| Description | Purity: Single arc by IEP against antisera to whole human serum and human IgG; no reaction to antisera to human IgA, IgD, IgE, or IgM;greater than 95% by SDS-PAGE and ELISA.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA Purity: Single arc by IEP against antisera to whole human serum and human IgG; no reaction to antisera to human IgA, IgD, IgE, or IgM;greater than 95% by SDS-PAGE and ELISA.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.Product Citation:Devaux JJ, Miura Y, Fukami Y, Inoue T, et al. Neurofascin-155 IgG4 in chronic inflammatory demyelinating polyneuropathy. Neurology. 2016 Mar 1;86(9):800-7. doi: 10.1212/WNL.0000000000002418. Epub 2016 Feb 3.IgG Subclasses and Isotypes of VH4-34 Encoded Antibodies. Bhat NM, Kshirsagar MA, Bieber MM, and Teng NNH. Immunol Invest. 2015;44(4):400-10. doi: 10.3109/08820139.2015.1015682... Read More | The content of this cell is too long for an XLSX file (more than 32767 characters). Please use the CSV format for this export | Gly-Pro-pNA hydrochloride is a dipeptidyl peptidase inhibitor that inhibits dipeptidyl peptidase II, dipeptidyl peptidase IV and dipeptidyl peptidase IX | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3）Less than 10ppm of recombinant trypsin... 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.One Unit yields 1µmole of CO2 per minute from L-tyrosine at 37°C, pH 5.5. The APOenzyme activity is measured in the presence of excess pyridoxal phosphate... Read More |