Creative Biolabs

Stress Granule Formation Assay

Creative Biolabs is a well-deserved expert neuroscience research service provider with years of project experience. Based on a comprehensive technology platform and professional specialists, we are devoted to offering customer-satisfied one-stop stress granule formation assays.

Overview of Amyotrophic Lateral Sclerosis (ALS)

Neurodegenerative disorders like frontotemporal dementia (FTD) and ALS are pathologically characterized by toxic protein deposition in the cytoplasm of affected neurons. Many of these aggregated proteins belong to the class of RNA binding proteins (RBP), and mutated forms of which account for a significant subset of familial ALS cases. ALS is a fatal neurodegenerative disorder characterized by the loss of upper and lower motor neurons in ALS. In ALS, classic familial inheritance is only observed in 5-10% of the cases (both dominant and recessive), with mutations in the superoxide dismutase 1 (SOD1) gene and C9orf72 being the major causes.

Mutations in stress granule (SG)-related RBPs associated with the FTD-ALS spectrum.Fig. 1. Mutations in stress granule (SG)-related RBPs associated with the FTD-ALS spectrum. (Baradaran-Heravi, et al., 2020)

Stress Granule Formation in ALS

Mutations in a series of RBP genes (TDP-43, FUS, TAF15, EWSR1, hnRNPA1, hnRNPA2B1, ATXN2, TIA1) have been identified to cause or influence disease risk for ALS and/or FTD. RBPs bind to RNAs to form heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and thereby control RNA processing and metabolism (i.e., transcription, RNA splicing, nuclear export, mRNA transport, translation, sequestration, and degradation). The majority of neurodegeneration-related RBPs harbor a conserved low complexity domain (LCD), also called the prion-like domain. The LCD is the key component that drives (liquid-liquid) phase separation (LLPS) and thereby mediates stress granule (SG) formation.

SGs are cytoplasmic RNP granules composed of repressed translational complexes and are generated upon cellular stress resulting in dynamic membrane-less compartments. SGs allow the cell to cope with stress by stalling mRNA translation and moving synthesis towards cytoprotective proteins. They are intrinsically dynamic and dissolve again as the stress passes. SGs have become prime suspects in the nucleation of toxic protein aggregation in FTD and ALS. Most of the disease-causing mutations map to the LCD regions of SG-related RBPs and disrupt their biophysical properties, leading to increased LLPS into SGs and aggregate formation. SGs formed by these FTD-ALS-linked mutant RBPs are impaired in their dynamics and remain insoluble, further trapping wild-type RBPs and leading to irreversible, toxic aggregates.

Stress granule (SG) mediated protein aggregation pathways under physiological conditions and disease.Fig. 2. Stress granule (SG) mediated protein aggregation pathways under physiological conditions and disease. (Baradaran-Heravi, et al., 2020)

Stress Granule Formation Assays at Creative Biolabs

With years of experience focusing on neuroscience research, Creative Biolabs provides comprehensive in vitro ALS assays including stress granule formation assay services. After years of investment, our platform equipped with state-of-the-art facilities, advanced technologies, and professional specialists is capable of offering customer-satisfied neuroscience research services.

If you are focusing on granule formation assay or any other neuroscience research services on the website, please don't hesitate to contact us for more information.


  1. Baradaran-Heravi, Y.; et al. Stress granule mediated protein aggregation and underlying gene defects in the FTD-ALS spectrum. Neurobiol Dis. 2020, 134: 104639.
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