| Description | KPNA6 Human Pre-designed siRNA Set A contains three designed siRNAs for KPNA6 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KPNA6 siRNA-1: 5 nmol (HPLC) KPNA6 siRNA-2: 5 nmol (HPLC) KPNA6 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:KPNA6 Human Pre-designed siRNA Set A contains three designed siRNAs for KPNA6 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KPNA6 siRNA-1: 5 nmol (HPLC) KPNA6 siRNA-2: 5 nmol (HPLC) KPNA6 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | IRAK-4 protein kinase inhibitor 2 (compound 1) is a potent inhibitor of interleukin-1 (IL-1) receptor-associated kinase-4 (IRAK-4), with an IC 50 of 4 µM. IRAK-4 protein kinase inhibitor 2 can be used for the research of inflammatory and immune-related conditions or disordersIn VitroIRAK-4 IRAK-4 protein kinase inhibitor 2 (compound 1) is a potent inhibitor of interleukin-1 (IL-1) receptor-associated kinase-4 (IRAK-4), with an IC 50 of 4 µM. IRAK-4 protein kinase inhibitor 2 can be used for the research of inflammatory and immune-related conditions or disordersIn VitroIRAK-4 protein kinase inhibitor 2 (compound 1) also inhibits IRAK-1, with an IC 50 of <10 µM. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:IRAK4 4 µM (IC 50 )... Read More | Recombinant human basic fibroblast growth factor (also known as basic FGF, bFGF, FGF2, FGF-beta, or heparin-binding growth factor), is a biologically active protein suitable for cell culture applications. bFGF regulates diverse processes such as cell proliferation, differentiation, survival, Recombinant human basic fibroblast growth factor (also known as basic FGF, bFGF, FGF2, FGF-beta, or heparin-binding growth factor), is a biologically active protein suitable for cell culture applications. bFGF regulates diverse processes such as cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation, and wound recovery. bFGF can be used in studies of angiogenesis, fibroblast mitosis, axonal outgrowth in PC-12 cells, receptor binding, and tyrosine phosphorylation. This strain is expressed in recombinant Escherichia coli, and after multi-step separation and purification, it is dissolved in 10mM PBS, 0.15 M NaCl (pH7.2) solution, filtered through a 0.22 µm filter membrane, and then freeze-dried to make a lyophilized powder... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:ROR1 (Receptor tyrosine kinase-like orphan receptor 1), also known as neurotrophic tyrosine kinase receptor-related 1 (NTRKR1), is a member of the ROR family within the receptor tyrosine kinases (RTK) superfamily. Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:ROR1 (Receptor tyrosine kinase-like orphan receptor 1), also known as neurotrophic tyrosine kinase receptor-related 1 (NTRKR1), is a member of the ROR family within the receptor tyrosine kinases (RTK) superfamily. Two ROR family members (ROR1 and ROR2) have been identified and are characterized by their intracellular tyrosine kinase domains, which are highly related to those of the Trk-family receptor tyrosine kinases, and by their extracellular Frizzled-like cysteine-rich domains and kringle domains, common to receptors of the Wnt family members. Human ROR1 is a type I transmembrane protein with 937 amino acids in length. It contains a 29 amino acid signal sequence, a 377 amino acid extracellular domain (ECD), a 21 amino acid transmembrane segment, and a 510 amino acid cytoplasmic region. Human ROR1 shares 97% and 58% amino acid sequence identity with mouse ROR1 and human ROR2, respectively. ROR1 has been shown to play crucial roles in developmental morphogenesis by acting as receptors or co-receptors to mediate Wnt5a-induced signaling. The bioactivity of ROR1 is measured by its ability to bind biotinylated recombinant mouse Wnt-5a in a functional ELISA... 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 |