| Description | Highly purified bovine corium pepsin solubilized collagen, atelo collagen, in 0.01 N HCl, pH 2. Predominantly Type I collagen with approximately 5% Type III at 6 mg/ml.Sterile filtered.BSE-Free.≥95% purity by SDS PAGE.Suitable for Biomedical research.Forms a gel at pH 7 and is ideal for 3D Highly purified bovine corium pepsin solubilized collagen, atelo collagen, in 0.01 N HCl, pH 2. Predominantly Type I collagen with approximately 5% Type III at 6 mg/ml.Sterile filtered.BSE-Free.≥95% purity by SDS PAGE.Suitable for Biomedical research.Forms a gel at pH 7 and is ideal for 3D biomaterial scaffolds for cell culture, engineering tissue, and drug delivery... Read More | Inquire | Seals and prevents freezing of stopcocks and ground-glass joints in high-vacuum systems at pressures less than 10-6 mm Hg. Heat stable (?40 to 260 °C), low vapor pressure, and chemically resistant. Colorless. 5.3 oz. tube | Inquire | 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 |