Amyloid Specific Neutra™ Antibody Products

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Accelerate Your Research and Development!

Are you currently facing challenges in accurately detecting and quantifying amyloid aggregates, struggling with the specificity of your research tools, or seeking reliable solutions for biomarker discovery in neurodegenerative diseases? Creative Biolabs’ Amyloid Specific Antibody Products help you achieve precise and reliable amyloid detection, enabling robust research into protein misfolding disorders and supporting the development of advanced diagnostics and therapeutics through high-specificity antibodies and comprehensive immunoassay tools.

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Introduction of Amyloid

Amyloids are highly ordered protein aggregates characterized by a fibrillar morphology, typically 7–13 nm in diameter, and a distinctive cross-β sheet secondary structure. This unique structural arrangement allows them to be stained by specific dyes like Congo red, exhibiting a characteristic yellow-green birefringence under polarized light. While some amyloids serve normal biological functions, such as in hormone storage or bacterial biofilm formation, their pathological accumulation is linked to over 50 human diseases, collectively known as amyloidoses.

Pathogenic amyloids form when previously healthy proteins misfold and aggregate into insoluble fibrous deposits within and around cells. This protein misfolding and deposition disrupts the healthy function of tissues and organs. Examples of amyloid-associated diseases include Alzheimer's disease (AD), where amyloid-beta (Aβ) peptides form plaques in the brain; Parkinson's disease, involving α-synuclein aggregation; and systemic amyloidoses, where various proteins like immunoglobulin light chains (AL amyloidosis) or transthyretin (ATTR amyloidosis) deposit in organs such as the kidneys, heart, and gastrointestinal tract. The formation of these fibrils is a nucleation-dependent process, resembling crystallization, where precursor proteins slowly oligomerize to form nuclei, followed by rapid elongation. The toxicity of amyloid aggregates is thought to stem from soluble oligomeric intermediates rather than the mature fibrils themselves, making their detection and characterization crucial for understanding disease pathogenesis and developing therapeutic interventions.

Fig 1. Schematic of Pathogenesis of Alzheimer’s disease. (OA Literature) Fig. 1 Pathogenesis of Alzheimer’s disease.1

Antibodies Against Amyloid

Antibodies targeting amyloid aggregates and their precursor proteins are indispensable tools in neurodegenerative disease research and diagnostics. These antibodies are designed to recognize specific conformations or epitopes present on amyloid fibrils or their soluble oligomeric forms. Their applications are broad and critical for advancing our understanding and management of amyloid-related disorders:

  • Immunohistochemistry (IHC) and Immunofluorescence (IF): Amyloid-specific antibodies are widely used to visualize and localize amyloid deposits in tissue sections, such as brain tissue in Alzheimer's disease or organ biopsies in systemic amyloidosis. This allows for the assessment of amyloid burden, distribution, and correlation with pathological changes.
  • Western Blotting (WB): These antibodies can detect specific amyloid precursor proteins or their cleaved fragments in cell lysates or tissue homogenates, providing insights into protein processing and aggregation pathways.
  • Enzyme-Linked Immunosorbent Assay (ELISA): ELISA-based assays utilizing amyloid-specific antibodies enable the sensitive and quantitative detection of amyloid peptides and their aggregates in biological fluids like cerebrospinal fluid (CSF) and plasma. This is crucial for biomarker discovery, diagnosis, and monitoring disease progression or therapeutic response.
  • Flow Cytometry (FACS): Antibodies can be used to detect intracellular or surface-bound amyloid species in cell populations, facilitating studies on cellular uptake, clearance mechanisms, and the impact of amyloid on cell viability.
  • Immunoprecipitation (IP): Amyloid-specific antibodies can be used to pull down amyloid aggregates or complexes for further biochemical characterization, including mass spectrometry to identify interacting proteins.
  • Therapeutic Development: Beyond diagnostics, amyloid-specific antibodies are being explored as potential therapeutic agents themselves, aiming to promote amyloid clearance or prevent aggregation. Passive immunization strategies, for instance, involve administering antibodies to clear existing plaques or neutralize toxic oligomers.

The development of highly specific antibodies capable of distinguishing between different amyloid conformations or stages of aggregation is paramount for accurate diagnosis and effective therapeutic strategies.

Why Choose Us?

Creative Biolabs’ Amyloid Specific Antibody Products are meticulously engineered to provide unparalleled precision and reliability for your research and diagnostic needs. These antibodies offer specific solutions for detecting various amyloid aggregates and their related precursor proteins, enabling researchers to accurately quantify amyloid presence, study protein misfolding pathways, and develop robust diagnostic and therapeutic tools. Our solutions facilitate the development of sensitive immunoassays, support pathological analysis, and aid in understanding the biological impact of amyloid formation, providing a crucial tool for both basic science and applied research in neurodegenerative diseases.

Our specific deliverables and solutions include:

  • Highly Specific Detection: Our antibodies are rigorously validated to ensure minimal cross-reactivity, providing accurate detection of amyloid aggregates in complex biological samples.
  • Quantitative Analysis: Facilitate precise quantification of amyloid burden in tissues and biofluids, essential for disease progression monitoring and therapeutic efficacy studies.
  • Biomarker Discovery and Validation: Support the identification and validation of novel amyloid-related biomarkers for early diagnosis and prognosis.
  • Drug Discovery and Development: Aid in screening and evaluating potential therapeutic compounds that target amyloid formation or clearance.
  • Pathological Characterization: Enable detailed immunohistochemical and immunofluorescence analysis of amyloid deposits in tissue sections, providing insights into disease pathology.

FAQs

Q: What are the primary applications for these antibodies in neurodegenerative disease research?

A: These antibodies are highly versatile and suitable for a broad range of applications, including ELISA, Western Blotting, Immunofluorescence, and immunohistochemistry. They are designed to meet the stringent requirements of both basic scientific research into protein misfolding mechanisms and the development of clinical diagnostic assays for conditions like Alzheimer's and Parkinson's disease.

Q: How do these antibodies ensure high specificity for amyloid aggregates?

A: Our antibodies are developed using advanced immunization strategies and rigorously screened against various amyloid conformations and related proteins. This meticulous approach ensures high specificity crucial for accurate research and diagnostic outcomes, minimizing false positives and enhancing data reliability.

Q: Can these antibodies differentiate between different forms of amyloid, such as monomers, oligomers, and fibrils?

A: Yes, we offer a selection of antibodies specifically designed to recognize distinct conformational epitopes present on different amyloid species. This allows researchers to differentiate between soluble oligomers, which are often considered the most toxic, and mature amyloid fibrils, providing critical insights into disease pathogenesis.

Q: What advantages do these antibodies offer in terms of sensitivity for detecting low-level amyloid burden?

A: Our antibodies are developed and optimized for exceptional sensitivity, enabling the detection of even low concentrations of amyloid aggregates. This high sensitivity is achieved through optimized antibody affinity and robust assay compatibility, providing reliable results even with challenging biological samples.

Q: Are these antibodies suitable for in vivo studies, such as animal models of amyloidosis?

A: Many of our antibodies are validated for in vivo applications, including immunohistochemistry in animal models of amyloidosis. We recommend reviewing the specific product datasheets or consulting with our scientific support team to ensure the antibody is appropriate for your particular in vivo experimental design.

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REFERENCE

  1. Sehar, Ujala et al. “Amyloid Beta in Aging and Alzheimer's Disease.” International journal of molecular sciences vol. 23,21 12924. 26 Oct. 2022, DOI:10.3390/ijms232112924. Distributed under Open Access license CC BY 4.0, without modification.
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Recombinant Human Anti-Amyloid (aa 1-42) Antibody (V3S-0622-YC2863) (CAT#: V3S-0622-YC2863)

Target: Amyloid

Host Species: Human

Target Species: Human,

Application: ELISA,WB,

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Recombinant Mouse Anti-Amyloid Antibody (V3S-0522-YC2892) (CAT#: V3S-0522-YC2892)

Target: Amyloid

Host Species: Mouse

Target Species: Human,

Application: ELISA,IHC,WB,FuncS,

For research use only, not directly for clinical use.


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