NPL Human

N-acetylneuraminate Pyruvate Lyase Human Recombinant
Cat. No.
BT7289
Source
Escherichia Coli.
Synonyms
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.
NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
N-acetylneuraminate lyase (NAL) is an enzyme responsible for catalyzing the breakdown of N-acetylneuraminate into N-acetyl-D-mannosamine and pyruvate. This enzyme belongs to the oxo-acid-lyase family, known for their ability to cleave carbon-carbon bonds. NAL plays a crucial role in the metabolic processes of amino sugars.
Description
Produced in E. coli, our NAL is a single, non-glycosylated polypeptide chain consisting of 340 amino acids (specifically, amino acids 1 to 320). With a molecular weight of 37.3 kDa, our NAL is fused to a 20 amino acid His-tag at the N-terminus and undergoes rigorous purification using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
Our NAL protein solution is provided at a concentration of 1 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 20% glycerol, 0.1 M NaCl, and 1 mM DTT.
Stability
For optimal storage, refrigerate the product at 4°C if the entire vial will be used within 2-4 weeks. For extended storage, freeze at -20°C. To further enhance long-term stability, consider adding a carrier protein such as HSA or BSA at a concentration of 0.1%. It is crucial to minimize freeze-thaw cycles to maintain product integrity.
Purity
Our NAL protein exhibits a purity exceeding 95.0%, as determined by SDS-PAGE analysis.
Synonyms
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.

Product Science Overview

Introduction

N-acetylneuraminate pyruvate lyase, also known as sialic acid aldolase, is an enzyme that plays a crucial role in the metabolism of sialic acids. Sialic acids are a family of nine-carbon sugars that are found on the surfaces of cells and are involved in various biological processes, including cellular communication, migration, adhesion, and infection processes . The enzyme catalyzes the reversible cleavage of N-acetylneuraminic acid (Neu5Ac) into N-acetyl-D-mannosamine (ManNAc) and pyruvate .

Structure and Function

N-acetylneuraminate pyruvate lyase belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds . The enzyme is a homotetramer, meaning it consists of four identical subunits. Each subunit contributes to the overall stability and activity of the enzyme. The enzyme exhibits high stability and activity at alkaline pH levels and moderate temperature ranges .

Physiological Role

The primary function of N-acetylneuraminate pyruvate lyase is to regulate the levels of sialic acids within the cell. Sialic acids are cleaved from sialoglycans by sialidases (neuraminidases) and can either be recycled in biosynthesis or degraded by N-acetylneuraminate pyruvate lyase . This degradation process is essential for maintaining the balance of sialic acids in the body, which is crucial for normal cellular functions.

Clinical Significance

Mutations in the gene encoding N-acetylneuraminate pyruvate lyase can lead to various medical conditions. For instance, deleterious variants in the enzyme have been associated with skeletal myopathy and cardiac edema in humans and zebrafish . These conditions are characterized by increased levels of free sialic acid, reduced muscle force and endurance, impaired mitochondrial function, and aberrant sialylation of proteins . Research has shown that N-acetylneuraminate pyruvate lyase is essential for muscle function and regeneration, serving as a general marker of muscle damage .

Applications

Human recombinant N-acetylneuraminate pyruvate lyase is used in various research and clinical applications. It is often employed in studies investigating the metabolism of sialic acids and their role in different biological processes. Additionally, the enzyme’s ability to catalyze the reverse aldol condensation reaction makes it a valuable tool for synthesizing sialic acid and its derivatives .

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