Alkaline Phosphatase recombinant, highly active

Description

• General description: Alkaline phosphatase (ALP) is a hydrolase enzyme. It is a highly active form in calf intestinal mucosa.[1][2] The calf intestinal alkaline phosphatase is a dimeric glycoprotein with a molecular weight of about 140kDa.[3]
• Specificity: Alkaline phosphatase catalyzed the hydrolysis of numerous phosphate esters, such as esters of primary and secondary alcohols, saccarides, cyclic alcohols, phenols and amines. Phosphodiesters do not react. The enzyme hydrolyzes inorganic pyrophosphate. The kinetic properties of the enzyme depend on many factors, such as enzyme purity, enzyme concentration in the assay, buffer, pH etc.
• Application: Alkaline Phosphatase can be coupled to other proteins via its amino and carbohydrate groups. The enzyme solution can be used directly for conjugation without prior dialysis. For conjugation of AP with IgG, a ration of 2.5:1 is recommended. The application of the conjugated enzyme varies from ELISAs and microarrays to western blot analysis.
• Biochem/physiol Actions: Alkaline phosphatase (ALP) is responsible for removing phosphate groups at the 5- and 3- positions from many types of molecules, such as nucleotides, proteins, and alkaloids.[2] It can also modify lipopolysaccharides by dephosphorylation of the lipid A moiety, thereby making it less toxic than the unmodified lipid A.[4]
• Specifications: ≥7,000 U/mg (+37°C; pNPP; DEA)
• Physical form: Solution in 3 M NaCl, pH 7.6, 5 mM magnesium chloride, 0.1 mM zinc chloride, 30 mM triethanolamine.
• Preparation Note: Activator: Mg2-, Co2- and Mn2-ions
• Other Notes: For life science research only. Not for use in diagnostic procedures.