| 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 | Inquire | Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Receptor-1, PAR-1 Agonist induces activation of protein kinase C isoenzymes alpha and epsilon in human HT-29 colon carcinoma cells expressing PAR1 endogeneously. On the cellular level, Protease-Activated Receptor-1, PAR-1 Agonist and thrombin prompted HT-29 cell migration and matrix adhesion by a PKCepsilon-dependent mechanism as concluded because of the inhibition of PAR1-mediated effects by the PKC inhibitor bisindolylmaleimide I and the PKCepsilon translocation inhibitory peptide EAVSLKPT but not by the PKC inhibitor Gö 6976. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:PAR-1... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:BIRC5, also known as Survivin and EPR-1, is a member of theIAP family. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but BIRC5 has only a single BIR domain. It is expressed cell Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:BIRC5, also known as Survivin and EPR-1, is a member of theIAP family. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but BIRC5 has only a single BIR domain. It is expressed cell cycle-dependently and highly expressed at mitosis. As a multitasking protein, BIRC5 has dual roles in promoting cell proliferation and preventing apoptosis. Survivin is a component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Survivin acts as an important regulator of the localization of this complex. It may counteract a default induction of apoptosis in G2/M phase... Read More |