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Anthrax PA Toxin Specific Neutra™ Antibody Products

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Are you currently facing long drug development cycles or challenges in antibody development for biodefense? Our Anthrax PA Toxin Specific Neutra™ Antibody Products help you develop highly specific therapeutics and diagnostic tools through advanced recombinant DNA technology and high-precision epitope mapping. Creative Biolabs provides validated neutralizing solutions to streamline your research and combat the deadly effects of Bacillus anthracis toxins.

Introduction of Anthrax PA Toxin

Anthrax is a severe infectious disease caused by the Gram-positive, spore-forming bacterium Bacillus anthracis. The primary driver of its pathogenesis is the secretion of a tripartite exotoxin system consisting of three non-toxic proteins that assemble into lethal complexes: Protective Antigen (PA), Lethal Factor (LF), and Edema Factor (EF).

Structure and Mechanism

Protective Antigen (PA, 83 kDa) is the central "B" component of the toxin, acting as a delivery vehicle for the enzymatic "A" components (LF and EF). PA is composed of four distinct domains:

  • Domain 1: Contains the furin cleavage site (RKKR) where PA83 is processed into PA63.
  • Domain 2: Crucial for membrane insertion and pore formation.
  • Domain 3: Facilitates the oligomerization of PA monomers.
  • Domain 4: Responsible for binding to host cell receptors, primarily TEM8 (Tumor Endothelium Marker-8) and CMG2 (Capillary Morphogenesis Protein 2).

Signaling and Pathogenesis

Once PA binds to a receptor, it is cleaved by host proteases, allowing the remaining PA63 to form a heptameric or octameric "pre-pore." This structure then captures LF and EF. Upon endocytosis and acidification of the endosome, the pre-pore undergoes a conformational change into a translocase channel, releasing LF and EF into the cytosol. LF, a zinc-dependent metalloprotease, cleaves mitogen-activated protein kinase kinases (MAPKKs), disrupting critical cell signaling pathways and inducing apoptosis. EF, a calmodulin-dependent adenylate cyclase, elevates cAMP levels, leading to massive edema and immunosuppression.

Clinical Impact

The clinical progression of inhalational anthrax is often rapid and fatal once toxin levels reach a critical threshold. While antibiotics can kill the bacteria, they cannot neutralize the toxins already present in the bloodstream. This underscores the vital importance of neutralizing antibodies (nAbs) as a therapeutic intervention to halt toxin-mediated damage.

Understanding the mechanisms behind anthrax toxins. (OA Literature) Fig.1 Understanding the mechanisms behind anthrax toxins and their development into a pioneering tool.1

Applications of anti-Anthrax PA Neutralizing Antibodies

Anti-PA neutralizing antibodies are indispensable tools in both biodefense research and clinical development. Their primary applications include:

  • Passive Immunotherapy: Serving as an immediate post-exposure prophylactic or treatment option when combined with antibiotics. By blocking the entry of LF and EF into cells, these antibodies prevent the systemic "shutdown" of the host immune system.
  • Diagnostic Assay Development: High-affinity nAbs are utilized in ELISA-based detection kits and lateral flow assays for the rapid identification of B. anthracis PA in clinical or environmental samples.
  • Vaccine Potency Testing: These antibodies serve as gold-standard controls in neutralization assays to evaluate the efficacy of next-generation recombinant PA (rPA) vaccines.
  • Mechanistic Research: Researchers use domain-specific nAbs to study the kinetics of toxin assembly, receptor hijacking, and the transition from pre-pore to membrane-spanning pore.

Our anti-Anthrax PA Toxin Neutralizing Antibodies

Creative Biolabs offers a robust portfolio of Neutra™ antibodies engineered to target every stage of the PA-mediated intoxication process. Our catalog includes:

  • Receptor-Blocking Antibodies: Monoclonal antibodies targeting Domain 4 that competitively inhibit the interaction between PA and host receptors (CMG2/TEM8).
  • Proteolysis Inhibitors: Specific clones that bind to Domain 1, preventing the furin-mediated cleavage of PA83 into its active PA63 form.
  • Oligomerization Blockers: Antibodies that interfere with the lateral assembly of PA monomers, halting the formation of the toxic heptamer.
  • Pore-Formation Inhibitors: Advanced Neutra™ products that stabilize the pre-pore structure, preventing the pH-dependent conversion into a translocase channel.

Each antibody undergoes stringent quality control, including surface plasmon resonance (SPR) for affinity measurement and cell-based neutralization assays (TNA) to ensure functional potency. Creative Biolabs also provides custom conjugation services (e.g., biotin, HRP, or fluorescent dyes) to facilitate seamless integration into your existing laboratory protocols.

Creative Biolabs is dedicated to providing high-performance biological reagents that empower researchers to overcome the challenges of biopharmaceutical development. Our Anthrax PA Toxin Specific Neutra™ Antibody Products represent the pinnacle of specificity and neutralizing power, designed to support your project from discovery through preclinical validation.

To learn more about our products or to discuss a custom antibody development project, please reach out to our scientific experts. We are committed to providing technical support and rapid turnaround times for all your research needs.

Reference

  1. Richter, Sandy, and Gudula Schmidt. "Anthrax Toxin: A Pioneer of Targeted Protein Toxins." Toxins vol. 17,11 533. 29 Oct. 2025, Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/toxins17110533
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Anthrax PA toxin (Carboxyl domain) Specific Recomb™ Antibody (V3S-0324-FY7), Human IgG (CAT#: V3S-1022-YC1693)

Target: Anthrax toxin PA

Host Species: Human

Target Species: Bacillus anthracis,

Application: ELISA,

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Recombinant Anti-Anthrax toxin PA Antibody (V3S-1022-YC1694) (CAT#: V3S-1022-YC1694)

Target: Anthrax toxin PA

Host Species: Human

Target Species: Bacillus subtilis,

Application: ELISA,

For research use only, not directly for clinical use.


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