Abcam, ab223521, Anti-NPL antibody

Size: 50µL
Rabbit Polyclonal NPL antibody. Suitable for WB, ICC/IF and reacts with Mouse, Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human NPL aa 1-100.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human,
Applications:WB, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Fragment Protein within Human NPL aa 1-100. The exact immunogen used to generate this antibody is proprietary information.Q9BXD5

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein G, Purification notes-Purity >95%., Storage buffer-pH: 7.4Preservative: 0.03% Proclin 300Constituents: PBS, 50% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°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.
The NPL protein also known as N-acetylneuraminate pyruvate lyase is an enzyme that catalyzes the reversible cleavage of N-acetylneuraminic acid (Neu5Ac) into pyruvate and N-acetylmannosamine. This protein weighs approximately 34 kDa and takes part in the sialic acid metabolism pathway. NPL is mainly expressed in the liver and kidney tissues in humans. It demonstrates a structural requirement for metal ions such as magnesium or manganese as co-factors to stabilize its active form.
Biological function summary
N-acetylneuraminate pyruvate lyase influences the recycling and regulation of sialic acids which are vital components of cell surface molecules involved in cellular recognition and signaling. This protein acts as part of a larger metabolic network involving sialic acid biosynthesis and degradation. It supports cellular functions by recycling sialic acid which gets added to glycoproteins and glycolipids contributing to cell surface architecture and function.
Pathways
The sialic acid metabolism involving the NPL protein connects to the broader glycosylation pathways impacting cell-cell communication and pathogen recognition. The NPL protein interacts with enzymes like sialyltransferases which transfer sialic acids to glycan chains and it maintains the rate of Neu5Ac production and consumption. It also relates to neuraminidases which cleave sialic acids from glycoconjugates ensuring dynamic metabolic fluxes in cells.
The function of NPL protein ties to the regulation of sialic acid levels impacting conditions such as sialuria and macrophage activity in sepsis. Sialuria is associated with excessive Neu5Ac accumulation due to malfunctioning NPL. Additionally altered sialic acid levels can affect immune responses in sepsis where NPL indirectly influences pathways involving other proteins such as sialoadhesins which bind to sialic acids on cell surfaces.