Amytracker - Information – Ebba Biotech AB

Amytracker are small fluorescent molecules for detection of protein aggregates.

Five Amytracker variants are available. All Amytracker variants are designed to bind to the Congo red binding pocket on the amyloid fibril. A minimum of eight in-register parallel-β-strands are required for binding. The Amytracker variants differ in affinity and spectral properties. As Amytracker are structural markers, you can achieve reliable fluorescent labeling of amyloids derived from a variety of amyloidogenic proteins or peptides from different species.

Amytracker are suitable for detecting amyloids in fresh or fixed tissue sections and cells. It is possible to use them for fibrillation assays and for systemic injection in vivo. They are exceptionally photo- and thermostable and allow for easy handling in any application. Amytracker work in a wide range of salt and pH conditions. When the pH is altered during the experiment, pH controls should be included. Amytracker can be used with fluorescence plate readers, fluorescence microscopes and confocal laser scanning microscopes, fluorescence life time imaging, fluorescence cytometry, Total internal reflection fluorescence (TIRF) microscopy and Multiphoton microscopy.

Store your Amytracker product in the fridge and use the opened container within 12 months. Amytracker is for research use only and is not for resale.

Amytracker Mix&Try is our recommended option for starting out with using Amytracker. It contains 10 µL of each variant. Testing the variants will allow you to determine which Amytracker is best suited for your experiments and available instruments.

All Amytracker variants label Aβ plaques and neurofibrillary tangles in tissue sections with AD pathology and α-synuclein aggregates in tissue sections with PD pathology. The optotracers are exceptionally photostable and fluorogenic. The variants differ with regards to affinity, cellular uptake and excitation and emission wavelengths (see Table below). When bound to a target, Amytracker can be imaged using epifluorescence, confocal and superresolution microscopy. Spectral information can be acquired using a fluorescence spectrophotometer. Contact us to learn more about Amytracker applications.

Table: Excitation- and emission wavelengths as well as recommended filter sets.
	Ex_max	Em_max	Recommended filter-sets
Amytracker 480	420 nm	480 nm	DAPI
Amytracker 520	460 nm	520 nm	FITC, GFP
Amytracker 540	480 nm	540 nm	FITC, GFP, YFP
Amytracker 630	520 nm	630 nm	PI, Cy3, TxRed, mCherry, Cy3.5
Amytracker 680	530 nm	680 nm	PI, mCherry, Cy3.5

Amytracker 680 is our red optotracer for labeling protein aggregates with repetitive arrangement of β-sheets. It labels Aβ plaques and neurofibrillary tangles in tissue sections with AD pathology and α-synuclein aggregates in tissue sections with PD pathology. Specifically, Amytracker 680 has been used to study amyloid formation during abnormal coagulation, Lewy body formation in a seeding based neuronal model, accumulation of misfolded proteins in the nucleolus and intracerebral formation of Aβ plaques using multiphoton microscopy. Contact us to learn more about Amytracker applications.

As all our optotracers, Amytracker 680 is exceptionally photostable and fluorogenic. When bound to a target, Amytracker 680 can be imaged using epifluorescence, confocal and superresolution microscopy. Spectral information can be acquired using a fluorescence spectrophotometer. Use recommended filter sets as well as excitation- and emission wavelengths according to the following table.

Table: Excitation- and emission wavelengths as well as recommended filter sets.
	Ex_max	Em_max	Recommended filter-sets
Amytracker 680	530 nm	680 nm	PI, mCherry, Cy3.5

Amytracker 680 is available in four different formulations (See volumes and prices in the drop-down list below):

Aqueous: 1 mg/ml solution in ultrapure water. The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations. To prevent evaporation of the aqueous solvent, close the container carefully after use, spin down liquid and use up small volumes quickly.
DMSO: 1 mg/ml solution in DMSO to prevent solvent evaporation. The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations.
Solid: 1 mg solid lyophilised in a sterile injection bottle. We recommend dilution to 4 mg/ml in physiological saline followed by intravenous injection with a total dose of 5 mg/KG.
Drop&Shine: 5 ml ready-to-use product in mounting medium. Ideal for use in tissue sections. Add a some Drop&Shine and mount your slide to detect amyloids within minutes.

Amytracker 630 is our orange optotracer for labeling protein aggregates with repetitive arrangement of β-sheets. It labels Aβ plaques and neurofibrillary tangles in tissue sections with AD pathology and α-synuclein aggregates in tissue sections with PD pathology. Contact us to learn more about Amytracker applications.

As all our optotracers, Amytracker 630 is exceptionally photostable and fluorogenic. When bound to a target, Amytracker 630 can be imaged using epifluorescence, confocal and superresolution microscopy. Spectral information can be acquired using a fluorescence spectrophotometer. Use recommended filter sets as well as excitation- and emission wavelengths according to the following table.

Table: Excitation- and emission wavelengths as well as recommended filter sets.
	Ex_max	Em_max	Recommended filter-sets
Amytracker 630	520 nm	630 nm	PI, Cy3, TxRed, mCherry, Cy3.5

Amytracker 630 is available as 1 mg/ml solution in ultrapure water (Aqueous) with volumes ranging from 10 - 200 µL (See volumes and prices in the drop-down list below). The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations. To prevent evaporation of the aqueous solvent, close the container carefully after use, spin down liquid and use up small volumes quickly.

Amytracker 540 is our yellow optotracer for labeling protein aggregates with repetitive arrangement of β-sheets. It labels Aβ plaques and neurofibrillary tangles in tissue sections with AD pathology and α-synuclein aggregates in tissue sections with PD pathology. Contact us to learn more about Amytracker applications.

As all our optotracers, Amytracker 540 is exceptionally photostable and fluorogenic. When bound to a target, Amytracker 540 can be imaged using epifluorescence, confocal and superresolution microscopy. Spectral information can be acquired using a fluorescence spectrophotometer. Use recommended filter sets as well as excitation- and emission wavelengths according to the following table.

Table: Excitation- and emission wavelengths as well as recommended filter sets.
	Ex_max	Em_max	Recommended filter-sets
Amytracker 540	480 nm	540 nm	FITC, GFP, YFP

Amytracker 540 is available as 1 mg/ml solution in ultrapure water (Aqueous) with volumes ranging from 10 - 200 µL (See volumes and prices in the drop-down list below). The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations. To prevent evaporation of the aqueous solvent, close the container carefully after use, spin down liquid and use up small volumes quickly.

Amytracker 520 is our green optotracer for labeling protein aggregates with repetitive arrangement of β-sheets. It labels Aβ plaques and neurofibrillary tangles in tissue sections with AD pathology and α-synuclein aggregates in tissue sections with PD pathology. Contact us to learn more about Amytracker applications.

As all our optotracers, Amytracker 520 is exceptionally photostable and fluorogenic. When bound to a target, Amytracker 520 can be imaged using epifluorescence, confocal and superresolution microscopy. Spectral information can be acquired using a fluorescence spectrophotometer. Use recommended filter sets as well as excitation- and emission wavelengths according to the following table.

Table: Excitation- and emission wavelengths as well as recommended filter sets.
	Ex_max	Em_max	Recommended filter-sets
Amytracker 520	460 nm	520 nm	FITC, GFP

Amytracker 520 is available as 1 mg/ml solution in ultrapure water (Aqueous) with volumes ranging from 10 - 200 µL (See volumes and prices in the drop-down list below). The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations. To prevent evaporation of the aqueous solvent, close the container carefully after use, spin down liquid and use up small volumes quickly.

Amytracker 480 is our blue optotracer for labeling protein aggregates with repetitive arrangement of β-sheets. It labels Aβ plaques and neurofibrillary tangles in tissue sections with AD pathology and α-synuclein aggregates in tissue sections with PD pathology. Specifically, Amytracker 480 has been used to study amyloid formation during abnormal coagulation. Contact us to learn more about Amytracker applications.

As all our optotracers, Amytracker 480 is exceptionally photostable and fluorogenic. When bound to a target, Amytracker 480 can be imaged using epifluorescence, confocal and superresolution microscopy. Spectral information can be acquired using a fluorescence spectrophotometer. Use recommended filter sets as well as excitation- and emission wavelengths according to the following table.

Table: Excitation- and emission wavelengths as well as recommended filter sets.
	Ex_max	Em_max	Recommended filter-sets
Amytracker 480	420 nm	480 nm	DAPI

Amytracker 480 is available as 1 mg/ml solution in ultrapure water (Aqueous) with volumes ranging from 10 - 200 µL (See volumes and prices in the drop-down list below). The product should be diluted 1:1000 before use. For use in live-cells, sometimes 1:500 is necessary due to uptake limitations. To prevent evaporation of the aqueous solvent, close the container carefully after use, spin down liquid and use up small volumes quickly.

Labeling of protein aggregates in tissue sections or cells

Amytracker can be used to label protein aggregates in tissue sections or cells prepared by the most common techniques. It can be used in freshly sliced tissue without fixation but also in fixed cells or sections obtained from flash-frozen or paraffin embedded tissues. Generally, fixation in 4% PFA works well...
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Amytracker for systemic injection

Amytracker can be used for intravenous- or intraperitoneal injection in small animals to label protein aggregates in vivo. It will readily cross the blood brain barrier and can be imaged by intra-vital microscopy or after removing the tissue and preparation of microscope slides. For systemic injection, we recommend to use...
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Fibrillation assay

This protocol describes how Amytracker can be utilized for fibrillation assays and detection of amyloids in liquid samples. As all Amytracker variants are highly fluorescent only when they are bound to their target, they are ideally suited for spectrophotometric analysis. We recommend to perform a titration to use Amytracker in...
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Live-cell imaging

All Amytracker variants cross the cell membrane of living cells without permeabilization. Due to their low background fluorescence and minimal interference with biological autofluorescence, we recommend Amytracker 630 or Amytracker 680 for live-cell imaging. As Amytracker do not bleach easily, they are excellently suited for repeated illumination during time-lapse imaging....
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Amytracker shows how α-Synuclein aggregates at the mitochondrial membrane

Faulty α-synuclein (α-Syn) aggregates in cells forming toxic α-Syn oligomers and finally Lewy Bodies which are the pathological hallmark of synucleinopathies. While Lewy Bodies are relatively easy to discern in a microscope, it turns out to be very difficult to investigate the early-intermediate forms of aggregates. A study published in...
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Studying the relationship between morphology and inflammatory effect of ɑ-synuclein aggregates

Parkinson's disease (PD) and Multiple System Atrophy (MSA) are both characterized by accumulation and misfolding of ɑ-synuclein (ɑ-syn). However, there are distinct differences between their pathology likely relating back to different strains of ɑ-syn aggregates. The goal of a study by De Luca et al. from IRCCS and SISSA in...
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Faulty ribosome quality control triggers amyloid aggregation

What causes the accumulation of toxic amyloid aggregates? An article by the group of Bingwei Lu from the Department of Pathology at Stanford University School of Medicine published in the journal Acta Neuropathologica Communications might have found the answer to this question. Their work shows that a defective ribosome quality...
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Amytracker labels amyloid forms of tau in a cell based model for tauopathies

Accumulation of abnormal tau protein in the brain has been described as pathological hallmark of a group of neurodegenerative disorders called tauopathies. The most common tauopathy is Alzheimer’s disease (AD). In AD, intracellular inclusions containing aggregates of hyperphosphorylated tau coexist with extracellular amyloid plaques containing aggregated amyloid-β (Aβ). Clinically, tau...
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Amyloids trigger proinflammatory signalling Multiple Myeloma

Multiple myeloma is a complex B-cell malignancy characterised by the accumulation of malignant plasma cells. Progression of multiple myeloma is related to dysregulated inﬂammatiory processes; especially leucocytes and tumor-associated macrophages (TAMs) are central during the initiation and progression of the disease and high concentration of TAMs often relates to drug...
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Amytracker: a tool to identify toxic dipeptide repeats

Repetitive genomic regions are known to expand across generations, due to errors during their replication, and cause a series of - mainly - neurological diseases collectively called repeat expansion diseases. One of these repetitive genomic regions is the GGGGCC (G4C2) locus in the C9orf72 gene. Its expansion is linked with...
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How mutations contribute to pathological diversity in synucleopathies

Alpha-synuclein (α-Syn) is a presynaptic neuronal protein encoded by the SNCA gene. It is expressed heavily in the brain and regulates synaptic vesicle trafficking and subsequent neurotransmitter release. Under certain conditions, α-Syn aggregates and forms, together with other components, intracellular inclusions called Lewy bodies (LBs) or Lewy Neurites (LN), which...
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Deciphering the complexity of intracellular Tau aggregates

Tau is an intrinsically disordered protein with the key function to stabilise axonal microtubules. In several neurological disorders collectively known as Tauopathies, tau proteins form aggregates that accumulate in cells and cause neuronal damage. The molecular mechanism which leads to tau aggregation is complex and liquid–liquid phase separation (LLPS), a...
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Linking aggregate size and toxicity using Amytracker

In the context of neurodegenerative diseases, large, fibrillar amyloid deposits - such as Lewy bodies, Amyloid plaques, and Neurofibrillary tangles - characterize the pathology of the disease but it has recently become evident that small, spherical aggregates below 20 nm in diameter are mainly responsible of the toxic response that...
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Protein aggregation in wound healing

Lipopolysaccharide (LPS) is a cell envelope glycolipid produced by most gram-negative bacteria. When LPS is recognized by Toll-like receptor 4 (TLR4) an innate host-response to bacterial infection is triggered. To achieve a robust antibacterial response while maintaining control of inﬂammatory processes, LPS has to be cleared from the infection site....
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Phase separated α-synuclein is more prone to aggregation

Alpha-synuclein (α-Syn) aggregation hallmarks a group of neurodegenerative diseases known as synucleinopathies with Parkinson’s disease as its most well-known representative. The molecular mechanism behind the aggregation of α-Syn is still not completely understood. Many aggregation-prone proteins, like α-Syn, are known to form phase-separated condensates and recent findings suggest that the...
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FL-OPTIR for studying biophysical properties of amyloids in cells and tissues

Infrared (IR) spectroscopy is an invaluable tool to study the biophysical properties of amyloid aggregates. Although historically used as a tool for composition analysis of chemical compounds as it measures the vibrational energy of chemical bonds, IR spectroscopy provides measures to analyse the size and rigidity of amyloid fibrils. Coupling...
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Spatial pattern of microglial activation in relation to amyloid plaques

Microglia cells play a vital role in regulating brain development, maintenance of neuronal networks, and injury repair. Their involvement in the progression of protein aggregation leading to neurodegenerative diseases is complex. While they can clear amyloid plaques and prevent their accumulation, dysfunctional microglia regulation may be a key factor in...
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Amyloidogenicity of SARS-CoV-2 spike protein

Infection with SARS-CoV-2 leads to patients developing the COVID-19 disease, which is a complex hyperinflammatory syndrome, characterised by acute respiratory distress (ARD). Aside from these severe respiratory symptoms, we now know that the virus can present in unexpected, varied, and long-lasting manners. Recent studies hint towards the amyloidogenicity of the...
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Lewy body formation in seeding based neuronal models

Parkinson’s disease is a brain disorder that causes unintended or uncontrollable movements, such as shaking, stiffness, and difficulty with balance and coordination. Symptoms usually begin gradually and worsen over time. As the disease progresses, people may have difficulty walking and talking. The basis of these symptoms is progressive neurodegeneration and...
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Prolonged stress leads to accumulation of misfolded proteins in the nucleolus

The nuclear proteome is rich in proteins which are prone to aggregate upon conformational stress. This might explain why intranuclear inclusions can often be found in neurodegenerative disorders associated with protein aggregation. Using a combination of fluorescence imaging, biochemical analyses, and proteomics, researchers at Max Planck Institute for Biochemistry around...
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Amytracker can be used for intracerebral multiphoton microscopy

A team of researchers from Massachusetts General Hospital and Harvard Medical School as well as Linköping University have used a fluorescent probe of the same type as Amytracker for multiphoton imaging of Amyloid-β deposits in transgenic mice in vivo. The fluorescent molecule clearly targeted and labeled core plaques in the...
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The clue to detect multiple systems atrophy?

In a study, recently published in Nature, a fluorescent tracer molecule similar to Amytracker has been used to detect α-synuclein aggregates in cerebrospinal fluid from patients with synucleopathy. Interestingly, the fluorescent tracer molecule was binding aggregates from patients with Multiple Systems Atrophy with higher affinity than aggregates from patients with...
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Anomalous fibrin amyloid formation

Lipopolysaccharides (LPS) from the Gram-negative cell envelope can be shed from dormant bacteria or from continual bacteria entry into the blood and serve to contribute to the chronic inflammation. The presence of highly substoichiometric amounts of LPS from Gram-negative bacteria caused fibrinogen clotting to lead to the formation of an...
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Amyloids in type-2 diabetes

Type-2 diabetes is a progressive condition marked by resistance towards the blood-sugar regulating hormone insulin. Recently, Type-2 diabetes is become recognized as an inflammatory condition which is often accompanied by cardiovascular complications. The teams around Prof. Etheresia Pretorius from Stellenbosh University and Prof. Douglas B. Kell from the University of...
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Advanced imaging

In a new study in the Journal of visualized experiments, the team around Prof. Peter Nilsson and Prof. Per Hammarström from Linköpings University describe how luminescent conjugated oligothiophenes (LCOs) can be used with Hyperspectral Imaging (HIS) and Fluorescence Lifetime Imaging (FLIM) to detect amyloid species. In a practical approach, the...
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Protein engineering for better PET radioligands

An approved method for visualization of Amyloid β (Aβ) plaques in patients suffering from Alzheimer's disease is Positron Emission Tomography (PET). This method requires a radiolabeled amyloid ligand. A frequently used molecule is Pittsburgh Compound B (PIB) which is a derivative of Thioflavin T. Radiolabeled PIB is well-suited to visualize...
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Artifical amyloids

A team of scientists around Frederic Rousseau from Switch Laboratory at KU Leuven have designed a biologically active amyloid from a peptide sequence occurring in vascular endothelial growth factor 2 (VEGFR2). The peptide, which the researchers named vascin forms artificial amyloids. The results show, however, that vascin amyloids are not...
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Multi-Laser / Multi-Detector Imaging with Amytracker

Amytracker are optotracers with structure-dependent photo-physical properties. All Amytracker variants are designed to bind to the Congo red binding pocket on the amyloid fibril and require a theoretical minimum of eight in-register parallel-β-strands for binding. Therefore, Amytracker reliably labels amyloids derived from a variety of amyloidogenic proteins or peptides from...
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Optotracing using Amytracker

Amytracker and Long Covid

Around 30% of the people infected with the SARS-CoV-2 virus report persistent symptoms for a long time after the acute infection ends. While the development of this long-term manifestation after COVID, referred to as Long COVID, has been framed as mysterious, it is actually a well described outcome of many...
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Amytracker and the age-pigment Lipofuscin

The macromolecules and organelles within cells are not permanent and need to get replaced over time. To do this, cells need to both produce new components and to degrade the old ones. The degradation of the bigger cellular structures depends on a process called autophagy. During autophagy, the cell envelopes...
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Amytracker for the study of tau aggregates

Tau is an intracellular protein which associates with microtubules and stabilizes them. Physiologically, Tau is phosphorylated to facilitate release from the microtubules and thereby favor microtubule shortening. In a pathological state, Tau is hyperphosphorylated which increases its tendency to aggregate in the cytoplasm. This means that conditions which promote abnormal...
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When proteins get out of shape

Human cells typically assemble a myriad of different proteins which constitute the work-force of the cellular environment and each of them is dedicated to a very specific function. The ability of a protein to perform its task is closely related to its structure: pockets, arms, and fingers are needed to...
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Are amyloid structures in abnormal blood clots a risk factor for amyloidosis?

Amyloidosis is the name for a group of conditions caused by a build-up of amyloid protein deposits in organs and tissues throughout the body. A great many diseases can be classified as amyloidosis. The most well known are the cerebral amyloidoses Alzheimer's and Parkinson's disease. Lesser known are the systemic...
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Phase separation and protein aggregation

Phase separation of biomolecules has recently been recognised as an important cellular process governing homogeneous organisation which is a driving force for cellular self-assembly. Multivalent interactions between biomolecules give rise to condensed phases with a spectrum of material properties from liquids to solids. The liquid-like properties (wetting, fusion, and dynamic...
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Amytracker fluorescence spectra

We named our Amytracker molecules after their peak emission wavelength when they are bound to their target. That means, when Amytracker is bound to a target, it will emit fluorescence at peak emission indicated by the number associated with its name. To view the excitation and emission spectra, please select...
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Amytracker compared to Congo Red

Amytracker fluorescence is one order of magnitude brighter than Congo Red. The affinity of Amytracker is in the nM range and thus, Amytracker is typically used at several fold lower concentrations. In a comparative study using human amyloidosis tissue, Amytracker detected amyloid deposits in 15 % of Congo Red negative...
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Does Amytracker bind unspecifically?

We tested a wide range of human tissues and didn't observe unspecific staining in most cell types. Positive Amytracker staining was obtained in Paneth cell granules in the intestine stained and the binding target in these cells is yet unclear. Due to the high sensitivity of Amytracker towards amyloids, and...
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Fixation technique for Amytracker

Generally, we recommend light fixation using ice-cold ethanol or acetone. This is because formalin-fixation has been shown to reduce the ability to stain inclusion bodies. Otherwise there shouldn't be any issues. You can use paraffin sections or cryosections. Note that epitope exposure and antigen retrieval is not needed when applying...
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Amytracker for use in various tissues and species

It is likely that Amytracker works on all kinds of tissues and species. Amytracker targets and detects the physical topography of the tertiary- and quaternary structure of mature and pre-fibrillar amyloid deposits. As such it is applicable to a wide range of animal models and different Amytracker molecules have been...
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Amytracker binding

All Amytracker molecules are designed to interact with the same binding site on the amyloid oligomer. Competition assays have shown that Amytracker competes for the congo red binding site but show much higher affinity. In essence the binding cavity and binding mode of Amytracker is is dictated by a groove...
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Amytracker for detection of Amyloidosis

Amytracker have been shown to bind with high affinity to aggregates composed of transthyretin (TTR) in Drosophila models of transthyretin amyloidosis (ATTR), as well as in human tissues The optotracers have been used to detect aggregates in following forms of human amyloid diseases: AA amyloidosis associated with accumulation of serum...
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Amytracker compared to Thioflavin

When Amytracker are not bound to a target, they exhibit an extremely low background fluorescence. Amytracker have also been shown to neither accelerate nor inhibit amyloid formation when used in recommended (substochoimetric) concentrations. Therefore, Amytracker are suitable for fibrillation assays and spectrophotometric detection. Amytracker have been shown to identify pre-fibrillar...
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How should I dilute Amytracker?

We supply Amytracker molecules with high affinity toward amyloid proteins. For staining of cryo- or paraffin sections, diluting the supplied solutions 1:1000 should be sufficient. If you want to increase the intensity, you might increase the concentration and use 1:500 dilution instead. For live cell staining, we usually recommend to...
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Amyloids - the dark matter of biology

Under some conditions, peptides or proteins may convert from their soluble forms into unsoluble highly ordered fibrillar aggregates. These aggregates may cause disease through various mechanisms. Prominent examples of aggregating peptides related to neurodegenerative diseases are Amyloid β peptides which play an important role in Alzheimer's disease and aggregating α-synuclein...
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Amytracker for amyloid staining

Amyloid detection has been notoriously difficult since current methods are either laborious, toxic and/or tend to detect mature fibrils but not protofibrils or premature aggregates. Amytracker are fluorescent tracer molecules binding to amyloids with high sensitivity. Amytracker have been shown to bind to prefibrillar states of amyloids and might therefore...
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Amytracker to investigate amyloid formation

The kinetics of amyloid formation from conformational conversion of a peptide or protein into its fibrillar form (amyloid) is studied using fibrillation assays using a spectrophotometer. This technique requires extremely low background fluorescence of the unbound probe and Thioflavin T has been widely used for this reason. The kinetic profile...
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Amytracker for superresolution microscopy

Super-resolution microscopy is becoming an important tool to study biological structures. As super-resolution techniques like STED overcome the physical diffraction limit of light, new microscopes with ever-decreasing resolution limits are being developed. Using these exciting techniques, the constraints are now imposed by the probes used for labelling. With STED microscopy,...
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Amytracker for live cell Imaging

As functional aspects of amyloids as well as the dynamic processes involving amyloid formation and amyloid toxicity are of growing interest many researchers are interested to study these processes in living cells. Non-invasive techniques like fluorescence microsopy have been perfected in recent years for the study of living cells. Unfortunately,...
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In vivo amyloid staining and intravital imaging

Intravital imaging is allowing researchers to capture images of biological processes in live animals. It has become an advanced tool to study the progression of Alzheimer's and other neurodegenerative diseases in transgenic mice. In vivo imaging using two-photon microscopy is an advantageous technique for observing tissues and organs at high...
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Testimonial - reMynd

Tom Cornelissen, PhD, reMYND Science Director Contract Research: “At reMYND's Contract Research Organization (CRO), we specialize in conducting efficacy and proof of concept studies using mouse models for Alzheimer's and Parkinson's disease. In our search for innovation, we have integrated Amytracker 520 from Ebba Biotech into our research protocols, and...
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Testimonial - Fabrizio Chiti

Prof. Fabrizio Chiti about Amytracker 630: "I like Amytracker probes because they can be used to detect amyloid-like species inside cells. We have used Amytracker 630 to exclude amyloid-like species of TDP-43 expressed in NSC34 cultured cells. We have also used cells treated with BSA and preformed Abeta fibrils as...
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Testimonial - Adam Kreutzer

Adam Kreutzer about Amytracker 680: “I have been very happy with the Amytracker dyes I have used thus far. I have easily worked the Amytracker dyes into my free-floating, fixed brain tissue immunostaining workflow. The nice thing about the Amytracker dyes is that I don’t have to dehydrate the tissue...
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Testimonial - Keiza Jack

Keiza Jack about Amytracker 540: “I have used Amytracker 540 in my PhD project as a tool to measure the structural differences of prion structures and prion-seeded amyloid fibrils. Amytracker 540 reports sensitively on subtle structural differences between protein structures, giving me a fast and reproduceable method to compare protein...
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Testimonial - Jaakko Sarparanta

Dr. Jaakko Sarparanta about Amytracker 680: ”We used Amytracker 680 to study the amyloid-like nature of pathological protein aggregates in muscle sections. The bright positive staining was easily interpreted and provided the much needed support for our Congo Red results.” Dr. Jaakko Sarparanta, Folkhälsan Research Center, Helsinki, Finland. Testimonial given...
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Testimonial - Megg Garcia

M. Garcia about Amytracker 520: "We are studying Alzheimer’s disease in mouse models and use a variety of anti-amyloid-beta antibodies and traditional dyes to look at amyloid-beta aggregation. Amytracker 520 gave a very clean staining with high signal to noise. It was easy to use as a part of routine...
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Amytracker - A New Frontier in Imaging of Amyloid Structures in Tissues

Ebba Biotech welcomes you to tune in to our webinar featuring Assistant Professor Oxana Klementieva from Lund's University. During her talk titled "Amytracker - A New Frontier in Imaging of Amyloid Structures in Tissues", Oxana Klementieva will detail her cutting-edge research into mechanisms of amyloid aggregation using novel imaging techniques....
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Amyloid fibril polymorphism in proteinopathies

Ebba Biotech's first webinar in 2023 is dedicated to "Amyloid Fibril Polymorphism" which has recently been shown to be a hallmark of many proteinopathies. One of the leading authorities in this field is Professor Per Hammarström from Linköping University. During this talk titled "Amyloid fibril polymorphism in proteinopathies", Prof. Hammarström...
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Consequences of coagulation in health and disease

Ebba Biotech welcomes you to listen to Prof. Resia Pretorius present her research findings using the Amytracker molecules. Her presentation titled “Consequences of coagulation in health and disease: The use of fluorescent markers” will detail past work with the Amytracker molecules within her group and her new exciting work with...
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Optotracers - multifunctional fluorescent tracers

On the first of June 2021, Ferdinand Choong, Ebba Biotech's co-founder, and Assistant Professor at Karolinska Institutet and AIMES (Center for the Advancement of Integrated Medical and Engineering), presented his research using Ebba Biotech's optotracers at the digital event Lab & Diagnostics of the Future 2021, held by Life Science...
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Fluorescence microscopy techniques using Amytracker-like molecules

A paper in the scientific video journal Jove (Nyström et al. (2017) Jove 128, 1–7) describes the application of Amytracker-like Molecules in combination with fluorescence microscopy techniques for detection and exploration of protein aggregates.
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Peter Nilsson develops multifunctional tools for diagnosis and therapy

Peter Nilson has been elected as future research leader from the Swedish Foundation for Strategic Research (SSF). His work about the development of multifunctional tools for diagnosis and therapy has led to the development of our Amytracker molecules.
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We named our Amytracker molecules after their peak emission wavelength when they are bound to their target. That means, when Amytracker is bound to a target, it will emit fluorescence at peak emission indicated by the number associated with its name.

To view the excitation and emission spectra, please select your Amytracker below :

Excitation (blue lines) and emission (red lines) spectra of unbound Amytracker (dotted lines) and Amytracker bound to a target (solid lines).

2024

Pinzi, Luca, Christian Conze, Nicolo Bisi, Gabriele Dalla Torre, Ahmed Soliman, Nanci Monteiro-Abreu, Nataliya I. Trushina, et al. 2024. “Quantitative Live Cell Imaging of a Tauopathy Model Enables the Identification of a Polypharmacological Drug Candidate That Restores Physiological Microtubule Interaction.” Nature Communications 15 (February): 1679. https://doi.org/10.1038/s41467-024-45851-6.

2023

Arad, Elad, Nimrod Golan, Hanna Rapaport, Meytal Landau, and Raz Jelinek. 2023. “Staphylococcus Aureus Functional Amyloids Catalyze Degradation of β-Lactam Antibiotics.” BioRxiv. https://doi.org/10.1101/2023.02.01.526669
Balana, Aaron T., Anne-Laure Mahul-Mellier, Binh A Nguyen, Mian Horvath, Afraah Javed, Eldon R. Hard, Yllza Jasiqi, et al. 2023. “O-GlcNAc Modification Forces the Formation of an α-Synuclein Amyloid-Strain with Notably Diminished Seeding Activity and Pathology.” BioRxiv, March, 2023.03.07.531573. https://doi.org/10.1101/2023.03.07.531573.
Chandhok, Sahil, Lionel Pereira, Evgenia A Momchilova, Dane Marijan, Richard Zapf, Emma Lacroix, Avneet Kaur, Shayan Keymanesh, Charles Krieger, and Timothy E Audas. 2023. “Stress-Mediated Aggregation of Disease-Associated Proteins in Amyloid Bodies.” Scientific Reports 13: 14471. https://doi.org/10.1038/s41598-023-41712-2.
Chia, Sean, Z Faidon Brotzakis, Robert I Horne, Andrea Possenti, Benedetta Mannini, Rodrigo Cataldi, Magdalena Nowinska, et al. 2023. “Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates.” Mol. Pharmaceutics 20: 183–93. https://doi.org/10.1021/acs.molpharmaceut.2c00548.
Frenkel, Alona, Eli Zecharia, Daniel Gómez-Pérez, Eleonora Sendersky, Yevgeni Yegorov, Avi Jacob, Jennifer I. C. Benichou, et al. 2023. “Cell Specialization in Cyanobacterial Biofilm Development Revealed by Expression of a Cell-Surface and Extracellular Matrix Protein.” Npj Biofilms and Microbiomes 2023 9:1 9 (March): 1–10. https://doi.org/10.1038/s41522-023-00376-6.
Gvazava, Nika, Sabine Konings, Efrain Cepeda-Prado, Valeriia Skoryk, Chimezie H Umeano, Jiao Dong, Iran A N Silva, et al. 2023. “Label-Free High-Resolution Infrared Spectroscopy for Spatiotemporal Analysis of Complex Living Systems.” BioRxiv. https://doi.org/10.1101/2023.01.05.522847.
Amaral, Mariana Juliani Do, Aline Ribeiro Passos, Satabdee Mohapatra, Taiana Sousa Lopes Da Silva, Renato Sampaio Carvalho, Marcius Da, Silva Almeida, Anderson De Sá Pinheiro, Susanne Wegmann, and Yraima Cordeiro. 2023. “Copper Drives Prion Protein Phase Separation and Modulates Aggregation.” BioRxiv. https://doi.org/10.1101/2023.02.15.528739.
Kreutzer, Adam G., Chelsea Marie T. Parrocha, Sepehr Haerianardakani, Gretchen Guaglianone, Jennifer T. Nguyen, Michelle N. Diab, William Yong, Mari Perez-Rosendahl, Elizabeth Head, and James S. Nowick. 2023. “Antibodies Raised Against an Aβ Oligomer Mimic Recognize Pathological Features in Alzheimer’s Disease and Associated Amyloid-Disease Brain Tissue.” BioRxiv, May, 2023.05.11.540404. https://doi.org/10.1101/2023.05.11.540404.
Kommaddi, Reddy Peera, Aditi Verma, Graciela Muniz-Terrera, Vivek Tiwari, Keerthana Chithanathan, Latha Diwakar, Ruturaj Gowaikar, et al. 2023. “Sex Difference in Evolution of Cognitive Decline: Studies on Mouse Model and the Dominantly Inherited Alzheimer Network Cohort.” Translational Psychiatry 13 (April): 1–12. https://doi.org/10.1038/s41398-023-02411-8.
Ornithopoulou, Eirini, Carolina Åstrand, Linnea Gustafsson, Thomas Crouzier, and My Hedhammar. 2023. “Self-Assembly of RGD-Functionalized Recombinant Spider Silk Protein into Microspheres in Physiological Buffer and in the Presence of Hyaluronic Acid.” ACS Applied Bio Materials, August. https://doi.org/10.1021/ACSABM.3C00373.
Petrlova, Jitka, Erik Hartman, Ganna Petruk, Jeremy Chun, Hwee Lim, Sunil Shankar Adav, Sven Kjellström, Manoj Puthia, and Artur Schmidtchen. 2023. “Protein Aggregation in Wound Fluid Confines Bacterial Lipopolysaccharide and Reduces in-Flammation.” BioRxiv. https://doi.org/10.1101/2023.01.27.525825.
Piroska, Leonard, Alexis Fenyi, Scott Thomas, Marie Aude Plamont, Virginie Redeker, Ronald Melki, and Zoher Gueroui. 2023. “Α-Synuclein Liquid Condensates Fuel Fibrillar α-Synuclein Growth.” Science Advances 9 (August): eadg5663. https://doi.org/10.1126/SCIADV.ADG5663.
Prater, Craig, Yeran Bai, Sabine C. Konings, Isak Martinsson, Vinay S. Swaminathan, Pontus Nordenfelt, Gunnar Gouras, Ferenc Borondics, and Oxana Klementieva. 2023. “Fluorescently Guided Optical Photothermal Infrared Microspectroscopy for Protein-Specific Bioimaging at Subcellular Level.” Journal of Medicinal Chemistry 66 (February): 2542–49. https://doi.org/10.1021/ACS.JMEDCHEM.2C01359/SUPPL_FILE/JM2C01359_SI_001.PDF.
Šulskis, Darius, and Andrius Sakalauskas. 2023. “Formation of Amyloid Fibrils by the Regulatory 14-3-3ζ Protein.” BioRxiv. https://doi.org/10.1101/2023.05.31.543065.

2022

Cascella, Roberta, Martina Banchelli, Seyyed Abolghasem Ghadami, Diletta Ami, Maria Cristina Gagliani, Alessandra Bigi, Tommaso Staderini, et al. 2022. “An in Situ and in Vitro Investigation of Cytoplasmic TDP-43 Inclusions Reveals the Absence of a Clear Amyloid Signature.” Annals of Medicine 55: 72–88. https://doi.org/10.1080/07853890.2022.2148734.
Choi, Minee L, Alexandre Chappard, Bhanu P Singh, Catherine Maclachlan, Andrey Y ✉ Abramov, Mathew H ✉ Horrocks, and Sonia ✉ Gandhi. 2022. “Pathological Structural Conversion of α-Synuclein at the Mitochondria Induces Neuronal Toxicity.” Nature Neuroscience.
Luca, Chiara Maria Giulia De, Alessandra Consonni, Federico Angelo Cazzaniga, Edoardo Bistaffa, Giuseppe Bufano, Giorgia Quitarrini, Luigi Celauro, et al. 2022. “The Alpha-Synuclein RT-QuIC Products Generated by the Olfactory Mucosa of Patients with Parkinson’s Disease and Multiple System Atrophy Induce Inflammatory Responses in SH-SY5Y Cells.” Cells 11 (January). https://doi.org/10.3390/cells11010087.
Wood, Jack I, Eugenia Wong, Damian M Cummings, John Hardy, Frances A Edwards Correspondence, Ridwaan Joghee, Aya Balbaa, et al. 2022. “Plaque Contact and Unimpaired Trem2 Is Required for the Microglial Response to Amyloid Pathology.” Cell Reports. https://doi.org/10.1016/j.celrep.2022.111686.
Pinzi, Luca, Christian Conze, Nicolo Bisi, Gabriele Dalla Torre, Nanci Monteiro-Abreu, Nataliya I Trushina, Ahmed Soliman, et al. 2022. “Quantitative Live Cell Imaging of a Tauopathy Model Enables the Identification of a Polypharmacological Drug Candidate That Restores Physiological Microtubule Regulation.” BioRxiv. https://doi.org/10.1101/2022.10.31.514565.
Petrlova, Jitka, Firdaus Samsudin, Peter J Bond, and Artur Schmidtchen. 2022. “SARS-CoV-2 Spike Protein Aggregation Is Triggered by Bacterial Lipopolysaccharide.” FEBS Letters. https://doi.org/10.1002/1873-3468.14490.
Morten, Michael J, Liina Sirvio, Huzefa Rupawala, Emma Mee Hayes, Aitor Franco, Carola Radulescu, Liming Ying, Samuel J Barnes, Arturo Muga, and Yu Ye. 2022. “Quantitative Super-Resolution Imaging of Pathological Aggregates Reveals Distinct Toxicity Profiles in Different Synucleinopathies.” PNAS. https://doi.org/10.1073/pnas.
Hochmair, Janine, Christian Exner, Maximilian Franck, Alvaro Dominguez‐Baquero, Lisa Diez, Hévila Brognaro, Matthew L Kraushar, et al. 2022. “Molecular Crowding and RNA Synergize to Promote Phase Separation, Microtubule Interaction, and Seeding of Tau Condensates.” The EMBO Journal 41 (June). https://doi.org/10.15252/EMBJ.2021108882.
Kitamura, Akira, Ai Fujimoto, Rei Kawashima, Yidan Lyu, Kanami Moriya, Ayumi Kurata, Kazuho Takahashi, et al. 2022. “Hetero-Oligomerization of TDP-43 Carboxy-Terminal Fragments with Cellular Proteins Contributes to Proteotoxicity.” BioRxiv, May. https://doi.org/10.1101/2022.05.22.493003.
Kumar, Senthil T., Anne Laure Mahul-Mellier, Ramanath Narayana Hegde, Gwladys Rivière, Rani Moons, Alain Ibáñez de Opakua, Pedro Magalhães, et al. 2022. “A NAC Domain Mutation (E83Q) Unlocks the Pathogenicity of Human Alpha-Synuclein and Recapitulates Its Pathological Diversity.” Science Advances 8 (April): 44. https://doi.org/10.1126/SCIADV.ABN0044.
Lackie, Rachel E., Aline S. de Miranda, Mei Peng Lim, Vladislav Novikov, Nimrod Madrer, Nadun C. Karunatilleke, Benjamin S. Rutledge, et al. 2022. “Stress-Inducible Phosphoprotein 1 (HOP/STI1/STIP1) Regulates the Accumulation and Toxicity of α-Synuclein in Vivo.” Acta Neuropathologica, November. https://doi.org/10.1007/s00401-022-02491-8.

2021

Aubi, Oscar, Karina S. Prestegård, Kunwar Jung-KC, Tie Jun Sten Shi, Ming Ying, Ann Kari Grindheim, Tanja Scherer, et al. 2021. “The Pah-R261Q Mouse Reveals Oxidative Stress Associated with Amyloid-Like Hepatic Aggregation of Mutant Phenylalanine Hydroxylase.” Nature Communications 2021 12:1 12 (April): 1–16. https://doi.org/10.1038/s41467-021-22107-1.
Frey, Bryan, Abdelrahman AlOkda, Matthew P. Jackson, Nathan Riguet, James A. Duce, and Hilal A. Lashuel. 2021. “Monitoring Alpha-Synuclein Oligomerization and Aggregation Using Bimolecular Fluorescence Complementation Assays: What You See Is Not Always What You Get.” Journal of Neurochemistry 157: 872–88. https://doi.org/10.1111/jnc.15147.
Frottin, Frédéric, Manuela Pérez-Berlanga, F Ulrich Hartl, and Mark S Hipp. 2021. “Multiple Pathways of Toxicity Induced by C9orf72 Dipeptide Repeat Aggregates and G4C2 RNA in a Cellular Model.” eLife 10 (June). https://doi.org/10.7554/eLife.62718.
Rimal, Suman, Yu Li, Rasika Vartak, Ji Geng, Ishaq Tantray, Shuangxi Li, Sungun Huh, et al. 2021. “Inefficient Quality Control of Ribosome Stalling During APP Synthesis Generates CAT-Tailed Species That Precipitate Hallmarks of Alzheimer’s Disease.” Acta Neuropathologica Communications 9 (December): 1–24. https://doi.org/10.1186/S40478-021-01268-6/FIGURES/7.
Hofbauer, Daniel, Dimitrios Mougiakakos, Andreas Mackensen, Stefano Ricagno, and Heiko Bruns Correspondence. 2021. “B2-Microglobulin Triggers NLRP3 Inflammasome Activation in Tumor-Associated Macrophages to Promote Multiple Myeloma Progression.” Immunity. https://doi.org/10.1016/j.immuni.2021.07.002.
Johari, Mridul, Jaakko Sarparanta, Anna Vihola, Per Harald Jonson, Marco Savarese, Manu Jokela, Annalaura Torella, et al. 2021. “Missense Mutations in Small Muscle Protein x-Linked (SMPX) Cause Distal Myopathy with Protein Inclusions.” Acta Neuropathologica. https://doi.org/10.1007/s00401-021-02319-x.

2020

Mahul-Mellier, Anne Laure, Johannes Burtscher, Niran Maharjan, Laura Weerens, Marie Croisier, Fabien Kuttler, Marion Leleu, Graham W. Knott, and Hilal A. Lashuel. 2020. “The Process of Lewy Body Formation, Rather Than Simply α-Synuclein Fibrillization, Is One of the Major Drivers of Neurodegeneration.” Proceedings of the National Academy of Sciences of the United States of America 117: 4971–82. https://doi.org/10.1073/pnas.1913904117.
Ghosh, Anshua, Keiko Mizuno, Sachin S. Tiwari, Petroula Proitsi, Beatriz Gomez Perez-Nievas, Elizabeth Glennon, Rocio T. Martinez-Nunez, and K. Peter Giese. 2020. “Alzheimer’s Disease-Related Dysregulation of mRNA Translation Causes Key Pathological Features with Ageing.” Translational Psychiatry 10: 1–18. https://doi.org/10.1038/s41398-020-00882-7.
Louros, Nikolaos, Gabriele Orlando, Matthias De Vleeschouwer, Frederic Rousseau, and Joost Schymkowitz. 2020. “Structure-Based Machine-Guided Mapping of Amyloid Sequence Space Reveals Uncharted Sequence Clusters with Higher Solubilities.” Nature Communications 11: 1–13. https://doi.org/10.1038/s41467-020-17207-3.

2019

Page, Martin J., Greig J. A. Thomson, J. Massimo Nunes, Anna Mart Engelbrecht, Theo A. Nell, Willem J. S. de Villiers, Maria C. de Beer, Lize Engelbrecht, Douglas B. Kell, and Etheresia Pretorius. 2019. “Serum Amyloid a Binds to Fibrin(ogen), Promoting Fibrin Amyloid Formation.” Scientific Reports 9: 1–14. https://doi.org/10.1038/s41598-019-39056-x.
Adams, Büin, J. Massimo Nunes, Martin J. Page, Timothy Roberts, Jonathan Carr, Theo A. Nell, Douglas B. Kell, and Etheresia Pretorius. 2019. “Parkinson’s Disease: A Systemic Inflammatory Disease Accompanied by Bacterial Inflammagens.” Frontiers in Aging Neuroscience 10: 1–17. https://doi.org/10.3389/fnagi.2019.00210.
Frottin, F., F. Schueder, S. Tiwary, R. Gupta, R. Körner, T. Schlichthaerle, J. Cox, R. Jungmann, F. U. Hartl, and M. S. Hipp. 2019. “The Nucleolus Functions as a Phase-Separated Protein Quality Control Compartment.” Science 365: 342–47. https://doi.org/10.1126/science.aaw9157.

2018

Waal, Greta M. de, Lize Engelbrecht, Tanja Davis, Willem J. S. de Villiers, Douglas B. Kell, and Etheresia Pretorius. 2018. “Correlative Light-Electron Microscopy Detects Lipopolysaccharide and Its Association with Fibrin Fibres in Parkinson’s Disease, Alzheimer’s Disease and Type 2 Diabetes Mellitus.” Scientific Reports 8: 1–12. https://doi.org/10.1038/s41598-018-35009-y.
Pretorius, Etheresia, Martin J. Page, Lisa Hendricks, Nondumiso B. Nkosi, Sven R. Benson, and Douglas B. Kell. 2018. “Both Lipopolysaccharide and Lipoteichoic Acids Potently Induce Anomalous Fibrin Amyloid Formation: Assessment with Novel Amytracker TM Stains.” Journal of the Royal Society Interface 15. https://doi.org/10.1098/rsif.2017.0941.

2017

Sehlin, Dag, Xiaotian T. Fang, Silvio R. Meier, Malin Jansson, and Stina Syvänen. 2017. “Pharmacokinetics, Biodistribution and Brain Retention of a Bispecific Antibody-Based PET Radioligand for Imaging of Amyloid-β.” Scientific Reports 7: 1–9. https://doi.org/10.1038/s41598-017-17358-2.
Pretorius, Etheresia, Martin J. Page, Lize Engelbrecht, Graham C. Ellis, and Douglas B. Kell. 2017. “Substantial Fibrin Amyloidogenesis in Type 2 Diabetes Assessed Using Amyloid-Selective Fluorescent Stains.” Cardiovascular Diabetology 16: 1–14. https://doi.org/10.1186/s12933-017-0624-5.