| 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 | Sequence:Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-AlaBiochemical mechanism:Amyloid protein β Protein segment 1-42 (A β 1-42) It has antioxidant and neuroprotective Sequence:Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-AlaBiochemical mechanism:Amyloid protein β Protein segment 1-42 (A β 1-42) It has antioxidant and neuroprotective properties. Amyloid protein β Protein accumulation is associated with Alzheimer's disease (AD) and Down syndrome. A β 1-42 regulates cholesterol transport and acts as a transcription factor. It may also have anti-inflammatory and antimicrobial effects.Application:Amyloid protein is found in the brain of patients with Alzheimer's disease and Down syndrome β- The main segment of the protein.Amyloid protein β Protein fragments 1-42 have been used to:1. A β Preparation of 1-42 oligomer2. Western blot analysis3. Immunomagnetic Reduction (IMR) Plasma A β 42 Detected interference test4. Study the effect of resveratrol on A β 1-42 induced impairment of spatial learning, memory and synaptic plasticity5. Study A β Role in epithelial cell culture... Read More | Reverse transcriptases are enzymes encoded in retroviruses viral genome. The enzyme is responsible for transcription of the viral RNA to produce a dsDNA that can be inserted into the host genome.Reverse transcriptases are multifunctional enzymes. These enzymes exhibit an RNA and DNA directed Reverse transcriptases are enzymes encoded in retroviruses viral genome. The enzyme is responsible for transcription of the viral RNA to produce a dsDNA that can be inserted into the host genome.Reverse transcriptases are multifunctional enzymes. These enzymes exhibit an RNA and DNA directed polymerase activity. In addition reverse transcriptases catalyze the degradation of RNA in an RNA-DNA hybrid. The exonucleolytic activity proceeds in a 5' ---> 3' direction. The RNA or DNA directed activity requires a template (RNA or DNA) and a primer. The following is a schematic illustration of the reaction:Unit definition: One unit incorporates 1 nanomole of tritiated dTMP into acid insoluble productsusing poly(A)•oligo(dT) 12-18 as the template-primer in 20 minutes at 37° C.ApplicationsHIV reverse transcriptase is used for research on the AIDS primer. However it can be substituted for AMV reverse transcriptase, which is mainly used to transcribe mRNA into double stranded cDNA, that can be inserted into prokaryotic vectors. The enzyme can also be used with either single stranded DNA or RNA templates to make probes for use in hybridization experiments. It can be used for labeling the termini of DNA fragments with protruding 5' termini. The enzyme can also be used to sequence DNAs by the dideoxy chain termination method of Sanger when the Klenow fragment of E. coli DNA polymerase I, or the T7 DNA polymerase yield unsatisfactory results.Reagents0.05 M Tris, pH 8.3, containing 0.008 M MgCl21 mg/ml polyadenylic acid in water (poly A)DNA primer:Oligo d(T)12-181 µ mole dTTP/mL stock solution[methyl-3H]-Thymidine 5'-triphosphate (3H-dTTP)dTTP-3H-dTTP working mix: Add 1-2 µL 3H-dTTP per mL of 100 nmol/mL dTTP in order to obtain 1 to 1.5 x 105 cpm/mL1% bovine serum albumin10% perchloric acid1% perchloric acidBuffer substrate reaction mixture: Prepare fresh, immediately before use:For each 1mL of reaction mixture required mix:0.7 mL Tris/HCl, pH 8.3, 0.008M MgCl20.3 mL 1 mg/mL poly(A) RNA template0.005 mL 0.02 mg/mL oligo d(T)12-18 DNA primer0.02mL 1% BSAEnzymedilute as needed wtih 0.05M Tris/HCl, pH 8.3, 0.008M MgCl2 containing 0.1 mg/mL (1%) BSAProcedurePipette into each tube as follows:Buffer substrate mix：0.1 mLdTTP-3H3-dTTP：0.1 mLEnzyme：5-10 µLIncubate 20 minutes at 37° C. Stop reaction by adding 1 ml 10% cold perchloric acid. Filter through 0.2µ manifold filters used with Millipore vacuum manifold. Wash four times using 2mL 1% cold perchloric acid/wash. Transfer filter to scintillation vials. Add 2mL Cellosolve (or 2-methoxyethanol) to dissolve filter. Filters become opaque upon addition of Cellosolve. Make sure filters are dissolved before proceeding. Add 10mL scintillation cocktail and count.Calculation... 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 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 | Purity＞98% (SDS-PAGE; HPLC). Purity is greater than 98% as determined by SEC-HPLC and reducing SDS-PAGE.FunctionCytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.Purity＞98% (SDS-PAGE; HPLC). Purity is greater than 98% as determined by SEC-HPLC and reducing SDS-PAGE.FunctionCytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.Human Granulocyte-Macrophage Colony Stimulating Factor Granulocyte-Macrophage Colony Stimulating Factor (GM-CSF) is secreted by a number of different cell types (including activated T cells, B cells, macrophages, mast cells, endothelial cells and fibroblasts) in response to cytokine or immune and inflammatory stimulation. It was initially characterized as a growth factor that can support the in vitro colony formation of granulocyte-macrophage progenitors and has functions of stimulates the growth and differentiation of hematopoietic precursor cells from various lineages. GM-CSF has also been reported to have a functional role on non-hematopoietic cells and can induce human endothelial cells to migrate and proliferate. Additionally, it can stimulate the proliferation of a number of tumor cell lines, including osteogenic sarcoma, carcinoma and adenocarcinoma cell lines. GM-CSF is used as a medication to stimulate the production of white blood cells following chemotherapy and has also recently been evaluated in clinical trials for its potential as a vaccine adjuvant in HIV-infected patients. The recombinant Human GM-CSF is a non-glycosylated polypeptide chain containing 127 amino acids... Read More |