| Description | ARHGEF17 Human Pre-designed siRNA Set A contains three designed siRNAs for ARHGEF17 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ARHGEF17 siRNA-1: 5 nmol (HPLC) ARHGEF17 siRNA-2: 5 nmol (HPLC) ARHGEF17 siRNA-3: 5 nmol (HPLC) siRNA ARHGEF17 Human Pre-designed siRNA Set A contains three designed siRNAs for ARHGEF17 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ARHGEF17 siRNA-1: 5 nmol (HPLC) ARHGEF17 siRNA-2: 5 nmol (HPLC) ARHGEF17 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 | Inquire | Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towardsArachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towards ?-D-Gal(1-3)-D-galNAc. It has potent anti-T activity and can be used to distinguish between human lymphocyte subsets. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 µg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose. PNA lectin is provided as a white to light yellow lyophilized powder from a buffer containing 10 mM NH4HCO3. The purity is determined by SDS-PAGE, which generates one band at 25-27 kDa.● Ultrapure quality ● Strong anti-T activity ● Sugar specificity: ?-D-Gal-(1-3)-D-GalNAc ● Agglutinates rabbit erythrocytes at < 0.1 µg/ml after trypsin treatment of the cells ● Lyophilized powderProbe in histochemistry and immuno-histochemistry;Human erythrocyte/lymphocyte studies... Read More | Human PTHrP-(1-36) is a secretory form of PTHrP with anticalciuric effects. Human PTHrP-(1-36) enhances beta cell function and proliferation. Human PTHrP-(1-36) can be used in the research of humoral hypercalcemia of malignancy (HHM) and hyperparathyroidism.In VitroHuman PTHrP-(1-36) (EC 50 : 0.05 Human PTHrP-(1-36) is a secretory form of PTHrP with anticalciuric effects. Human PTHrP-(1-36) enhances beta cell function and proliferation. Human PTHrP-(1-36) can be used in the research of humoral hypercalcemia of malignancy (HHM) and hyperparathyroidism.In VitroHuman PTHrP-(1-36) (EC 50 : 0.05 nM) increases intracellular calcium in human epidermal keratinocytes. Human PTHrP-(1-36) (100 nM, 24 h) increases human β-cell proliferation. Human PTHrP-(1-36) (100 nM, 30 min) enhances insulin secretion in human islets. PTHrP-(1-36) (mouse, EC 50 : 1 nM) induces a rapid Ca 2+ response in UMR 106 cells. MCE has not independently confirmed the accuracy of these methods. They are for reference only.In VivoPTHrP-(1-36) (mouse, 160 µg/kg, s.c., for 5 days/week for 7, 30, or 90 days) enhances beta cell regeneration and increases beta cell mass in a mouse model of partial pancreatectomy. PTHrP-(1-36) (mouse, 100 µg/kg, s.c., every other day) reverses the observed decrease of Wisp1 expression in the diabetic mice. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... Read More | Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |