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ALS Therapeutic Target Characterization Assay

Creative Biolabs offers comprehensive service that encompasses an array of aspects, from identifying potential therapeutic targets to elucidating cellular processes implicated in Amyotrophic Lateral Sclerosis (ALS) pathogenesis.

Highlighted ALS Therapeutic Targets

Creative Biolabs provides an extensive array of characterization assays targeting ALS-associated genes, aiming to address diverse facets of ALS pathogenesis. The following is a compilation of gene targets currently under investigation for potential ALS therapeutic interventions:

  • C9orf72
  • SOD1
  • FUS
  • TARDBP (TDP-43)
  • Ataxin-2 (ATXN2)
  • TBK1
  • VCP
  • PFN1
  • OPTN
  • MATR3
  • UNC13A

Target Characterization Assays at Creative Biolabs

Some of ALS targets undergo various post-translational modifications, including phosphorylation, ubiquitination, and cleavage.

Abnormal modifications can lead to aggregation into insoluble protein aggregates, a hallmark of ALS and FTLD pathology.

In ALS and FTLD, protein aggregates are commonly found in the cytoplasm of affected neurons. Aggregated proteins are often hyperphosphorylated and ubiquitinated, contributing to their misfolding and accumulation.

Proteins are normally localized in the nucleus, where they participate in RNA-related processes. In ALS disease, these proteins can translocate to the cytoplasm and form pathological aggregates. We provide nucleo-cytoplasmic transport assay and mislocalization assay to confirm the localization of specific proteins.

Most ALS targets bind to RNA and regulate the splicing patterns of various genes. Dysregulation of RNA processing due to gene dysfunction can contribute to neurodegenerative processes.

Stress granules are cellular structures that form in response to various stressors, such as oxidative stress or cellular damage, and are implicated in ALS and other neurodegenerative diseases.

Highlighted Targets Characterization

Characterizing the proteins associated with ALS is crucial for understanding the molecular mechanisms underlying the disease. Here's a brief overview of our protein characterization for some key ALS-associated genes:

Target Introduction Characterization Assays
SOD1 SOD1 encodes a cytoplasmic antioxidant enzyme involved in protecting cells from oxidative stress.
  • Mutant forms of SOD1 are known to misfold and aggregate, contributing to ALS pathology.
  • Aggregated SOD1 can be detected using immunohistochemistry, immunofluorescence, and biochemical assays.
  • Studies focus on understanding how SOD1 mutations lead to toxicity, oxidative damage, and disruption of cellular processes.
C9orf72 C9orf72 mutations involve a hexanucleotide repeat expansion in an intronic region, leading to RNA toxicity and protein aggregation.
  • The research investigates the generation and aggregation of dipeptide repeat proteins (DPRs) translated from the expanded repeats.
  • Immunohistochemistry and immunofluorescence can detect aggregates of DPRs in affected tissues and cells.
  • Protein-protein interaction assays help identify interactions between DPRs and other cellular components.
TDP-43 TDP-43 is an RNA-binding protein that plays a role in RNA metabolism and is associated with ALS and Frontotemporal Dementia (FTD).
  • Immunohistochemistry and immunofluorescence detect abnormal localization and aggregation of TDP-43 in ALS-affected neurons.
  • Biochemical assays analyze TDP-43 post-translational modifications and interactions with other proteins.
  • RNA binding assays explore how TDP-43 mutations affect RNA processing and splicing.
FUS FUS is another RNA-binding protein associated with ALS and forms pathological cytoplasmic inclusions.
  • Similar to TDP-43, FUS is analyzed using immunohistochemistry, immunofluorescence, and biochemical assays for aggregation and localization.
  • Functional assays examine the impact of FUS mutations on RNA metabolism and cellular processes.
Optineurin (OPTN) and UBQLN2 Mutations in these genes are linked to familial ALS
  • Research focuses on understanding how mutant optineurin and UBQLN2 lead to protein aggregation and impairment of protein degradation pathways.
  • Immunohistochemistry, immunofluorescence, and biochemical assays are used to study protein aggregation and localization.
PFN1 Mutations in PFN1 have been associated with ALS.
  • Studies investigate the effects of mutant PFN1 on cytoskeletal dynamics and cellular function.
  • Protein-protein interaction assays explore how mutant proteins interact with other cellular components.

For inquiries and collaborations, please don't hesitate to contact us for more information.

For Research Use Only. Not For Clinical Use.
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