| Description | DescriptionSulfhydryl Blocked proprietary manufacturing process effectively blocks free thiol groups to provide a high monomer albumin with less cross-reactivity. Applications include, but are not limited to, Immunoassays (RIA, EIA, etc.), Hybridization, Protein Standard, Diluent, Conjugate or DescriptionSulfhydryl Blocked proprietary manufacturing process effectively blocks free thiol groups to provide a high monomer albumin with less cross-reactivity. Applications include, but are not limited to, Immunoassays (RIA, EIA, etc.), Hybridization, Protein Standard, Diluent, Conjugate or Enzyme Stabilizer.ApplicationsProtease-sensitive Immunoassays (i.e. RIA, EIA, Fluorescent & Chemiluminescent)Protein Standard, DiluentProtein, Conjugate or Enzyme StabilizerX Thiol sensitive applications (quantification of thiol containing analytes, chemiluminescent assays, or conjugations)Selected cell culture applicationsFeatures/BenefitsFree of reactive sulfhydryl groupsFree of interfering immunoglobulinsHigh purity, low interference, low backgroundVirtually no detectable protease activity, ensures assay integritySuperior solubility/filterability for ease of useManufactured from MPI inspected bovine plasmaSpecificationsProtein (dry basis) ≥ 98.0%Purity (albumin) ≥ 98%Moisture ≤ 5.0%BIgG None DetectedSodium ≤ 15.0 mg/gChloride ≤ 6.0 mg/gFree Sulfhydryl Content ≤ 0.1 mol/mol albuminpH (7% Solution)/Temp 6.5-7.5/AmbientProtease None DetectedPhysical CharacteristicsBovine Serum Albumin is a highly soluble yellow to green with tan to green cast lyophilized powder. A solution of up to 30% in de-ionized water is clear to slightly hazy and virtually particulate-free.Storag RecommendationsStore sealed in a cool, dry environment for 3 years, and up to 5 years with re-qualification... Read More | Inquire | Purity：>95%(SDS-PAGE) Function：Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface Purity：>95%(SDS-PAGE) Function：Cooperates with MD-2 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Up-regulates cell surface molecules, including adhesion molecules.Background：CD14 is a 55 kDa cell surface glycoprotein that is preferentially expressed on monocytes/macrophages. The human CD14 cDNA encodes a 375 amino acid (aa) residue precursor protein with a 19 aa signal peptide and a C-terminal hydrophobic region characteristic for glycosylphosphatidyinositol (GPI)-anchored proteins. Human CD14 has four potential N-linked glycosylation sites and also bears O-linked carbohydrates. The amino acid sequence of human CD14 is approximately 65% identical with the mouse, rat, rabbit, and bovine proteins. CD14 is a pattern recognition receptor that binds lipopolysaccharides (LPS) and a variety of ligands derived from different microbial sources. The binding of CD14 with LPS is catalyzed by LPS-binding protein (LBP). The toll-like-receptors have also been implicated in the transduction of CD14-LPS signals. Similar to other GPI-anchored proteins, soluble CD14 can be released from the cell surface by phosphatidyinositol-specific phospholipase C. Soluble CD14 has been detected in serum and body fluids. High concentrations of soluble CD14 have been shown to inhibit LPS-mediated responses. However, soluble CD14 can also potentiate LPS response in cells that do not express cell surface CD14... Read More | purity>97% by SDS-PAGE and HPLC analysesFunctionFunctionElicits growth inhibition on melanoma cells in vitro as well as some other neuroectodermal tumors, including gliomas.Post-translationalMay possess two intramolecular disulfide bonds | 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 |