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AB230526

Anti-Neuraminidase antibody

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(1 Publication)

Rabbit Polyclonal Neuraminidase antibody. Suitable for WB, IHC-P and reacts with Mouse, Rat, Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human NEU1 aa 150 to C-terminus.

View Alternative Names

NANH, NEU1, Sialidase-1, Acetylneuraminyl hydrolase, G9 sialidase, Lysosomal sialidase, N-acetyl-alpha-neuraminidase 1

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Neuraminidase antibody (AB230526)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Neuraminidase antibody (AB230526)

Formalin-fixed, paraffin-embedded human adrenal tissue stained for Neuraminidase with ab230526 at 1/100 dilution in immunohistochemical analysis.

Western blot - Anti-Neuraminidase antibody (AB230526)
  • WB

Supplier Data

Western blot - Anti-Neuraminidase antibody (AB230526)

All lanes:

Western blot - Anti-Neuraminidase antibody (ab230526) at 1/500 dilution

Lane 1:

Mouse liver tissue extract

Lane 2:

Rat liver tissue extract

Predicted band size: 45 kDa

true

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Rat, Human

Applications

WB, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human NEU1 aa 150 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q99519

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification
Storage buffer
pH: 7.3 Preservative: 0.02% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Neuraminidase sometimes called sialidase functions as an enzyme that cleaves sialic acid residues from glycoproteins and glycolipids. This process is essential for the maturation and release of progeny viruses from infected cells. Enzymatically active neuraminidase proteins weigh about 60 kilodaltons and localize on the surface of influenza viruses. Researchers identify its expression on the viral envelope playing a pivotal role in the viral life cycle. Neuraminidase activity is an important target for drug development against influenza.
Biological function summary

Neuraminidase significantly impacts viral virulence and host cell infection. It is part of the functional machinery required for viral particle detachment from the host cell membrane facilitating the spread of infection. Neuraminidase works alongside other viral proteins including hemagglutinin which attaches the virus to the host cell. The neuraminidase function of trimming sialic acids is critical in the ongoing interaction between virus and host.

Pathways

The influenza lifecycle heavily involves neuraminidase-mediated sialic acid cleavage. This enzyme contributes to pathways by enabling the efficient release of new viral particles enhancing the infectivity of the virus. Neuraminidase operates in concert with hemagglutinin which initially binds the virus to host cells by attaching to the sialic acid residues. This interplay is vital in viral replication pathways which propagate the infection cycle.

Influenza directly relates to neuraminidase as it is a primary means by which the virus spreads within the host. Neuraminidase inhibitors are a class of antiviral drugs that target this protein important for treating and managing influenza infections. Besides influenza research links neuraminidase activity to bacterial infections with some bacterial neuraminidases implicated in the pathogenesis of diseases like pneumonia. The relationship to hemagglutinin in viral influenza highlights the significance of neuraminidase as a target in therapeutic interventions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
See full target information NEU1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

JCI insight 9: PubMed38271096

2024

Purine nucleoside phosphorylase inhibition is an effective approach for the treatment of chemical hemorrhagic cystitis.

Applications

Unspecified application

Species

Unspecified reactive species

Amanda Wolf-Johnston,Youko Ikeda,Irina Zabbarova,Anthony J Kanai,Sheldon Bastacky,Robert Moldwin,Joel Nh Stern,Edwin K Jackson,Lori A Birder
View all publications

Product promise

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