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Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) (MALS verified)

抗体来源(Source)

Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) is a chimeric monoclonal antibody recombinantly expressed from HEK293, which combines the variable region of a mouse monoclonal antibody with Human constant domain.

克隆号(Clone)

5B2

种属(Species)

Mouse

亚型(Isotype)

Human IgG1 | Human Kappa

偶联(Conjugate)

Unconjugated

抗体类型(Antibody Type)

Recombinant Monoclonal

种属反应性(Reactivity)

Virus

免疫原(Immunogen)

Recombinant Influenza A [Victoria/4897/2022] Hemagglutinin (HA) Protein is expressed from human 293 cells.

特异性(Specificity)

Specifically recognizes Influenza A [Victoria/4897/2022] Hemagglutinin (HA).

应用(Application)

ApplicationRecommended Usage
Western Blot10-0.02 μg/mL
ELISA0.01-100 ng/mL

纯度(Purity)

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

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 No cross-reactivity in ELISA with
Influenza A [A/Hong Kong/483/97 (H5N1)] HA, His Tag (Cat. No. HA1-V5229).
Influenza A [Wisconsin/67/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H7).
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 (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 Virus HA (H3N2) Protein, His Tag (Cat. No. H32-V52H3).
Influenza A Virus (A/District of Columbia/27/2023) HA (H3N2) Protein, His Tag (Cat. No. H32-V52H5).
Influenza A Virus (A/Croatia/10136RV/2023) HA (H3N2) Protein, His Tag (Cat. No. H32-V52H4).
Influenza A (A/Sydney/1304/2022) Hemagglutinin (HA) Protein, His Tag (Cat. No. HA2-V52H9).
Influenza B (B/Singapore/INFTT-16-0610/2016) Hemagglutinin (HA) Protein, His Tag (Cat. No. HAE-V52H5).
Influenza B (B/Singapore/WUH4618/2021) Hemagglutinin (HA) Protein, His Tag (Cat. No. HAE-V52H6).
This product No cross-reactivity in WB with
Influenza B (B/Singapore/WUH4618/2021) Hemagglutinin (HA) Protein, His Tag (Cat. No. HAE-V52H6).
Influenza A (A/Sydney/1304/2022) Hemagglutinin (HA) Protein, His Tag (Cat. No. HA2-V52H9).

 

电泳(SDS-PAGE)

Hemagglutinin/HA (Influenza Virus) SDS-PAGE

Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) 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).

SEC-MALS

Hemagglutinin/HA (Influenza Virus) SEC-MALS

The purity of Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) (Cat. No. HA1-MY2158) is more than 90% and the molecular weight of this protein is around 135-165 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

Hemagglutinin/HA (Influenza Virus) ELISA

Immobilized Influenza A [Victoria/4897/2022] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H8) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) (Cat. No. HA1-MY2158) with a linear range of 0.01-3 ng/mL (QC tested).

Protocol

Hemagglutinin/HA (Influenza Virus) ELISA

Immobilized Influenza A [A/Victoria/2570/2019] Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H6), Influenza A (A/Georgia/12/2022) Hemagglutinin (HA) Protein, His Tag (Cat. No. HAE-V52H7), Influenza A [Sydney/5/2021 (H1N1)] HA Protein, His Tag (Cat. No. HA1-V52H4), Influenza A [A/Wisconsin/588/2019 (H1N1)] HA, His Tag (Cat. No. HA1-V52H3) at 1 μg/mL (100 μL/well) can bind Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) (Cat. No. HA1-MY2158) with a linear range of 0.01-13 ng/mL (Routinely tested).

Protocol

 

Western Blot验证

Hemagglutinin/HA (Influenza Virus) WESTERN BLOT

Detection of Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) by Western Blot. Monoclonal Anti-Influenza A (H1N1) Virus HA broadly Antibody, Human IgG1 (5B2) at 0.02 μg/mL dilution + Influenza A (A/Georgia/12/2022) Hemagglutinin (HA) Protein, His Tag at 400 ng.

Secondary: (HFC)-HRP Goat Anti-Human IgG,Fcγ fragment specific (min X Bov,Hrs,Ms Sr Prot) at 1/2000 dilution

Predicted band size: 65-95 kDa | 180 kDa 12% Bis-Tris Protein Gel

 
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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

Design, Synthesis and Anti-Influenza Virus Activity of 4-Tert-Butyl-N-(3-Oxo-1-Thia-4-Azaspiro[4.5]Dec-4-yl)Benzamide Derivatives That Target Hemagglutinin-Mediated Fusion
Çınar, Alikadıoğlu, Soylu-Eter et al
Drug Dev Res (2025) 86 (2), e70080
Abstract: Hemagglutinin (HA) is a viral glycoprotein that mediates influenza virus entry into the host cell and is considered a relevant viral target. We here report the identification of a class of 4-tert-butylphenyl-substituted spirothiazolidinones as HA-mediated fusion inhibitors with specific activity against influenza A/H3N2 virus. The novel spirocyclic compounds were achieved by using one-pot cyclocondensation method and the chemical structures were characterized by IR, 1H NMR, 13C NMR, and elemental analysis. Compound 2c, bearing methyl substitutions at positions 2- and 8- of the spiro ring displayed an EC50 value against influenza A/H3N2 virus of 1.3 μM and an antiviral selectivity index of 30. The fusion-inhibiting effect of compound 2c was revealed in the polykaryon assay which is based on cell-cell fusion when influenza virus H3 HA-transfected cells are exposed to low pH. Computer-aided docking was performed to predict the possible binding pocket in the H3 HA trimer. Resistance data and in silico studies indicated that compound 2c has an overlapping binding pocket in the stem region of H3 HA with the known fusion inhibitors TBHQ and arbidol.© 2025 The Author(s). Drug Development Research published by Wiley Periodicals LLC.
Modulation of lipid nanoparticle-formulated plasmid DNA drives innate immune activation promoting adaptive immunity
Tursi, Tiwari, Bedanova et al
Cell Rep Med (2025)
Abstract: Nucleic acid vaccines have grown in importance over the past several years, with the development of new approaches remaining a focus. We describe a lipid nanoparticle-formulated DNA (DNA-LNP) formulation which induces robust innate and adaptive immunity with similar serological potency to mRNA-LNPs and adjuvanted protein. Using an influenza hemagglutinin (HA)-encoding construct, we show that priming with our HA DNA-LNP demonstrated stimulator of interferon genes (STING)-dependent upregulation and activation of migratory dendritic cell (DC) subpopulations. HA DNA-LNP induced superior antigen-specific CD8+ T cell responses relative to mRNA-LNPs or adjuvanted protein, with memory responses persisting beyond one year. In rabbits immunized with HA DNA-LNP, we observed immune responses comparable or superior to mRNA-LNPs at the same dose. In an additional model, a SARS-CoV-2 spike-encoding DNA-LNP elicited protective efficacy comparable to spike mRNA-LNPs. Our study identifies a platform-specific priming mechanism for DNA-LNPs divergent from mRNA-LNPs or adjuvanted protein, suggesting avenues for this approach in prophylactic and therapeutic vaccine development.Copyright © 2025 The Authors. Published by Elsevier Inc. All rights reserved.
Electro-active evanescent-wave cavity ring-down spectroscopy immunosensor for influenza virus detection
Alnaanah, Qatamin, Mendes et al
Biomed Opt Express (2025) 16 (3), 982-994
Abstract: The early and accurate detection of viral pathogens is critical for effective disease management and public health safety. This study introduces an immunosensor that integrates an electro-active evanescent-wave cavity ring-down spectroscopy (EW-CRDS) platform with a sandwich-type bioassay for label-free detection of the influenza A (H5N1) hemagglutinin (HA) protein, achieving a detection limit of 15 ng/mL. The sensor is constructed by functionalizing the EW-CRDS platform within a micro-electrochemical flow cell with a monoclonal antibody specific to the target antigen. Upon antigen binding, a secondary polyclonal antibody conjugated with a redox-active methylene blue dye is captured. This dye undergoes reversible optical signal changes during redox transitions, which are electrochemically modulated and detected with high sensitivity. Unlike conventional approaches, this sensor employs electrochemical modulation to amplify surface-specific optical signals while reducing processing time and minimizing background noise. The results demonstrate the potential of this technology for real-time monitoring and rapid, reliable diagnosis of infectious diseases, offering excellent sensitivity and ease of operation in detecting influenza viruses. This work highlights the promise of the electro-active EW-CRDS platform for antigen detection in clinical settings.© 2025 Optica Publishing Group.
Pathogenicity and transmissibility of bovine-derived HPAI H5N1 B3.13 virus in pigs
Kwon, Trujillo, Carossino et al
bioRxiv (2025)
Abstract: Since the first emergence of highly pathogenic avian influenza (HPAI) H5N1 viruses in dairy cattle, the virus has continued to spread, reaching 17 states and at least 970 dairy herds in the United States. Subsequently, spillovers of the virus from dairy cattle to humans have been reported. Pigs are an important reservoir in influenza ecology because they serve as a mixing vessel in which novel reassortant viruses with pandemic potential can be generated. Here, we show that oro-respiratory infection of pigs resulted in productive replication of a bovine-derived HPAI H5N1 B3.13 virus. Infectious virus was mainly identified in the lower respiratory tract of principal infected pigs, and sero-conversion was observed in most of the principal pigs at later time points. In one animal, we detected the emergence of a mutation in hemagglutinin (HA) previously associated with increased affinity for "mammalian-type" α2,6-linked sialic acid receptors, but this mutation did not reach consensus levels. Sentinel contact pigs remained sero-negative throughout the study, indicating lack of transmission. The results support that pigs are susceptible to a bovine-derived HPAI H5N1 B3.13 virus, but this virus did not replicate as robustly in pigs as mink-derived HPAI H5N1 and swine-adapted influenza viruses.
Showing 1-4 of 4977 papers.
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