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Monoclonal Anti-HA (strain A/Bangkok/1/1979 (H3N2)) Antibody, Mouse IgG1 (2D10)

抗体来源(Source)

Monoclonal Anti-HA (strain A/Bangkok/1/1979 (H3N2)) Antibody, Mouse IgG1 (2D10) is a Mouse monoclonal antibody produced from a hybridoma created by fusing SP2/0 myeloma and Mouse B-lymphocytes.

克隆号(Clone)

2D10

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

免疫原(Immunogen)

Recombinant Influenza A [A/Bangkok/1/1979 (H3N2)] HA derived from human 293 cells.

特异性(Specificity)

This product is a specific antibody specifically reacts with Influenza A [A/Bangkok/1/1979 (H3N2)] HA.

应用(Application)

ApplicationRecommended Usage
ELISA0.4-100 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 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/Wisconsin/588/2019 (H1N1)] HA, His Tag (Cat. No. HA1-V52H3).
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-V52H14).
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 [A/Hong Kong/483/97 (H5N1)] HA, His Tag (Cat. No. HA1-V5229).
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 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 (Vietnam/1194/2004(H5N1)) Hemagglutinin (HA) Protein, His Tag (Cat. No. HA1-V52H9).
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).

 

电泳(SDS-PAGE)

Hemagglutinin/HA (Influenza Virus) SDS-PAGE

Monoclonal Anti-HA (strain A/Bangkok/1/1979 (H3N2)) Antibody, Mouse IgG1 (2D10) 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/Bangkok/1/1979 (H3N2)] Hemagglutinin (HA) Protein, His Tag (MALS verified) (Cat. No. HA2-V52H3) at 2 μg/mL (100 μL/well) can bind Monoclonal Anti-HA (strain A/Bangkok/1/1979 (H3N2)) Antibody, Mouse IgG1 (2D10) (Cat. No. HA2-Y181) with a linear range of 0.195-6.25 ng/mL. (QC 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

A highly stable lyophilized mRNA vaccine for Herpes Zoster provides potent cellular and humoral responses
Munoz-Moreno, Allaj, Gadee et al
NPJ Vaccines (2025) 10 (1), 49
Abstract: Herpes zoster (HZ) is a painful vesicular rash that occurs upon varicella-zoster virus (VZV) reactivation in older adults and immunocompromised individuals. Although there is currently an approved vaccine for the prevention of shingles, its administration is commonly associated with high reactogenicity. This highlights the need to develop new vaccine alternatives with long lasting immunity and improved tolerability upon administration. In the present study, 10 different vaccine candidate designs using two different codon optimizations targeting the VZV glycoprotein E (gE) were generated. A subset of mRNA constructs were formulated into lipid nanoparticles and assessed for their ability to induce specific cellular and humoral immune responses following vaccination in mice. Notably, the selected mRNA vaccine candidates induced high levels of antibodies and robust CD4+ but also CD8+ immune responses. Moreover, we showed that our alternate lyophilized vaccine provides comparable immunogenicity to current liquid frozen formulations and is stable under long-term storage conditions.© 2025. The Author(s).
Immune response and safety of the adjuvanted recombinant zoster vaccine in adults 50 years of age and older in India: A randomized phase 3 trial
Naficy, Chugh, Tariq et al
Vaccine (2025) 50, 126819
Abstract: Reactivation of latent varicella-zoster virus can cause herpes zoster (shingles) and associated complications, such as post-herpetic neuralgia. The adjuvanted recombinant zoster vaccine (RZV) was shown to be efficacious in preventing herpes zoster and have an acceptable safety profile in adults ≥50 years of age. However, no clinical data on RZV were available in an Indian population. The aim of the current study was to assess the immunogenicity and safety of RZV in adults ≥50 years of age in India.In this randomized, placebo-controlled, observer-blind, multi-center trial, conducted between February 2022 and March 2023, participants ≥50 years of age received two doses (with a two-month interval) of RZV (N = 143) or placebo (N = 145). Blood samples were collected pre-dose 1 and one month post-dose 2 to quantify anti-glycoprotein E (gE) antibody concentrations. Solicited adverse events (AEs) with onset within seven days and unsolicited AEs with onset within 30 days following any RZV or placebo dose were recorded. Serious AEs (SAEs) and potential immune-mediated diseases (pIMDs) were recorded until trial end (six months post-dose 2).At one month post-dose 2, vaccine response rate in the RZV group was 85.7 % (95 % confidence interval [CI]: 78.4 %-91.3 %), meeting the primary objective's success criterion (lower limit of 95 % CI ≥60 %). The adjusted geometric mean anti-gE antibody concentration ratio between the RZV and placebo groups was 19.8 (95 % CI, 14.1-27.8), meeting the secondary objective's success criterion (lower limit of 95 % CI ≥3). Solicited AEs were reported by 103 (72.0 %) RZV and 86 (59.3 %) placebo recipients; most had mild-to-moderate severity. No intervention-related unsolicited AE or SAE and no pIMD or death were reported.Two doses of RZV induced a robust antibody response, comparable to that reported in other populations, and had a safety profile similar to the known RZV safety profile.gov: NCT05219253.Copyright © 2025 GSK. Published by Elsevier Ltd.. All rights reserved.
Immune Response to an Adjuvanted Recombinant Zoster Vaccine in Japanese Patients with Rheumatoid Arthritis Receiving Upadacitinib (End Zoster-J Study): Study Protocol for an Exploratory Parallel Triple-Arm Prospective Trial
Watanabe, Fujii, Imai et al
J Clin Med (2024) 13 (23)
Abstract: Background: Janus kinase (JAK) inhibitors have emerged as a new class of disease-modifying anti-rheumatic drugs in the treatment of rheumatoid arthritis (RA). However, herpes zoster is one of the common adverse events of JAK inhibitors, including upadacitinib, which is especially high in Japanese patients with RA compared to those from Western countries. Recombinant zoster vaccine (Shingrix®) is an adjuvanted subunit vaccine containing varicella-zoster virus (VZV) glycoprotein E (gE) that is effective in adults over 50 years of age. Despite this, no studies have examined its immunogenicity in Japanese patients receiving upadacitinib. Therefore, this study aims to examine the effectiveness of the recombinant zoster vaccine in Japanese patients with RA receiving upadacitinib. Methods: This is a single-center, exploratory, interventional, open-label, parallel triple-arm, prospective study. A total of 69 patients (23 in each group) aged 50 years or over and treated with a stable dose of methotrexate (MTX) monotherapy (6-12 mg/week), upadacitinib monotherapy (15 mg/day), or MTX (6-12 mg/week) + upadacitinib 15 mg/day (combination) for at least 1 month prior to study entry will be included. Moreover, all three groups will receive two intramuscular injections of the recombinant zoster vaccine at 8-week intervals. The primary endpoint is the proportion of positive anti-gE antibodies 4 weeks after the second injection. Secondary endpoints include RA disease activity, positive gE-specific CD4+ T-cells, and VZV-specific antibodies at indicated time points. Data on outcome measures will be collected at baseline and at 4, 8, 12, and 20 weeks. Endpoints will be summarized using descriptive statistics from baseline therapy, and results will be compared in an exploratory manner. Discussion: Despite the limited generalizability due to its design as a single-center, single-ethnic study, small sample size, and short observation period, this study provides evidence on the effectiveness and tolerability of recombinant zoster vaccine in Japanese patients with RA receiving upadacitinib.
Structures of the Varicella Zoster Virus Glycoprotein E and Epitope Mapping of Vaccine-Elicited Antibodies
Harshbarger, Holzapfel, Seraj et al
Vaccines (Basel) (2024) 12 (10)
Abstract: Background: Varicella zoster virus (VZV) is the causative agent for chickenpox and herpes zoster (HZ, shingles). HZ is a debilitating disease affecting elderly and immunocompromised populations. Glycoprotein E (gE) is indispensable for viral replication and cell-to-cell spread and is the primary target for anti-VZV antibodies. Importantly, gE is the sole antigen in Shingrix, a highly efficacious, AS01B-adjuvanted vaccine approved in multiple countries for the prevention of HZ, yet the three-dimensional (3D) structure of gE remains elusive. Objectives: We sought to determine the structure of VZV gE and to understand in detail its interactions with neutralizing antibodies. Methods: We used X-ray crystallography and cryo-electron microscopy to elucidate structures of gE bound by recombinant Fabs of antibodies previously elicited through vaccination with Zostavax, a live, attenuated vaccine. Results: The 3D structures resolve distinct central and C-terminal antigenic domains, presenting an array of diverse conformational epitopes. The central domain has two beta-sheets and two alpha helices, including an IgG-like fold. The C-terminal domain exhibits 3 beta-sheets and an Ig-like fold and high structural similarity to HSV1 gE. Conclusions: gE from VZV-infected cells elicits a human antibody response with a preference for the gI binding domain of gE. These results yield insights to VZV gE structure and immunogenicity, provide a framework for future studies, and may guide the design of additional herpesvirus vaccine antigens. Teaser: Structures of varicella zoster virus glycoprotein E reveal distinct antigenic domains and define epitopes for vaccine-elicited human antibodies.
Showing 1-4 of 115 papers.
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