Rabbit anti-Human Neuraminidase Polyclonal Antibody | anti-NA antibody

Anti-Human Neuraminidase Antibody

Cat. Num. AAA4158678

• Reactivity: Human
• Applications: ELISA
• Purity: Affinity Purified
• Synonyms: Neuraminidase; Polyclonal Antibody; Anti-Human Neuraminidase Antibody; Human Neuraminidase; anti-NA antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This is an affinity purified antibody produced by immunoaffinity chromatography using the immunizing peptide after immobilization to a solid phase. This antibody reacts with human Neu2. Based on sequence we expect this antibody to react with neuraminidase from other sources, although specific reactivity has not been confirmed.
• Purity/Purification: Affinity Purified
• Form/Format: Liquid; PBS, pH 7.4 with 0.05% sodium azide.
• Concentration: 1ug/ul (varies by lot)
• Sequence Length: 466

• Applicable Applications for anti-NA antibody: ELISA (EIA)
• Application Notes: This antibody is suitable for western blotting, immunocytochemistry, immunoprecipitation, transfected cell culture, primary cell culture, and ELISA.
• Immunogen: This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to amino acids 110-124 of Human Neu2.
• Preparation and Storage: This product is stable for several weeks at 4 degree C as an undiluted liquid. Dilute only prior to immediate use.; For extended storage, aliquot contents and freeze at-20 degree C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.

Testing Data

Related Product Information for anti-NA antibody

Neuraminidases or sialidases are exoglycosidases that catalyze the cleavage of alpha-glycosidically linked terminal N-acetyl neuraminic acid from sialylated glycoconjugates. They are widely spread in nature, occurring in viruses, bacteria, fungi, protozoa, birds and mammals. Together, the neuraminidases form a family of hydrolases that share a conserved active site and similar sequence motifs. Three types of neuraminidase are found in mammals and are defined as lysosomal, plasma membrane and cytosolic on the basis of their biochemical properties and subcellular distribution. Lysosomal N-acetylneuraminidase (NEU1) has significant primary structure characteristics of other mammalian and microbial sialidases with similar substrate specificity. However, unlike other members of this family, lysosomal neuraminidase requires the carboxypeptidase protective protein/cathepsin A (PPCA) for intracellular transport and lysosomal activation. The enzyme is only catalytically active when it is bound to PPCA and is a component of a high molecular weight, multi-protein complex containing PPCA, beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase. Using a hamster Sial3 probe, Monti et al. (1999) identified the gene encoding sialidase-2, which they designated NEU2, from a human genomic library. The 2 putative exons of NEU2 encode a deduced 380-amino acid protein with a calculated molecular mass of 42.23 kD. The NEU2 protein has significant homology with the mammalian, viral, and bacterial sialidases. It shares over 72% similarity with the hamster and rat cytosolic sialidases and over 42% similarity with human NEU1. NEU2 contains a potential N-linked glycosylation site, 2 aspartic acid block consensus sequences, and an N-terminal F/YRIP sequence motif which is part of the active site of other sialidase enzymes. Monti et al. hypothesized that NEU2 has a cytosolic localization because it does not contain a cleavage site, transmembrane domain, or targeting motifs.

NCBI and Uniprot Product Information

• NCBI GI #: 8486158
• NCBI GenBank Nucleotide #: NP_056663.1
• UniProt Accession #: P03474
• NCBI Official Full Name: neuraminidase
• UniProt Protein Name: Neuraminidase
• Protein Family: Neuraminidase
• UniProt Gene Name: NA

Uniprot Description

Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.