| Catalog No. | Size | Price (USD) |
| 40502-V07B-50 | 50 µg | $380.64 |
| 40502-V07B-100 | 100 µg | $765.73 |
General Information
| Formulation | Lyophilized from sterile 20mM PB, 150 mM NaCl, 10% Glycerol, pH 7.0. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Endotoxin | < 1.0 EU per μg protein as determined by the LAL method. |
| Shipping | In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
| Stability & Storage | Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution | To find reconstitution info, click on 'COA' at the top of the page, enter the lot number and product size for the lot-specific COA. |
| Purity | > 90 % as determined by SDS-PAGE. |
| Activity | Measured by its ability to cleave a fluorogenic substrate, 2'-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid. |
| Protein Construction | A DNA sequence encoding the Influenza B (B/PHUKET/3073/2013) neuraminidase (translated amino acids of EPI529344) (Leu38-Leu466) was expressed with a polyhistidine tag at the N-terminus. |
| Accession# | EPI529344 |
| Expressed Host | Baculovirus-Insect Cells |
| Species | Influenza B |
| Predicted N Terminal | His |
| Molecule Mass | The recombinant Influenza B (B/PHUKET/3073/2013) neuraminidase consists of 445 amino acids and predicts a molecular mass of 49.5 kDa. The apparent molecular mass of the protein is approximately 52.5 kDa in SDS-PAGE under reducing conditions. |
Image / Experimental Information
| Image 1 Alt Text | Influenza B Neuraminidase Protein 14967 |
| Image 1 URL | Source image |
Background Information
| Description | Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Influenza neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Influenza neuraminidase is composed of four identical subunits arranged in a square. It is normally attached to the virus surface through a long protein stalk. The active sites are in a deep depression on the upper surface. They bind to polysaccharide chains and clip off the sugars at the end. The surface of neuraminidase is decorated with several polysaccharide chains that are similar to the polysaccharide chains that decorate our cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of the influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme that facilitates virus release and efficient spread of the progeny virus from cell to cell. Influenza antibody and influenza antibodies are very important research tools for influenza diagnosis, influenza vaccine development, and anti-influenza virus therapy development. The monoclonal or polyclonal antibody can be raised with protein based antigen or peptide-based antigen. Antibodies raised with protein-based antigen could have better specificity and/or binding affinity than antibodies raised with peptide based antigen, but the cost associated with the recombinant protein antigen is usually higher. Anti-influenza virus hemagglutinin (HA) monoclonal antibody or polyclonal antibody can be used for ELISA assay, western blotting detection, Immunohistochemistry (IHC), flow cytometry, neutralization assay, hemagglutinin inhibition assay, and early diagnosis of influenza viral infection. Sino Biological has developed state-of-the-art monoclonal antibody development technology platforms: mouse monoclonal antibody and rabbit monoclonal antibody. Our rabbit monoclonal antibody platform is one of a kind and offers some unique advantages over mouse monoclonal antibodies, such as high affinity, low cross-reactivity with rabbit polyclonal antibodies. |
| References |
|
title: Baseline innate and T cell populations are correlates of protection against symptomatic influenza virus infection independent of serology
authors: Robert C. Mettelman; Aisha Souquette; ...; Paul G. Thomas
journal: Nature immunology
date: 2024-09-01
pmid: 37592015
doi: 10.1038/s41590-023-01590-2
pmcid: 10566627
cited_by_count: 63
techniques: Blocking Assay; Derivative Assay; Enzyme-linked Immunosorbent Assay; Incubation; Purification; Recombinant; Virus
bioz_score: 94
title: Tissue-specific sex differences in pediatric and adult immune cell composition and function
authors: Mahina Tabassum Mitul; Jenna M. Kastenschmidt; ...; Lisa E. Wagar
journal: Frontiers in Immunology
date: 2024-05-15
doi: 10.3389/fimmu.2024.1373537
pmcid: 11133680
cited_by_count: 0
bioz_score: 94
title: Fc functional antibody responses to adjuvanted versus unadjuvanted seasonal influenza vaccination in community-dwelling older adults.
authors: Hillary A Vanderven; Ian Barr; ...; Stephen J Kent
journal: Vaccine
date: 2021-02-26
pmid: 32035709
doi: 10.1016/j.vaccine.2020.01.066
cited_by_count: 10
techniques: HI Assay; Recombinant
bioz_score: 94
title: Memory B Cell Activation, Broad Anti-influenza Antibodies, and Bystander Activation Revealed by Single-Cell Transcriptomics
authors: Felix Horns; Cornelia L. Dekker; Stephen R. Quake
journal: Cell Reports
date: 2021-02-03
pmid: 31968262
doi: 10.1016/j.celrep.2019.12.063
pmcid: 7891556
cited_by_count: 159
techniques: Cell Isolation; Multiplex Assay; Recombinant; Sequencing; Software
bioz_score: 94
title: Transcriptional program of memory B cell activation, broadly binding anti-influenza antibodies, and bystander activation after vaccination revealed by single-cell transcriptomics
authors: Horns Felix; Dekker Cornelia L.; Quake Stephen R.
journal: bioRxiv
date: 2019-07-22
doi: 10.1101/709337
cited_by_count: 0
techniques: Purification
bioz_score: 94
