Rabbit Polyclonal NRAM antibody. Suitable for WB, ELISA and reacts with Recombinant full length protein - Influenza A samples. Cited in 9 publications.
Images
Publications
Filter by
- JCI insight 7:2022The UIP/IPF fibroblastic focus is a collagen biosynthesis factory embedded in a distinct extracellular matrix.Applications:Unspecified applicationReactive species:Unspecified reactive speciesJeremy A Herrera,Lewis Dingle,M Angeles Montero,Rajamiyer V Venkateswaran,John F Blaikley,Craig Lawless,Martin A SchwartzPubMed 35852874
- Viruses 14:2022Characterization of Immune Response towards Generation of Universal Anti-HA-Stalk Antibodies after Immunization of Broiler Hens with Triple H5N1/NA-HA-M1 VLPs.Applications:Unspecified applicationReactive species:Unspecified reactive speciesBeata Gromadzka,Milena Chraniuk,Lilit Hovhannisyan,Karolina Uranowska,Bogusław Szewczyk,Magdalena Narajczyk,Mirosława PanasiukPubMed 35458460
- Methods in molecular biology (Clifton, N.J.) 2183:331-3562020Attenuation Methods for Live Vaccines.Applications:Unspecified applicationReactive species:Unspecified reactive speciesDipasree Hajra,Akshay Datey,Dipshikha ChakravorttyPubMed 32959252
- mBio 11:2020Heterosubtypic Protection Induced by a Live Attenuated Influenza Virus Vaccine Expressing Galactose-α-1,3-Galactose Epitopes in Infected Cells.Applications:Unspecified applicationReactive species:Unspecified reactive speciesLi-Meng Yan et. al.PubMed 32127444
- Journal of virology 89:10762-732015Generation of Live Attenuated Influenza Virus by Using Codon Usage Bias.
- Cell death & disease 4:e5622013Influenza A virus nucleoprotein induces apoptosis in human airway epithelial cells: implications of a novel interaction between nucleoprotein and host protein Clusterin.
- PloS one 5:e155562010The low-pH stability discovered in neuraminidase of 1918 pandemic influenza A virus enhances virus replication.
- PloS one 5:e122172010A pandemic influenza H1N1 live vaccine based on modified vaccinia Ankara is highly immunogenic and protects mice in active and passive immunizations.
- Journal of immunology (Baltimore, Md. : 1950) 182:3063-712009Vaccinia virus-based multivalent H5N1 avian influenza vaccines adjuvanted with IL-15 confer sterile cross-clade protection in mice.Applications:WBReactive species:Unspecified reactive speciesLeo L M Poon,Y H Connie Leung,John M Nicholls,Pin-Yu Perera,Jack H Lichy,Masafumi Yamamoto,Thomas A Waldmann,J S Malik Peiris,Liyanage P PereraPubMed 19234203
Key facts
- Isotype
- IgG
- Host species
- Rabbit
- Storage buffer
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS- Form
- Liquid
- Clonality
- Polyclonal
Reactivity data
Select an application| WB | ELISA | |
|---|---|---|
| Influenza A | Predicted | Predicted |
| Recombinant full length protein - Influenza A | Tested | Tested |
WB
TestedTested
| Species | Dilution info | Notes |
|---|---|---|
Species Recombinant full length protein - Influenza A | Dilution info 1 µg/mL | Notes - |
PredictedPredicted
| Species | Dilution info | Notes |
|---|---|---|
Species Influenza A | Dilution info - | Notes - |
ELISA
TestedTested
| Species | Dilution info | Notes |
|---|---|---|
Species Recombinant full length protein - Influenza A | Dilution info 1000 ng/mL | Notes It will detect 10 ng of free peptide at 1 μg/ml. |
PredictedPredicted
| Species | Dilution info | Notes |
|---|---|---|
Species Influenza A | Dilution info - | Notes - |
Associated Products
Select an associated product type
2 products for Alternative Product
Target data
Function
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 moieties 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.
Alternative names
Neuraminidase, NA
Recommended products
Rabbit Polyclonal NRAM antibody. Suitable for WB, ELISA and reacts with Recombinant full length protein - Influenza A samples. Cited in 9 publications.
Key facts
- Isotype
- IgG
- Host species
- Rabbit
- Storage buffer
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS- Form
- Liquid
- Clonality
- Polyclonal
- Purification technique
- Affinity purification Immunogen
- Specificity
ab21304 can be used for the detection of the Neuraminidase protein from the H5N1 strain of avian influenza A in ELISA and WB. It will detect 10 ng of free peptide at 1 μg/mL.
- Concentration
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage conditions
- +4°C
- Appropriate long-term storage conditions
- +4°C
Notes
Abcam is leading the way to address reproducibility in scientific research with our highly validated recombinant monoclonal and recombinant multiclonal antibodies. Search & select one of Abcam's thousands of recombinant alternatives to eliminate batch-variability and unnecessary animal use.
If you do not find a host species to meet your needs, our catalogue and custom Chimeric range provides scientists the specificity of Abcam's RabMAbs in the species backbone of your choice. Remember to also review our range of edited cell lines, proteins and biochemicals relevant to your target that may help you further your research goals.
Abcam antibodies are extensively validated in a wide range of species and applications, so please check the reagent specifications meet your scientific needs before purchasing. If you have any questions or bespoke requirements, simply visit the Contact Us page to send us an inquiry or contact our Support Team ahead of purchase.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Avian Influenza A Neuraminidase sometimes called N1 or neuraminidase protein is a viral enzyme with significant mechanical functions in the life cycle of influenza viruses. This enzyme a glycoprotein with an approximate mass of 470 kDa is expressed on the surface of the influenza virus particles. Neuraminidase cleaves sialic acid residues from glycoproteins and glycolipids facilitating the release of newly formed viral particles from infected host cells. This action helps the virus to spread efficiently and infect more cells.
- Biological function summary
In the influenza virus life cycle the neuraminidase protein helps in preventing viral self-aggregation and assists in viral movement within the host. It is not part of a complex but functions in coordination with the hemagglutinin protein. Both neuraminidase and hemagglutinin are found on the viral envelope and play important roles in the viral infection process with hemagglutinin binding to host cell receptors and neuraminidase aiding in viral egress.
- Pathways
Neuraminidase activity is integral to the sialic acid metabolic pathway ensuring the process of viral particle release is efficient. Neuraminidase works alongside hemagglutinin in the infection cycle with the two proteins together maintaining equilibrium necessary for efficient viral replication and dissemination. Additionally neuraminidase is involved in the neuraminidase inhibitor pathway which is targeted for antiviral drug development that block its function to prevent virus spread.
- Associated diseases and disorders
Avian influenza neuraminidase is most associated with influenza infections specifically avian influenza affecting both birds and occasionally humans. Antigenic variation in neuraminidase leads to the emergence of new strains complicating vaccine development and treatment strategies. Neuraminidase also plays a role in swine flu pathogenesis interacting with host proteins and hemagglutinin to mediate infection. Efforts to create avian antibodies target neuraminidase aiming to develop therapies that can either prevent or limit the spread of these infections.
Product promise
Tested
We have tested this species and application combination and it works. It is covered by our product promise.
Expected
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
Predicted
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
Not recommended
We do not recommend this combination. It is not covered by our product promise.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
3 product images
Image from Hessel A et al, PLoS One. 2010 Aug 16;5(8). pii: e12217, Fig 1.Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21304)
Expression of the H1 or N1 proteins by recombinant vaccinia viruses was detected by Western blotting. Vero cells in case of the VV-L constructs, or the avian cell line DF-1 [15] in case of MVA, were infected at a multiplicity of infection of 0.1 for 48 hours. MVA-H1-Ca or rVVL-H1-Ca infected cells were harvested by scraping or by adding trypsin. MVA-N1-Ca or rVVL-N1-Ca infected cells were harvested by scraping. Sonicated cell lysates were loaded onto 12% polyacrylamide gels and afterwards blotted on nitrocellulose membrane. To detect the H1 protein, a sheep antiserum against the A/California/7/2009 hemagglutinin (NIBSC 09/152) was used. Donkey-anti-sheep alkaline phosphatase-conjugated IgG was used as a secondary antibody. To detect the N1 protein ab21304 was utilized. Goat-anti-rabbit alkaline phosphatase-conjugated IgG was used as a secondary antibody. A whole virus vaccine H1N1 A/California/7/2009 [16] served as positive control.
Neuraminidase expression in chicken cells.All lanes: Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21304)
Predicted band size: 51 kDa
Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21304)
1h incubation at RT in 5% NFDM/TBST.
All lanes: Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21304) at 1 µg/mL
Lane 1: Avian Influenza Neuraminidase recombinant protein at 50 ng
Lane 2: Avian Influenza Neuraminidase recombinant protein at 100 ng
SecondaryAll lanes: Goat anti-rabbit IgG HRP conjugate at 1/10000 dilution
Predicted band size: 51 kDa
ELISA - Anti-Avian Influenza A Neuraminidase antibody (ab21304)
Validation with Avian Influenza NA Protein Coating Antigen: Avian Influenza Neuraminidase recombinant protein, 2 μg/mL, incubated at 4˚C overnight. Detection Antibodies: ab21304, dilution: 1-1000 ng/mL, incubated at RT for 1 hr. Secondary Antibodies: Goat anti-rabbit HRP at 1/10000 dilution, incubated at RT for 1 hr.
Downloads
Product protocols
- Visit the general protocols
- Visit troubleshooting
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com