoprotein.Function:Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation... Read More | Inquire |