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

Anti-Human Neuraminidase Antibody

Cat. Num. AAA4158725

• Reactivity: Human
• Applications: Western Blot, ELISA, Immunohistochemistry, Immunoprecipitation
• Purity: Purified
• Synonyms: Neuraminidase; Polyclonal Antibody; Anti-Human Neuraminidase Antibody; Human Neuraminidase; anti-NA antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This antiserum is directed against Neu1 and reacts with the Neu1 from human tissues. Based on sequence we expect this antibody to react with neuraminidase from other sources, although specific reactivity has not been confirmed.
• Purity/Purification: 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: Western Blot (WB), ELISA (EIA), Immunohistochemistry (IHC), Immunoprecipitation (IP)
• Application Notes: This antibody is suitable for western blotting, immunocytochemistry, immunoprecipitation, transfected cell culture, primary cell culture, and ELISA.
• Immunogen: This whole rabbit serum was prepared by repeated immunizations with a bacterially expressed and purified fusion protein excluding the signal peptide (first 45 amino acids) and the first 6 N-terminal amino acids of the processed form of human lysosomal neuraminidase (see link below for the full length sequence of the human gene product).
• 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

Testing Data

Testing Data

Related Product Information for anti-NA antibody

Neuraminidases or sialidases are exoglycosidases that catalyze the cleavage of a-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 Nacetylgalactosamine-6-sulfate sulfatase. The autosomal recessive genetic deficiency of NEU1 is associated with sialidosis, a neurodegenerative lysosomal storage disorder.

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.