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540221

Sigma-Aldrich

Purine Nucleoside Phosphorylase, Human, Recombinant, E. coli

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Synonym(s):
PNP
UNSPSC Code:
12352202
NACRES:
NA.42

recombinant

expressed in E. coli

Quality Level

form

liquid

specific activity

≥25 units/mg protein

manufacturer/tradename

Calbiochem®

shipped in

dry ice

storage temp.

−20°C

General description

Recombinant, human purine nucleotide phosphorylase expressed in E. coli without tags. Purine nucleoside phosphorylase catalyzes the phosphorlysis of N-ribosidic bonds of purine nucleosides and deoxynucleosides in a reversible reaction. Human PNP is a target for therapeutic T-cell immune response intervention. Useful in the detection of inorganic phosphate from biochemical reactions.
Recombinant, human purine nucleotide phosphorylase expressed in E. coli without tags. Purine nucleoside phosphorylase catalyzes the phosphorolysis of N-ribosidic bonds of purine nucleosides and deoxynucleosides. This reaction is reversible. The human enzyme is a target for therapeutic immune response intervention.

Warning

Toxicity: Standard Handling (A)

Unit Definition

One unit is defined as the amount of enzyme that will convert 1 µmol of MESG and 1 µmol of Pi into 1 µmol of 2-amino-6-mercapto-7-methylpurine and 1 µmol of ribose phosphate in 1 min at 25°C, pH 7.6.

Physical form

In 50 mM Tris-HCl, pH 7.6.

Analysis Note

Single band by SDS-PAGE

Other Notes

Filgueira de Azevedo, W.Jr., et al. 2003. Biochem. Biophys. Res. Commun.309, 917.
Silva, R.G., et al. 2003. Protein Expr. Purif.27, 158.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Roman S Iwasaki et al.
Nucleic acids research, 48(17), e101-e101 (2020-08-17)
Recent efforts in biological engineering have made detection of nucleic acids in samples more rapid, inexpensive and sensitive using CRISPR-based approaches. We expand one of these Cas13a-based methods to detect small molecules in a one-batch assay. Using SHERLOCK-based profiling of

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