Recombinant human Nucleoside phosphorylase protein (His tag N-Terminus)
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Recombinant human Nucleoside phosphorylase protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 289 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec, FuncS.
View Alternative Names
NP, PNP, Purine nucleoside phosphorylase, Inosine phosphorylase, Inosine-guanosine phosphorylase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human Nucleoside phosphorylase protein (His tag N-Terminus) (AB101210)
15% SDS-PAGE analysis of ab101210 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Nucleoside phosphorylase is important in maintaining nucleotide homeostasis. It operates as a monomer or part of a homotrimeric complex which allows it to efficiently catalyze its reactions in purine metabolism. The absence or dysfunction of PNP results in the accumulation of nucleosides and diminished levels of nucleotide pools which can severely hamper DNA replication and repair.
Pathways
Nucleoside phosphorylase plays an integral role in the purine salvage pathway which is vital for recycling purines to form new nucleotides. It works alongside other enzymes such as adenine phosphoribosyltransferase to conserve energy by recycling purines. This pathway connects closely with the hypoxanthine-guanine phosphoribosyltransferase (HGPRT) pathway showing how PNP is intertwined in broader nucleotide biosynthesis and degradation processes.
Specifications
Form
Liquid
Additional notes
ab101210 was purified using conventional chromatography techniques.
General info
Function
Catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed : 23438750, PubMed : 9305964). Preferentially acts on 6-oxopurine nucleosides including inosine and guanosine (PubMed : 9305964).
Sequence similarities
Belongs to the PNP/MTAP phosphorylase family.
Target data
Product promise
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