| Description | COX5A Human Pre-designed siRNA Set A contains three designed siRNAs for COX5A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components COX5A siRNA-1: 5 nmol (HPLC) COX5A siRNA-2: 5 nmol (HPLC) COX5A siRNA-3: 5 nmol (HPLC) siRNA Negative Control:COX5A Human Pre-designed siRNA Set A contains three designed siRNAs for COX5A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components COX5A siRNA-1: 5 nmol (HPLC) COX5A siRNA-2: 5 nmol (HPLC) COX5A 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 | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein,Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein, released actively following cytokine stimulation as well as passively during cell death. It is the prototypic damage-associated molecular pattern (DAMP) molecule and has been implicated in several inflammatory disorders. HMGB1 signals via the receptor for advanced glycation end-product (RAGE) and members of the toll-like receptor (TLR) family. The most prominent HMGB1 protein and mRNA expression arthritis are present in pannus regions, where synovial tissue invades articular cartilage and bone. HMGB1 promotes the activity of proteolytic enzymes, and osteoclasts need HMGB1 for functional maturation. As a non-histone nuclear protein, HMGB1 has a dual function. Inside the cell, HMGB1 binds DNA, regulating transcription, and determining chromosomal architecture. Outside the cell, HMGB1 can serve as an alarmin to activate the innate system and mediate a wide range of physiological and pathological responses. Extracellular HMGB1 represents an optimal " necrotic marker" selected by the innate immune system to recognize tissue damage and initiate reparative responses. However, extracellular HMGB1 also acts as a potent pro-inflammatory cytokine that contributes to the pathogenesis of diverse inflammatory and infectious disorders. HMGB1 has been successfully therapeutically targeted in multiple preclinical models of infectious and sterile diseases including arthritis. As shown in studies on patients as well as animal models, HMGB1 can play an important role in the pathogenesis of the rheumatic disease, including rheumatoid arthritis, systemic lupus erythematosus, and polymyositis among others. Besides, enhanced postmyocardial infarction remodeling in type 1 diabetes mellitus was partially mediated by HMGB1 activation... Read More | Inquire | Fibroblast growth factor-21 (FGF-21) belongs to the large FGF family and it is specifically induced by HMGCS2 activity. In mice, brown adipose tissue becomes a source of systemic FGF21 after cold exposure. FGF-21 stimulates glucose uptake in differentiated adipocytes via the induction of glucose Fibroblast growth factor-21 (FGF-21) belongs to the large FGF family and it is specifically induced by HMGCS2 activity. In mice, brown adipose tissue becomes a source of systemic FGF21 after cold exposure. FGF-21 stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression and the activity depends on the presence of KLB. FGF-21, in the presence of β-Klotho as a protein cofactor, signals through the FGFR 1c and 4 receptors. Murine FGF-21 shows limited binding to heparin. In addition, Murine FGF-21 respectively shows 81% and 92% a.a. identity to human and rat FGF-21, and it show activity on human and rat cells. Recombinant Murine FGF21 is a 19.9kDa globular protein containing 182 amino acid residues.Purity>96%(SDS-PAGE, HPLC)Additional sequence informationA single non-glycosylated polypeptide chain containing 182 amino acids. This product is for the mature full length protein. The signal peptide is not included.FunctionStimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity requires the presence of KLB... Read More | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |