| Description | Antithrombin III is found in normal serum at 15 mg per 100 ml. Found at higher levels in plasma than in serum because of complexing with thrombin during coagulation. Functions in the inhibition of the proteolytic enzymes involved in blood coagulation and fibrinolysis, including factor Xa, plasmin, Antithrombin III is found in normal serum at 15 mg per 100 ml. Found at higher levels in plasma than in serum because of complexing with thrombin during coagulation. Functions in the inhibition of the proteolytic enzymes involved in blood coagulation and fibrinolysis, including factor Xa, plasmin, thrombin, and trypsin. Potency is strongly enhanced by heparin. Clinically, reduced levels are indicative of hypercoagulability. Extinction Coefficient: 0.65 Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
Purified Native Human Antithrombin III, Human PlasmaBulk Qty Available.Antithrombin III is found in normal serum at 15 mg per 100 ml. Found at higher levels in plasma than in serum because of complexing with thrombin during coagulation. Functions in the inhibition of the proteolytic enzymes involved in blood coagulation and fibrinolysis, including factor Xa, plasmin, thrombin, and trypsin. Potency is strongly enhanced by heparin. Clinically, reduced levels are indicative of hypercoagulability. Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.Athens Research & Technology products are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research use only.Product Citation:Perera, Natascha C., Oliver Schilling, Heike Kittel, Walter Back, Elisabeth Kremmer, and Dieter E. Jenne. "NSP4, an elastase-related protease in human neutrophils with arginine specificity. Proceedings of the National Academy of Sciences 109, no. 16 (2012): 6229-6234.Guo C, et al.High-resolution probing heparan sulfate–antithrombin interaction on a single endothelial cell surface: single-molecule AFM studies.Phys Chem Chem Phys. 2015 May 28;17(20):13301-6. doi: 10.1039/c5cp01305d.Tafaleng EN, et al.Induced pluripotent stem cells model personalized variations in liver disease resulting from α1-antitrypsin deficiency.Hepatology. 2015 Jul;62(1):147-57. doi: 10.1002/hep.27753. Epub 2015 Apr 13... Read More | Nucleoprotein (396-404) TFA is the 396 to 404 fragment of lymphocytic choriomeningitis virus (LCMV). Nucleoprotein (396-404) TFA is the H-2D(b)-restricted immunodominant epitope and can be used as a molecular model of viral antigen.Biological Activity:Nucleoprotein (396-404) TFA is the 396 to 404 Nucleoprotein (396-404) TFA is the 396 to 404 fragment of lymphocytic choriomeningitis virus (LCMV). Nucleoprotein (396-404) TFA is the H-2D(b)-restricted immunodominant epitope and can be used as a molecular model of viral antigen.Biological Activity:Nucleoprotein (396-404) TFA is the 396 to 404 fragment of lymphocytic choriomeningitis virus (LCMV). Nucleoprotein (396-404) TFA is the H-2D(b)-restricted immunodominant epitope and can be used as a molecular model of viral antigen... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Interleukin 33 (IL-33), also known as DVS27 or NF-HEV (Nuclear Factor from High Endothelial Venules), is a pro-inflammatory protein and a chromatin-associated cytokine of the IL-1 family with high sequencePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Interleukin 33 (IL-33), also known as DVS27 or NF-HEV (Nuclear Factor from High Endothelial Venules), is a pro-inflammatory protein and a chromatin-associated cytokine of the IL-1 family with high sequence and structural similarity to IL-1 and IL-18. IL-33 protein is expressed highly and rather selectively by high endothelial venule endothelial cells (HEVECs) in human tonsils, Peyer's patches, and lymph nodes. IL-33 protein has transcriptional regulatory properties, and the researches suggested that IL-33 is a dual-function protein that might act both as a cytokine and as an intracellular nuclear factor. As a type 2 cytokines, IL-33 protein also play a pivotal role in helminthic infection and allergic disorders... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Interleukin-6 (IL-6) is a pleiotropic, alpha-helical, 22-28 kDa phosphorylated and variably glycosylated cytokine that plays important roles in the acute phase reaction, inflammation, hematopoiesis, bone metabolism,Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:Interleukin-6 (IL-6) is a pleiotropic, alpha-helical, 22-28 kDa phosphorylated and variably glycosylated cytokine that plays important roles in the acute phase reaction, inflammation, hematopoiesis, bone metabolism, and cancer progression. Mature human IL-6 is 183 amino acids (aa) in length and shares 39% aa sequence identity with mouse and rat IL-6. Alternative splicing generates several isoforms with internal deletions, some of which exhibit antagonistic properties. IL-6 induces signaling through a cell surface heterodimeric receptor complex composed of a ligand-binding subunit (IL-6 R alpha) and a signal-transducing subunit (gp130). IL-6 binds to IL-6 R alpha, triggering IL-6 R alpha association with gp130 and gp130 dimerization. Gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM. Soluble forms of IL-6 R alpha are generated by both alternative splicing and proteolytic cleavage. In a mechanism known as trans-signaling, complexes of soluble IL-6 and IL-6 R alpha elicit responses from gp130-expressing cells that lack cell surface IL-6 R alpha. Trans-signaling enables a wider range of cell types to respond to IL-6, as the expression of gp130 is ubiquitous, while that of IL-6 R alpha is predominantly restricted to hepatocytes, monocytes, and resting lymphocytes. Soluble splice forms of gp130 block trans-signaling from IL-6/IL-6 R alpha but not from other cytokines that use gp130 as a co-receptor. IL-6, along with TNF-alpha and IL-1, drives the acute inflammatory response and the transition from acute inflammation to either acquired immunity or chronic inflammatory disease. When dysregulated, it contributes to chronic inflammation in obesity, insulin resistance, inflammatory bowel disease, arthritis, sepsis, and atherosclerosis. IL-6 can also function as an anti-inflammatory molecule, as in skeletal muscle where it is secreted in response to exercise. In addition, it enhances hematopoietic stem cell proliferation and the differentiation of Th17 cells, memory B cells, and plasma cells... Read More | Purity>95% SDS-PAGE.FunctionReceptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the Purity>95% SDS-PAGE.FunctionReceptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity... Read More |