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Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5)

抗体来源(Source)

Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) is a Mouse monoclonal antibody produced from a hybridoma created by fusing SP2/0 myeloma and Mouse B-lymphocytes.

克隆号(Clone)

13A5

种属(Species)

Mouse

亚型(Isotype)

Mouse IgG1 | Mouse Kappa

偶联(Conjugate)

Unconjugated

抗体类型(Antibody Type)

Hybridoma Monoclonal

种属反应性(Reactivity)

Virus

特异性(Specificity)

This product is a specific antibody specifically reacts with HA.

应用(Application)

ApplicationRecommended Usage
ELISA0.1-50 ng/mL

纯度(Purity)

>95% as determined by SDS-PAGE.

纯化(Purification)

Protein A purified / Protein G purified

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

交叉验证(Cross Verification)

This product can cross in Elisa with
Influenza A [A/Darwin/6/2021 (H3N2)] HA Protein, His Tag (Cat. No. HA2-V52H5).
Influenza A [A/Darwin/9/2021 (H3N2)] HA Protein, His Tag (Cat. No. HA2-V52H6).
Influenza A Virus HA (H3N2) Protein, His Tag (Cat. No. H32-V52H3).
This product No cross-reactivity in ELISA with
Influenza A [Victoria/4897/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H8).
Influenza A [Wisconsin/67/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H7).
Influenza A [A/Victoria/2570/2019] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H6).
Influenza A [Sydney/5/2021 (H1N1)] HA Protein, His Tag (Cat. No. HA1-V52H4).
Influenza A (Vietnam/1194/2004(H5N1)) Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H9).
Influenza A (Guangdong/18SF020(H5N6)) Hemagglutinin (HA) Protein, His Tag (Cat. No.HA6-V52H3).
Influenza A (turkey/Germany-MV/R2472/2014(H5N8)) HA Protein, His Tag (Cat. No. HA8-V52H3).
Influenza A (A/Shanghai/02/2013(H7N9)) Hemagglutinin (HA) Protein, His Tag (Cat. No. HA9-V52H3).
Influenza A [A/guinea fowl/Hong Kong/WF10/99(H9N2)] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA2-V52H7).
Influenza B [Austria/1359417/2021 (B/Victoria lineage)] Hemagglutinin (HA) Protein, His Tag (Cat. No. HAE-V52H3).
Influenza B [Phuket/3073/2013 (B/Yamagata lineage)] HA Protein, His Tag (Cat. No. HAE-V52H4).
Influenza A [A/Bangkok/1/1979 (H3N2)] HA, His Tag (Cat. No. HA2-V52H3).
Influenza A [A/Wisconsin/588/2019 (H1N1)] HA, His Tag (Cat. No. HA1-V52H3).
Influenza A [A/Hong Kong/483/97 (H5N1)] HA, His Tag (Cat. No. HA1-V5229).

 

电泳(SDS-PAGE)

Hemagglutinin/HA (Influenza Virus) SDS-PAGE

Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).

 

活性(Bioactivity)-ELISA

Hemagglutinin/HA (Influenza Virus) ELISA

Immobilized Influenza A [A/Darwin/6/2021 (H3N2)] HA Protein, His Tag (Cat. No. HA2-V52H5) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) (Cat. No. HA2-Y290) with a linear range of 0.1-6 ng/mL (QC tested).

Protocol

Hemagglutinin/HA (Influenza Virus) ELISA

Immobilized Influenza A [A/Darwin/9/2021 (H3N2)] HA Protein, His Tag (Cat. No. HA2-V52H6) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) (Cat. No. HA2-Y290) with a linear range of 0.2-13 ng/mL (Routinely tested).

Protocol

Hemagglutinin/HA (Influenza Virus) ELISA

Immobilized Influenza A Virus HA (H3N2) Protein, His Tag (Cat. No. H32-V52H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) (Cat. No. HA2-Y290) with a linear range of 0.1-6 ng/mL (Routinely tested).

Protocol

Hemagglutinin/HA (Influenza Virus) ELISA

Immobilized Influenza A Virus (A/Croatia/10136RV/2023) HA (H3N2) Protein, His Tag (Cat. No. H32-V52H4)/Influenza A Virus (A/District of Columbia/27/2023) HA (H3N2) Protein, His Tag (Cat. No. H32-V52H5) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) (Cat. No. HA2-Y290) with a linear range of 0.2-13 ng/mL (Routinely tested).

Protocol

 

活性(Bioactivity)-SPR

Hemagglutinin/HA (Influenza Virus) SPR

Influenza A [A/Darwin/6/2021 (H3N2)] HA Protein, His Tag (Cat. No. HA2-V52H5) captured on CM5 chip via anti-His antibody can bind Monoclonal Anti-HA-H3N2(Influenza A/Darwin/6/2021) Antibody, Mouse IgG1 (13A5) (Cat. No. HA2-Y290) with an affinity constant of 3.43 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

Protocol

 
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背景(Background)

Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of 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. Hemagglutinin also plays a major role in the determination of host range restriction and virulence. As a class I viral fusion protein, hemagglutinin is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane.

 

前沿进展

Broad Mucosal and Systemic Immunity in Mice Induced by Intranasal Booster With a Novel Recombinant Adenoviral Based Vaccine Protects Against Divergent Influenza A Virus
Li, Wang, Guo et al
J Med Virol (2025) 97 (4), e70326
Abstract: The development of broad-spectrum universal influenza vaccines and optimization of vaccination strategies to address the threats posed by pandemics and emerging influenza viruses are critical for public health. In this study, an adenovirus type 5 vector-based influenza vaccine carrying the hemagglutinin (HA) stem of H1, HA stem of H3, and neuraminidase (NA) of N1 from the influenza virus was constructed. Immune responses were evaluated in mice using various vaccination strategies: prime-only (intramuscular [IM] or intranasal [IN]) and prime-boost (IM + IN). Compared with the prime-only strategy, the prime-boost strategy significantly enhanced the systemic immune response, inducing higher levels of antigen-specific IgG, mucosal IgA, and T cell immunity in the spleen and lungs. Furthermore, the IN boosting strategy provided complete protection in mice challenged with the H1N1-PR8, rgH3N2-X31, and rgH5N1-Vietnam viruses, significantly reducing viral loads in the lungs and alleviating lung tissue pathologies. In conclusion, this study elucidates potential avenues for the development and application of universal influenza vaccines using customized mucosal boosting strategies.© 2025 Wiley Periodicals LLC.
Tracking Seasonal Influenza Trends in South Tyrol During 2022/2023 Using Genomic Surveillance Data
Bianconi, Manica, Moroder et al
Influenza Other Respir Viruses (2025) 19 (4), e70083
Abstract: Influenza seasons are characterized by a complex interplay of co-circulating strains with high spatial and temporal heterogeneities. Surveillance is crucial for monitoring the spread and evolution of the virus and design effective public health response strategies.We combined epidemiological, virological, and genomic surveillance data to provide a comprehensive analysis of influenza subtypes circulating in the South Tyrol region (Italy) during season 2022/2023, leveraging phylogenetic and phylodynamic approaches.Clinical samples were collected from patients exhibiting influenza-like symptoms and evaluated by molecular diagnostics. Whole genome sequencing was conducted, and the hemagglutinin (HA) gene sequences were used for phylogenetic analysis. A birth-death skyline model was applied to estimate strain-specific effective reproduction numbers (Re) and attack rates.Out of 4891 samples tested, 862 tested positive for influenza, of which 224 genomes were sequenced. Phylogenetic analysis of HA gene revealed A(H3N2) strains predominantly clustering in clade 3C.2a1b.2a.2b, followed by 3C.2a1b.2a.1b. A(H1N1pdm09) strains predominantly clustered in clade 6B.1A.5a.2a. Exclusive circulation of B (Victoria) subtype strains aligned with the global trend, all falling within clade V1A.3a.2. Phylogenetic analyses indicate that the strains isolated in the South Tyrol region closely resembled those circulating in the rest of Italy and Austria. Re peaked at 1.16-1.35 (95%CI) for A(H3N2), 1.06-1.34 for A(H1N1pdm09) and 1.02-1.29 for B (Victoria). 95%CI of attack rates were 6.3%-33.5% for A(H3N2), 0.6%-5.0% for A(H1N1pdm09), and 0.8%-6.5% for B (Victoria).Epidemiological estimates from traditional surveillance data can be corroborated by those derived from genomic sequencing, providing more robust assessments of viral transmissibility and attack rates with limited additional effort.© 2025 The Author(s). Influenza and Other Respiratory Viruses published by John Wiley & Sons Ltd.
Antiviral Activity of Berbamine Against Influenza A Virus Infection
Cho, Choi, Ma
Int J Mol Sci (2025) 26 (6)
Abstract: Berbamine (BBM) is a bibenzyl isoquinoline present in the traditional Chinese herbal medicine Berberis amurensisis Rupr. The present study demonstrates that BBM exerts strong antiviral efficacy against influenza A virus (IAV) infection. We examined the anti-IAV effect of BBM using green fluorescent protein (GFP)-expressing influenza A and H1N1 IAV. The fluorescence microscopy, fluorescence-activated cell sorting analysis, and plaque assay showed that BBM significantly hinders IAV infection. The immunofluorescence analysis confirmed the anti-influenza activity of BBM. From the time-of-addition and hemagglutination inhibition results, it is elucidated that the antiviral effect of BBM is closely related to its inhibitory effect against viral binding and entry at an early infection stage. Our findings imply that BBM has the potential to be developed as a potent antiviral drug against influenza viral infection.
Analysis of polyclonal and monoclonal antibody to the influenza virus nucleoprotein in different oligomeric states
Myers, Conlon, Gallagher et al
Virus Res (2025)
Abstract: Influenza virus nucleoprotein (NP) is one of the most conserved influenza proteins. Both NP antigen and anti-NP antibodies are used as reagents in influenza diagnostic kits, with applications in both clinical practice and influenza zoonotic surveillance programs. Despite this, studies on the biochemical basis of NP diagnostic serology and NP epitopes are not as developed as for hemagglutinin (HA), the fast-evolving antigen which has been the critical component of current influenza vaccines. Here, we characterized the NP serology of mice, ferrets, and human sera and the immunogenic effects of NP antigen presented as different structural complexes. Furthermore, we show that the classical mouse anti-NP mAb HB65 could detect NP in some commercial influenza vaccines. MAb HB65 bound a linear epitope with nanomolar affinity. Our analysis suggests that linear NP epitopes paired with their corresponding characterized detection antibodies could aid in designing and improving diagnostic technologies for influenza viruses.Copyright © 2025. Published by Elsevier B.V.
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