| Description | Biochemical Test:Electrophoresis (purity > 80%)Calculated Isoelectric Point:pH 6.9 | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (By similarity).Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (By similarity).Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger. Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation (By similarity).Fc-binding subunit that associates with FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation (By similarity).Mediates enhanced ADCC in response to afucosylated IgGs... Read More | Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer... 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 | BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L,BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Unlike egg-white avidin, which has a net positive charge at neutral pH and contains about 7% carbohydrate, streptavidin has almost no net charge at neutral pH, does not contain carbohydrate, and exhibits lower non-specific background. Streptavidin conjugates are widely used together with a conjugate of biotin for specific detection of a variety of proteins, protein motifs, nucleic acids and other molecules. This FITC-streptavidin conjugate was prepared by highly purified Streptavidin and free FITC was removed. Streptavidin (FITC) is a useful second-step reagent for the indirect immunofluorescent staining of cells in combination with biotinylated primary antibodies for flow cytometric analysis. Excitation at 488nm light leads to a fluorescence emission maximum of 520 nm.Recommended Usage：Every lot of Streptavidin-FITC is tested by flow cytometry using biotinylated primary antibodies. From this testing it is recommended that between 0.02 and 0.25 µg of streptavidin be used per 106 cells in a 100 µl staining volume... Read More |