Recombinant Human NPL protein
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Recombinant Human NPL protein is a Human Full Length protein, in the 1 to 320 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
C1orf13, NPL, N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human NPL protein (AB106873)
15% SDS-PAGE analysis of 3μg ab106873.
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
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.
Specifications
Form
Liquid
Additional notes
ab106873 is purified using conventional chromatography techniques.
General info
Function
Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (PubMed : 33895133). It prevents sialic acids from being recycled and returning to the cell surface (PubMed : 33895133). Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (PubMed : 22692205, PubMed : 33895133). Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (Probable).
Sequence similarities
Belongs to the DapA family. NanA subfamily.
Target data
Product promise
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