Bacterial alkaline phosphatase (E. coli)

Bacterial alkaline phosphatase (E. coli) nonspecifically catalyzes the removal of most phosphomonoester bonds from the 5' and 3' termini of DNA and RNA without degrading diphosphate or triphosphate linkages. The enzyme is purified from an E. coli strain that does not harbor RNase activity. Bacterial alkaline phosphatase (E. coli) is supplied in a buffer of 50 mM Tris-HCl (pH 8.0), 100 mM KCl, 1 mM MgCl₂, and 50% glycerol.

Cat. #	Product	Size	Price
2120B	Alkaline Phosphatase (E coli C75)	250 Units	USD $452.00
Bacterial Alkaline Phosphatase nonspecifically catalyzes the removal of most phosphomonoester bonds, but it does not degrade diphosphate or triphosphate linkages. The enzyme is purified from an E. coli strain lacks RNase. Alkaline Phosphatase is supplied in 50 mM Tris-HCl (pH 8.0), 100 mM KCl, 1 mM MgSO₄ and 50% glycerol. Cat. # 2120B contains 5 of Cat. # 2120A. Please refer to Cat. # 2120A for complete product documentation and resources. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Image Data Back 2120B: Alkaline Phosphatase (E coli C75)
2120A	Alkaline Phosphatase (E coli C75)	50 Units	USD $116.00
Bacterial Alkaline Phosphatase nonspecifically catalyzes the removal of most phosphomonoester bonds, but it does not degrade diphosphate or triphosphate linkages. The enzyme is purified from an E. coli strain lacks RNase. Alkaline Phosphatase is supplied in 50 mM Tris-HCl (pH 8.0), 100 mM KCl, 1 mM MgSO₄ and 50% glycerol. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 2120A: Alkaline Phosphatase (E coli C75)

More Information

Applications

Phosphate group removal to reduce self-ligation and vector background
Dephosphorylation of DNA 5' termini prior to kinase labeling reactions

Source

E. coli strain C75

Storage

–20°C

Note

Bacterial alkaline phosphatase (E. coli) is extremely stable and is not completely heat-inactivated; therefore, to inactivate the enzyme, reaction products need to be purified twice via phenol-chloroform extraction followed by ethanol precipitation.

Buffer

Supplied with 10X Reaction Buffer [500 mM Tris-HCl (pH 9.0), 10 mM MgCl₂]

Unit definition

One unit is defined as the amount of enzyme required to generate 1 µmol/min of p-nitrophenol from p-nitrophenylphosphate at 25°C and pH 8.0.

Concentration

0.5 U/µl

Product citations

Reid, T. W. & Wilson, I. B. E. coli Alkaline Phosphatase. Enzym. 4, 373–415 (1971).

Takanami, M. Analysis of the 5'-terminal nucleotide sequences of ribonucleic acids: I. The 5'-termini of Escherichia coli ribosomal RNA. J. Mol. Biol. 23, 135–48 (1967).

Additional product information

Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.

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