Product Description
Size: 10µg
Recombinant Human PNP Protein Standard (His tag) is a Human Full Length protein, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE, sELISA.
Key facts
Purity:>80% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag C-Terminus,
Applications:sELISA, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P00491,
Animal free:Yes,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.3 - 7.5Constituents: 12.6% Glycerol (glycerin, glycerine), 2.922% Sodium chloride, 1.742% L-Arginine, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic
Product details:
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our
Scientific Support
team to know which antibody pair is suitable for this protein.
Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Nucleoside phosphorylase also known as PNP or purine nucleoside phosphorylase is an enzyme with a vital mechanical role in nucleoside metabolism. The enzyme facilitates the phosphorolytic cleavage of the glycosidic bond in nucleosides producing ribose 1-phosphate and free bases such as guanine and hypoxanthine. This catalytic function plays an important part in nucleotide salvage pathways. PNP has a molecular mass of approximately 32000 Daltons and shows expression predominantly in the lymphoid tissues including the thymus and spleen.
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.
Deficiencies in nucleoside phosphorylase correlate strongly with immunodeficiencies notably purine nucleoside phosphorylase deficiency (PNP deficiency) which leads to compromised T-cell immunity. This condition can result in recurrent infections and developmental delay. Additionally the enzyme's dysregulation associates with certain leukemias where altered nucleotide pools contribute to the proliferation of malignant cells. In these contexts PNP interacts with proteins central to these disorders including those involved in purine metabolism placing it at a critical junction for potential therapeutic intervention.
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Collaboration
Tony Tang
Email: Tony.Tang@iright.com
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