| Description | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.99 | 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 | Product IntroductionHuman epidermal growth factor (EGF) has a molecular weight of 6 KD, contains 53 amino acids, and has three intramolecular disulfide bonds.Upon binding to EGFR, a specific receptor located on the cell surface, EGF causes a series of biochemical reactions in the cell: increasing Product IntroductionHuman epidermal growth factor (EGF) has a molecular weight of 6 KD, contains 53 amino acids, and has three intramolecular disulfide bonds.Upon binding to EGFR, a specific receptor located on the cell surface, EGF causes a series of biochemical reactions in the cell: increasing the level of calcium ion concentration in the cell, promoting the progress of glycolysis, increasing the synthesis of proteins, and can enhance the expression of EGFR, a specific class of genes to promote DNA synthesis and cell proliferation.Specification parametersSource Pichia pastorisAppearance white lyophilized powderActivity ≥1.0×106IU/mgpH 6.5-7.5Molecular weight 6.5kDEndotoxin ≦1.0 EU/mgCAS No 62253-63-8Matters needing attentionReconstitution: reconstitution of REGF lyophilized powder to 100-200 µg/ml with sterile water is recommended and further dilution with other solvents may be performed.REGF dissolved at 4 ° C can be stored for 2-7 days and used up as soon as possible.To not use for short periods, store at - 20 ℃.Use as soon as possible after opening to avoid contamination.Limitations of useIt is suitable for research, laboratory and production use only and cannot be used directly in humans... Read More | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map (PubMed:23307924). Required for normal formation of bones and joints in the limbs, skull, digits and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. Regulation of GDF6 expression seems to be a mechanism for evolving species-specific changes in skeletal strucutres. Seems to positively regulates differentiation of chondrogenic tissue through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A, leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation of chondrogenic differentiation is inhibited by NOG (PubMed:26643732). Also involved in the induction of adipogenesis from mesenchymal stem cells. This mechanism acts through the growth factor receptors subunits BMPR1A, BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and MAPK14/p38... 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 |