NEU1 Human

Sialidase 1 Human Recombinant

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Cat. No.

BT25881

Source

E.coli.

Synonyms

Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

Appearance

Sterile Filtered colorless solution.

Purity

Greater than 85% 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.

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Description

Biological Functions

NEU1 regulates diverse cellular processes through desialylation:

Lysosomal Regulation

Cleaves sialic acid from lysosomal-associated membrane protein 1 (LAMP1), modulating lysosomal exocytosis and extracellular matrix remodeling .
Deficiency disrupts elastin fiber synthesis, impacting vascular and connective tissues .

Elastogenesis

Part of the elastin receptor complex (ERC) with PPCA and elastin-binding protein (EBP) .
Pharmacological inhibition of NEU1 blocks elastin fiber assembly in fibroblasts and smooth muscle cells .

Insulin Signaling

Enhances insulin receptor activation by desialylating its glycan chains.
NEU1-deficient models show impaired AKT phosphorylation, reversible via exogenous NEU1 supplementation .

Cancer and Immune Regulation

Acts as a tumor suppressor by desialylating growth factor receptors (e.g., PDGFR, IGFR), reducing mitogenic signaling .
Modulates integrin-mediated adhesion and leukocyte transmigration, with NEU1 inhibitors reducing lymphocyte migration by 40–60% .

Therapeutic Implications

Table 2: NEU1 in Disease and Therapy

Condition	Mechanism	Therapeutic Approach
Sialidosis	NEU1 mutations → lysosomal storage	Enzyme replacement therapy (ERT)
Alzheimer’s Disease	Aβ plaque modulation via desialylation	NEU1 activators (preclinical)
Cancer	Overexpression reduces invasiveness	NEU1 gene therapy
Inflammation	Regulates TLR4 and β1-integrin signaling	Small-molecule inhibitors (e.g., oseltamivir derivatives)

Mechanistic Insights from Recent Studies

Membrane Localization: NEU1’s plasma membrane pool is PPCA-independent, challenging earlier assumptions about its lysosomal exclusivity .
Dimerization: TM2-mediated self-association enhances sialidase activity, with point mutations (e.g., G328I) reducing activity by >50% .
Substrate Specificity: Preferential cleavage of α2,3- and α2,6-linked sialic acids over α2,8 linkages .

Research Challenges and Future Directions

Structural Ambiguities: Discrepancies between β-propeller models and transmembrane domain predictions require cryo-EM validation .
Isoform Selectivity: Developing NEU1-specific inhibitors remains challenging due to homology with NEU3/NEU4 .
Clinical Translation: ERT for sialidosis shows promise but faces delivery hurdles across the blood-brain barrier .

Product Specs

Introduction

Sialidase 1 (NEU1) is a lysosomal enzyme responsible for cleaving terminal sialic acid residues from molecules like glycoproteins and glycolipids. It functions within the lysosome as part of a three-protein complex, working in conjunction with beta-galactosidase and cathepsin A. Mutations in the NEU1 gene can lead to sialidosis, a lysosomal storage disorder. Sialidosis presents in two forms: type 1 (characterized by cherry-red spots in the eye and myoclonus or a normosomatic presentation) with a later onset, and type 2 (the dysmorphic type) which manifests earlier in life with more severe symptoms.

Description

Recombinant human NEU1, produced in E. coli, is a single polypeptide chain consisting of 393 amino acids (residues 48-415). It has a molecular weight of 42.9 kDa. The NEU1 protein includes a 25 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic methods.

Physical Appearance

A clear, colorless solution that has been sterilized by filtration.

Formulation

The NEU1 solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 0.15M NaCl, 1mM DTT, and 10% glycerol.

Stability

For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For longer periods, store frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.

Purity

Purity is determined to be greater than 85% based on SDS-PAGE analysis.

Synonyms

Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

Source

E.coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSHMENDFG LVQPLVTMEQ LLWVSGRQIG SVDTFRIPLI TATPRGTLLA FAEARKMSSS DEGAKFIALR RSMDQGSTWS PTAFIVNDGD VPDGLNLGAV VSDVETGVVF LFYSLCAHKA GCQVASTMLV WSKDDGVSWS TPRNLSLDIG TEVFAPGPGS GIQKQREPRK GRLIVCGHGT LERDGVFCLL SDDHGASWRY GSGVSGIPYG QPKQENDFNP DECQPYELPD GSVVINARNQ NNYHCHCRIV LRSYDACDTL RPRDVTFDPE LVDPVVAAGA VVTSSGIVFF SNPAHPEFRV NLTLRWSFSN GTSWRKETVQ LWPGPSGYSS LATLEGSMDG EEQAPQLYVL YEKGRNHYTE SISVAKISVY GTL

Product Science Overview

Introduction

Sialidase 1, also known as NEU1, is a lysosomal enzyme that plays a crucial role in the catabolism of sialic acids. Sialic acids are terminal acidic monosaccharides that influence the chemical and biological properties of glycoconjugates. The removal of sialic acids by sialidase modulates various biological processes by altering the conformation and binding sites of functional molecules.

Structure and Expression

Sialidase 1 belongs to the N-acetyl-α-neuraminidase family and is encoded by the NEU1 gene. It is expressed in many tissues, with high expression in the pancreas and weak expression in the brain. The enzyme is a part of a multienzyme complex that includes Cathepsin A (protective protein), β-galactosidase, and N-acetylgalactosamine-6-sulfate sulfatase.

Function

Sialidase 1 catalyzes the removal of sialic acid residues from glycoproteins and glycolipids. This enzymatic activity is essential for the proper functioning of lysosomal catabolism. The enzyme has a preference for α2-3 and α2-6 sialyl linkages. The activity of Sialidase 1 is strictly dependent on its presence in the multienzyme complex.

Clinical Significance

Deficiencies in Sialidase 1 lead to sialidosis, a rare lysosomal storage disease characterized by the accumulation of sialylated glycoproteins and glycolipids in tissues. This condition manifests in various symptoms, including developmental delay, myoclonus, and vision problems.

Recombinant Production

Recombinant Human Sialidase 1 is produced using various expression systems, including yeast, E. coli, baculovirus, and mammalian cells. The recombinant protein is often tagged with His-tag for purification purposes and is supplied as a filtered solution for research use.

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NEU1 Human

Description

Biological Functions

Lysosomal Regulation

Elastogenesis

Insulin Signaling

Cancer and Immune Regulation

Therapeutic Implications

Table 2: NEU1 in Disease and Therapy

Mechanistic Insights from Recent Studies

Research Challenges and Future Directions

Product Specs

Product Science Overview

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