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Creative Biolabs

Tau Uptake and Seeding Assay Service

As a Contract Research Organization (CRO) specializing in neurobiology research, we understand the critical role of aberrant tau protein aggregation in neurodegenerative diseases such as Alzheimer's disease. (AD). Our highly sensitive in vitro tau uptake and seeding assays provide comprehensive support to research institutions and pharmaceutical companies, spanning from fundamental research to preclinical development. For further information regarding the products and services provided, project-specific consultation, and pricing, please submit an inquiry here.

Introduction

Transcellular transfer of tau. (Mudher, et al., 2017)

Tau protein uptake is a critical step in the insidious spread of tau pathology throughout the brain in neurodegenerative diseases like AD and frontotemporal dementia. Understanding the mechanisms by which tau is taken up by neurons—including endocytosis, transmembrane diffusion, and axonal transport—is crucial for developing therapies that can halt or slow disease progression.

Tau seeding is a critical mechanism in the progression of neurodegenerative diseases. In this process, misfolded tau proteins act as "seeds," converting normal tau into a pathological form that spreads between neurons. This prion-like propagation amplifies tau pathology, contributing to cognitive decline.

Available Assays at Creative Biolabs

  • Accurate Tau Seeding Model

By combining ultrasound treatment with heparin, we faithfully mimic the intricate process of tau aggregation. Utilizing recombinant tau protein, including both wild-type and the P301L mutant, we assess both uptake efficiency and seeding capacity. SDS-PAGE and immunofluorescence techniques are employed for quantitative analysis, providing detailed insights into the dynamics of tau aggregate formation and propagation.

  • Custom-Developed Neuron Models

Partner with Our Experts for Custom Neuronal Models: Our experienced team specializes in developing custom neuronal models for tau protein research. We work closely with you to select the optimal cell source (primary neurons, cell lines, or iPSC-derived neurons) and tailor the model to your exact specifications. Our expertise in cell culture and genetic engineering ensures that you receive a high-quality, reliable model to advance your research.

  • Exosome Isolation and Biomarker Analysis

Exosomes isolated from the central nervous system (CNS) were analyzed using ELISA, Western blot, and FACS to detect tau (total tau, pT181, pS396) and other AD-related biomarkers (Aβ42, NfL). These analyses provide valuable data for investigating the mechanisms underlying AD.

Case Study: SH-SY5Y Cell Model for Tau Internalization

Fig 1: Recombinant tau is internalized via LRP1-mediated endocytosis, which leads to its degradation in the lysosomes. Fig.1 Recombinant tau is internalized via LRP1-mediated endocytosis, leading to its degradation in lysosomes.2, 3

Uptake and Seeding Assay Service for Tau Isoforms

Identify Tau Isoforms Involved in Alzheimer's Disease: Creative Biolabs' tau uptake and seeding assays can help you identify specific tau isoforms (0N, 1N, 2N, 1R, 2R, 3R, 4R) implicated in AD, including those contributing to the imbalanced 4R/3R ratio. Gain valuable insights into tau pathology and accelerate your research.

Fig 2: The binding affinity of tau protein for the LRP1 receptor is significantly reduced by phosphorylation. Fig.2 Phosphorylation significantly reduces the binding affinity of tau protein for the LRP1 receptor.2, 3

Partner with Our Experts for Breakthrough Discoveries: Our team of specialists provides one-on-one technical consultation, regulatory support, and proactive project management. Whether you're a small biotech or a leading research institute, we're committed to helping you achieve your research goals with maximum efficiency and minimal cost.

References

  1. Mudher, Amrit, et al. "What is the evidence that tau pathology spreads through prion-like propagation?" Acta neuropathologica communications 5 (2017): 1-20.
  2. Cooper, Joanna M., et al. "Regulation of tau internalization, degradation, and seeding by LRP1 reveals multiple pathways for tau catabolism." Journal of Biological Chemistry 296 (2021).
  3. Distributed under Open Access license CC BY 4.0, without modification.
For Research Use Only. Not For Clinical Use.
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