PNP, human recombinant protein
Purine nucleoside phosphorylase, NP, Inosine phosphorylase, PRO1837, PUNP
|Calculated MW||34.2 kDa (309 aa, 1-289 aa + His Tag)|
|Other Names||Purine nucleoside phosphorylase, NP, Inosine phosphorylase, PRO1837, PUNP|
|Results||Specific activity is > 40,000 pmol/min/ µg|
|Sequence||MGSSHHHHHH SSGLVPRGSH MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY GEIPNFPRST VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FSGQNPLRGP NDERFGDRFP AMSDAYDRTM RQRALSTWKQ MGEQRELQEG TYVMVAGPSF ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS|
|Storage||-20°C; 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol, 2 mM DTT and 0.1 M NaCl|
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PNP belongs to the PNP/MTAP phosphorylase family of proteins. This protein catalyzes the reversible phosphorolysis of ribonucleosides and 2'-deoxyribonucleosides with specificity for guanine, hypoxanthine and their analogs. PNP deficiency is a rare autosomal recessive genetic disease associated with a severe defect in T-lymphocyte function and neurologic disorder in children, comprising four percent of combined immunodeficiency cases. Recombinant human PNP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques
Williams S.R.,et al.Nucleic Acids Res. 12:5779-5787(1984).
Williams S.R.,et al.J. Biol. Chem. 262:2332-2338(1987).
Yu L.,et al.Environ. Health Perspect. 111:1421-1427(2003).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Ebert L.,et al.Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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