Mycobacterium tuberculosis Specific Neutra™ Antibody Products
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Are you currently facing challenges in developing highly specific and sensitive Tuberculosis (TB) diagnostics, particularly in distinguishing latent infection or obtaining reliable detection reagents for complex clinical samples? Our M. tuberculosis Specific Neutra™ Antibody Products help you accelerate TB diagnostic development and basic research, obtaining high-specificity detection reagents through advanced antibody engineering and high-throughput validation platforms.
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Introduction of M. tuberculosis
Mycobacterium tuberculosis (Mtb) is the slow-growing bacillus responsible for Tuberculosis (TB), a leading global cause of death. Mtb is defined by a lipid-rich cell wall (including mycolic acids and lipoarabinomannan (LAM)) that confers resistance and is highly immunogenic. Its slow growth and ability to enter a latent, non-replicating state complicate diagnosis. Mtb primarily infects and survives within alveolar macrophages by inhibiting phagosome-lysosome fusion, leveraging key virulence factors like ESAT-6 and CFP-10 to modulate the host immune response. TB manifests as latent (asymptomatic) or active disease. Accurate immunological detection of specific secreted proteins, such as ESAT-6 and CFP-10, is critical for differentiating infection status.
Fig.1 An overview of adaptive immunity to Mtb infection, and the progression of TB disease presentations.1
Antibodies Against M. tuberculosis
Antibodies against Mtb antigens are indispensable, highly selective tools for research, diagnostics, and therapeutics. We target well-studied, specific antigens—like the virulence factors ESAT-6 and CFP-10 (for active infection diagnostics), the cell wall lipoglycan Lipoarabinomannan (LAM) (for rapid clinical urine tests), and the Ag85 Complex and GlnA1 (for research into cell wall biology and drug targets). These reagents are utilized extensively to develop serological diagnostics for rapid point-of-care detection in patient samples (blood, urine), act as high-affinity probes for basic research on Mtb protein expression and function, and support drug development through high-throughput monitoring of anti-TB compound effects on antigen secretion.
Fig.2 Potential functions of antibodies against Mtb.1
Why Choose Us?
Creative Biolabs is dedicated to supplying the highest quality M. tuberculosis reagents, backed by over 20 years of expertise in infectious disease biology. We understand your success depends on reliable tools.
- Exceptional Specificity and Quality Control: Our Neutra™ antibodies undergo rigorous validation, including epitope mapping and affinity measurements, ensuring minimal cross-reactivity and lot-to-lot consistency crucial for clinical applications and longitudinal studies.
- Broad Versatility and Coverage: We offer an extensive catalog covering both secreted virulence factors (ESAT-6, CFP-10) and structural components (LAM). Each antibody is guaranteed compatible across multiple platforms, including ELISA, WB, IF, and IHC, ensuring seamless integration into diverse diagnostic and research pipelines.
- Proven Reliability: Our antibodies have been featured in research by leading global institutions, with successful outcomes documented in Published Data, demonstrating their utility in complex biological matrices.
FAQs
Q: How can I ensure the antibody I choose is specific only to M. tuberculosis and not to related environmental mycobacteria (NTMs)?
A: High specificity is ensured by targeting unique Mtb antigens like the ESAT-6/CFP-10 complex (absent in most NTM strains). Validation includes comprehensive cross-reactivity testing against common NTMs using standardized immunoassays; always review the product's NTM specificity data to confirm its suitability for your application.
Q: What is the recommended application for detecting active infection versus simply determining exposure to the pathogen?
A: For active infection detection, prefer antibodies targeting secreted antigens (like ESAT-6 or LAM), as these are shed in high concentrations during disease. For exposure/immune response studies, antibodies for T-cell assays (like IGRA) or those targeting cell wall components are more relevant. The choice depends entirely on the specific biomarker associated with the disease state you are investigating.
Q: Are these high-affinity reagents suitable for use in high-throughput point-of-care diagnostic platforms?
A: Absolutely. High-affinity reagents are vital for point-of-care (POC) tests like Lateral Flow Assays (LFAs) because they maximize signal detection from low-concentration biomarkers in minimal volumes. Their stability and robust binding kinetics ensure the reliability and speed required for decentralized, high-throughput diagnostic screening in resource-limited settings.
Q: What factors should I consider when selecting a primary antibody to detect a protein that is only transiently expressed during the bacterial lifecycle?
A: When dealing with transiently expressed or low-abundance targets, prioritize monoclonal antibodies with extremely high affinity (low nanomolar to picomolar range). Additionally, ensure the antibody is compatible with sensitive detection methods, such as Western Blotting or highly sensitive Immunofluorescence microscopy, and amplification techniques (like use with HRP or fluorescent labels), to capture the ephemeral signal.
Q: For functional assays, such as Mtb protein inhibition studies, is a monoclonal or a polyclonal antibody generally more effective?
A: For specific functional inhibition, a monoclonal antibody is typically the superior choice. Monoclonals bind a single epitope with high precision, allowing for the targeted blocking of a specific functional domain. Polyclonals, while providing a strong signal for general detection, may be less effective or introduce variability in blocking experiments due to their heterogeneous nature.
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REFERENCE
- McIntyre, Sophie et al. "Antibodies as clinical tools for tuberculosis." Frontiers in immunology vol. 14 1278947. 14 Dec. 2023, Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3389/fimmu.2023.1278947
