| Description | ATWLPPR Peptide TFA, a heptapeptide, acts as a selective neuropilin-1 inhibitor, inhibits VEGF 165 binding to NRP-1, used in the research of angiogenesis. ATWLPPR Peptide TFA has potential in reducing the early retinal damage caused by diabetes. Appearance:SolidIC50& Target:Neuropilin-1In Vitro:ATWLPPR Peptide TFA, a heptapeptide, acts as a selective neuropilin-1 inhibitor, inhibits VEGF 165 binding to NRP-1, used in the research of angiogenesis. ATWLPPR Peptide TFA has potential in reducing the early retinal damage caused by diabetes. Appearance:SolidIC50& Target:Neuropilin-1In Vitro:ATWLPPR Peptide TFA is a selective neuropilin-1 inhibitor, inhibits VEGF 165 binding to NRP-1 by 82% at 100 µM. MCE has not independently confirmed the accuracy of these methods. They are for reference only.In Vivo:ATWLPPR (400 µg/kg, s.c.) preserves vascular integrity and decreases the oxidative stress level, possibly reduces the early retinal damage caused by diabetes. ATWLPPR prevents the increase of inflammation-associated proteins (GFAP, VEGF and ICAM-1) iBiological Activity:ATWLPPR Peptide TFA, a heptapeptide, acts as a selective neuropilin-1 inhibitor, inhibits VEGF 165 binding to NRP-1, used in the research of angiogenesis. ATWLPPR Peptide TFA has potential in reducing the early retinal damage caused by diabetes... Read More | Inquire | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Epitope tagging offers an easy and universalPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Epitope tagging offers an easy and universal strategy for the identification and purification of proteins derived by recombinant DNA technology. The insertion of a Maltose Binding Protein (MBP) tag creates a stable fusion product that does not interfere with the bioactivity of the protein or with the biodistribution of the MBP tagged product... 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 | Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The HOLOenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase... Read More |