| 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 | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: CD4, also known as L3T4, T4, and W3/25, is an approximately 55 kDa type I transmembrane glycoprotein that is expressed predominantly on thymocytes and a subset of mature T lymphocytes. It is a standard phenotype marker for the identification of T cell populations. Mature human CD4 consists of a 371 amino acid (aa) extracellular region containing four immunoglobulin-like domains, a 22 aa transmembrane segment, and a 40 aa cytoplasmic domain. Within the ECD, human CD4 shares approximately 52% aa sequence identity with mouse and rat CD4. CD4 is expressed along with CD8 on double positive T cells during their development in the thymus. Either CD4 or CD8 expression is then lost, giving rise to single positive (SP) CD4+ or CD8+ mature T cells. CD4+ SP cells, also known as T helper cells, further differentiate into multiple subsets of CD4+ cells including Th1, Th2, Th17, Tfh, and Treg cells which regulate humoral and cellular immunity. CD4 is reexpressed on circulating CD8+ T cells upon activation and contributes to their cytotoxic effector activity. In human, CD4 is additionally expressed on macrophages, neutrophils, monocytes, NK cells, and neurons and glial cells in the brain. Similar CD4 distribution between species cannot be assumed as demonstrated by its presence on macrophages in human and rat but not in mouse. CD4 binds directly to MHC class II molecules on antigen presenting cells. This interaction contributes to the formation of the immunological synapse which is focused around the TCR-MHC class II-antigenic peptide interaction. Palmitoylation of two cysteine residues in the cytoplasmic tail of CD4 promotes the localization of CD4 in lipid rafts and its ability to augment TCR signaling via activation of the tyrosine kinase Lck. CD4 also functions as a chemotactic receptor for IL-16 and, in human, as a co-receptor for the gp120 surface glycoprotein of HIV-1... Read More | Purity>95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose Purity>95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.Post-translationalHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation... Read More | Inquire |