Description

Neuraminidase is a critical glycoside hydrolase enzyme that catalyzes the hydrolysis of terminal sialic acid residues from glycoproteins, glycolipids, and oligosaccharides. This enzymatic activity is essential for fundamental research in glycobiology, virology, and the development of diagnostic and therapeutic agents. It is a vital reagent for scientists and manufacturers in the pharmaceutical, biotechnology, and diagnostic industries, particularly for studying influenza virus mechanisms, processing glycoproteins, and developing carbohydrate-based drugs.

Application

• Glycoprotein Research & Analysis: Used to cleave sialic acid residues from glycoproteins for structural analysis, functional studies, and to improve chromatographic separation.
• Virology & Antiviral Development: Essential for studying influenza virus neuraminidase function, screening potential antiviral compounds, and evaluating vaccine efficacy.
• Diagnostic Reagent Production: Incorporated into enzymatic assay kits for the detection of sialic acid levels in clinical samples, aiding in the diagnosis of certain metabolic and disease states.
• Biopharmaceutical Processing: Employed in the controlled desialylation of therapeutic proteins (e.g., antibodies, hormones) to modulate their pharmacokinetic properties, such as serum half-life.
• Cell Surface Modification: Used to remove sialic acids from cell membranes to study cell adhesion, signaling, and immune recognition processes.
• Food & Beverage Analysis: Applied in the analysis of sialylated compounds in food products, including dairy and infant formula.

Basic Information

Product Name	Neuraminidase
CAS No.	9001-67-6
Molecular Formula	Contact for details
Molecular Weight	Contact for details
Synonyms	Sialidase; Acylneuraminyl Hydrolase; Exo-α-sialidase; Receptor-Destroying Enzyme (RDE); N-Acetylneuraminic Hydrolase; Glycoprotein Neuraminidase; Influenza Virus Neuraminidase (analog); EC 3.2.1.18
EINECS	Contact for details

Quality Control

Our Neuraminidase is produced and tested under stringent quality management systems. Each lot undergoes comprehensive analysis to ensure high specific activity, purity, and functional consistency. We provide detailed Certificates of Analysis (COA) with key parameters including activity (U/mg), protein content, and purity assessed by SDS-PAGE. Our quality commitment supports applications requiring reliable and reproducible enzymatic performance in research and manufacturing.

Storage

Preserve in a tightly closed container, protected from light. For long-term stability, store lyophilized powder at -20°C. Reconstituted enzyme solutions should be aliquoted and stored at -20°C or below to prevent repeated freeze-thaw cycles. The product is hygroscopic (moisture-sensitive); ensure the container is sealed tightly after each use to maintain activity.

Specification

Item	Specification
Appearance	White to off-white lyophilized powder
Identification (Activity)	Conforms
Specific Activity	≥ [Value] U/mg protein
Protein Content (Bradford)	≥ [Value] %
Purity (SDS-PAGE)	≥ [Value] %
pH (in solution)	5.0 - 7.0
Endotoxin	< [Value] EU/mg

Note: Specifications can be tailored. Please contact us for the detailed technical data sheet of a specific grade.