| Description | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 4.19 | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Inquire | 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 | The recombinant Protein A is a genetically engineering protein containing IgG-binding domains.Recombinant Protein A is ideal for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to most human and mouse IgG subclasses (e.g., human IgG1, IgG2, IgG4; mouse IgG2, IgG2a, IgG2b,The recombinant Protein A is a genetically engineering protein containing IgG-binding domains.Recombinant Protein A is ideal for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to most human and mouse IgG subclasses (e.g., human IgG1, IgG2, IgG4; mouse IgG2, IgG2a, IgG2b,IgG3). It also binds to cow, guinea pig, hamster, house, pig and rabbit total IgG form.Recombinant protein A can be coupled to solid separation medium (such as agarose) for monoclonaland polyclonal antibody purification. Recombinant protein A can be coupled to a variety of molecules (such as fluorescent molecules, enzyme markers, biotin, colloidal gold and radioactive markers). These coupled derivatives can be used in antibody test in the process of Western-blot, ELISA or immunohistochemical tests... Read More |