Biomarker Analysis Services for Amyotrophic Lateral Sclerosis
At Protheragen, we offer specialized biomarker analysis services tailored exclusively for Amyotrophic Lateral Sclerosis (ALS) research and drug discovery. Our comprehensive biomarker panel is designed to support preclinical therapeutic development by enabling a deeper understanding of ALS pathophysiology and molecular mechanisms. Please note that all services are strictly dedicated to drug discovery and preclinical development; we do not provide clinical diagnostic services.
Effective therapeutic intervention in ALS begins with the precise discovery and identification of relevant biomarkers. Protheragen's biomarker discovery services are integral to the drug development process, providing the foundation for target selection, mechanism elucidation, and efficacy assessment. Our approach encompasses high-throughput screening of candidate markers, followed by robust validation workflows to ensure the reliability and reproducibility of findings. This systematic process supports informed decision-making in early-stage drug development.
Multi Omics: Leveraging cutting-edge -omics technologies—including genomics, transcriptomics, proteomics, and metabolomics—Protheragen conducts comprehensive studies of biological systems implicated in ALS. Our integrated multi-omics platform enables the identification of DNA, RNA, protein, and metabolite biomarkers, facilitating a holistic view of disease-relevant pathways such as autophagy, RNA metabolism, protein aggregation, oxidative stress, and neuroinflammation. This approach provides critical insights into the complex molecular landscape of ALS.
Candidate Validation: We employ rigorous validation strategies to establish the relevance of candidate biomarkers to ALS pathophysiology. Our process includes preliminary screening using high-sensitivity assays, association studies with disease mechanisms, and evaluation of biomarker specificity and reproducibility. Promising candidates are prioritized based on criteria such as biological plausibility, technical performance, and alignment with ALS disease mechanisms, ensuring a focused and scientifically robust preclinical pipeline.
Diverse Technological Platforms: Protheragen offers custom assay development across a diverse suite of technological platforms, enabling adaptation to specific biomarker requirements. Our capabilities include immunoassays, mass spectrometry, flow cytometry, molecular diagnostics, and advanced histopathology and imaging platforms. Each platform is optimized for sensitivity, throughput, and compatibility with various sample types, supporting flexible and precise biomarker quantification.
Immunoassays: We develop and optimize enzyme-linked immunosorbent assays (ELISA), chemiluminescent immunoassays, and multiplex bead-based immunoassays for quantitative and qualitative detection of protein biomarkers relevant to ALS.
Mass Spectrometry: Our LC-MS/MS workflows provide high-sensitivity, high-specificity quantification of peptides and proteins, supporting both targeted and discovery-based biomarker analysis.
Flow Cytometry: We utilize multiparametric flow cytometry for the detection and quantification of cellular biomarkers, including protein expression and cell population profiling.
Molecular Diagnostics: We offer nucleic acid-based assays for the detection of genetic variants, repeat expansions, and gene expression changes associated with ALS.
Histopathology And Imaging: Our histopathological and advanced imaging methods enable spatial localization and visualization of biomarker distribution in tissue samples.
Rigorous Method Validation: All analytical methods undergo rigorous validation according to current regulatory and scientific guidelines. We assess performance characteristics such as sensitivity, specificity, linearity, accuracy, precision, and reproducibility. Comprehensive quality control measures—including the use of reference materials and standardized protocols—are implemented to ensure the reliability of assay results throughout the preclinical research process.
Protheragen delivers quantitative biomarker analysis using validated, state-of-the-art technologies. Our capabilities enable precise measurement of biomarker concentrations, dynamic range assessment, and longitudinal monitoring of biomarker changes in response to therapeutic interventions. Data integrity and reproducibility are maintained through stringent quality management systems.
Sample Analysis: We handle a variety of preclinical sample types, including tissue lysates, cell cultures, biofluids (such as serum, plasma, and cerebrospinal fluid), and model organism samples. Standardized sample processing and analysis protocols are employed to ensure consistency and minimize preanalytical variability. Each step is subject to rigorous quality assurance measures to safeguard data quality and interpretability.
High Throughput Capabilities: Our high-throughput analytical platforms support multiplexed biomarker analysis, enabling simultaneous quantification of multiple targets from limited sample volumes. This approach increases efficiency, conserves valuable samples, and accelerates data generation—facilitating rapid, large-scale preclinical studies for ALS biomarker research.
| Gene Target | Biological Function | Application as a Biomarker |
|---|---|---|
| C9orf72-SMCR8 complex subunit (C9orf72) | C9orf72 (chromosome 9 open reading frame 72) encodes a protein that forms a heterotrimeric complex with SMCR8 and WDR41. This complex is involved in the regulation of autophagy and lysosomal homeostasis. Specifically, C9orf72-SMCR8 functions as a guanine nucleotide exchange factor (GEF) for Rab GTPases, which are key regulators of vesicular trafficking. The complex has been implicated in the control of endosomal trafficking, autophagosome maturation, and response to cellular stress. Loss of function or hexanucleotide repeat expansions in C9orf72 are associated with neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), highlighting its role in neuronal health and maintenance. | Repeat expansions in the C9orf72 gene, particularly the GGGGCC (G4C2) hexanucleotide repeat in the non-coding region, are used as a genetic biomarker in the diagnosis of familial and sporadic cases of ALS and FTD. Genetic testing for C9orf72 repeat expansion is routinely performed to identify affected individuals and to help differentiate ALS/FTD from other neurodegenerative disorders. Additionally, the presence of C9orf72 repeat expansions has been correlated with specific clinical features and disease progression in ALS and FTD. |
| FUS RNA binding protein (FUS) | FUS RNA binding protein (FUS) is a multifunctional protein involved in various aspects of RNA metabolism. It is a member of the FET (FUS, EWS, TAF15) family of RNA-binding proteins. FUS participates in transcriptional regulation, RNA splicing, mRNA transport, and DNA repair. It contains RNA recognition motifs and a prion-like domain, facilitating its interaction with RNA and other proteins. FUS is predominantly localized in the nucleus but can shuttle between the nucleus and cytoplasm. Its role is critical in maintaining genomic stability and regulating gene expression, particularly in neuronal cells. | FUS has been studied as a biomarker in neurodegenerative diseases, especially amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Mutations in the FUS gene and abnormal cytoplasmic accumulation of FUS protein have been observed in subsets of ALS and FTLD cases. Immunohistochemical detection of FUS-positive inclusions in neuronal tissues can aid in the pathological classification of these disorders. Additionally, FUS expression and localization patterns are investigated in research settings to distinguish between different subtypes of neurodegenerative diseases. |
| TAR DNA binding protein (TARDBP) | TAR DNA binding protein (TARDBP) encodes the protein TDP-43, which is a ubiquitously expressed, highly conserved RNA- and DNA-binding protein. TDP-43 is primarily localized in the nucleus, where it plays critical roles in the regulation of gene expression, including transcriptional repression, alternative splicing, mRNA stability, and transport. It binds to UG-rich RNA sequences and is involved in RNA processing events such as pre-mRNA splicing and microRNA biogenesis. TDP-43 also shuttles between the nucleus and cytoplasm and participates in the formation of ribonucleoprotein complexes, contributing to RNA metabolism and neuronal function. | TDP-43 has been identified as a pathological hallmark in several neurodegenerative diseases, most notably amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). In these conditions, TDP-43 is often found abnormally phosphorylated, ubiquitinated, and mislocalized from the nucleus to the cytoplasm, where it forms insoluble aggregates. Detection of TDP-43 pathology in neural tissue is used as an indicator of disease presence and subtype differentiation in ALS and FTLD. Additionally, TDP-43 levels and its pathological forms are investigated in cerebrospinal fluid and blood as potential biomarkers for diagnosis, disease progression, and prognosis in neurodegenerative disorders. |
| ataxin 2 (ATXN2) | Ataxin 2 (ATXN2) is a protein encoded by the ATXN2 gene and is primarily involved in RNA metabolism. It contains domains that facilitate interactions with RNA and proteins, including an Lsm (Like-Sm) domain and polyglutamine (polyQ) tract. ATXN2 has roles in the regulation of mRNA stability, translation, and polyadenylation. It is localized to the cytoplasm and associates with stress granules, which are involved in cellular responses to stress. Additionally, ATXN2 has been implicated in endocytosis and the regulation of energy homeostasis. Expansion of the CAG repeat in the ATXN2 gene leads to an abnormally long polyQ tract in the protein, which is associated with neurodegenerative disorders such as spinocerebellar ataxia type 2 (SCA2). | ATXN2 is utilized in research and clinical contexts as a biomarker for neurodegenerative diseases, particularly spinocerebellar ataxia type 2 (SCA2). The number of CAG repeats in the ATXN2 gene is measured to assist in the diagnosis and genetic characterization of SCA2. Intermediate-length CAG expansions in ATXN2 have also been associated with an increased risk for amyotrophic lateral sclerosis (ALS), and ATXN2 repeat length is studied as a potential risk modifier in ALS and other neurodegenerative conditions. |
| interleukin 6 (IL6) | Interleukin 6 (IL6) is a pleiotropic cytokine produced by a variety of cell types, including macrophages, T cells, B cells, fibroblasts, endothelial cells, and others, in response to infections, tissue injury, and other inflammatory stimuli. IL6 plays a central role in the regulation of immune responses, acute phase reactions, hematopoiesis, and inflammation. It acts by binding to its receptor complex (IL6R and gp130), activating intracellular signaling pathways such as the JAK/STAT pathway. IL6 stimulates the production of acute phase proteins in the liver, promotes differentiation of B cells into antibody-secreting plasma cells, influences T cell differentiation, and modulates the activity of various immune and non-immune cells. | IL6 is measured in biological fluids, such as serum or plasma, to assess the presence and magnitude of inflammation. Elevated IL6 concentrations have been observed in a range of conditions, including infections, autoimmune disorders, sepsis, and certain malignancies. Its levels are commonly used as an indicator of systemic inflammatory response and are associated with disease activity or severity in various clinical contexts. |
| microtubule associated protein tau (MAPT) | Microtubule associated protein tau (MAPT) encodes the tau protein, which is primarily expressed in neurons of the central nervous system. Tau is a microtubule-associated protein that stabilizes microtubules, which are essential components of the neuronal cytoskeleton. By binding to microtubules, tau promotes their assembly and maintains their structural integrity, thereby supporting axonal transport and neuronal morphology. Tau undergoes various post-translational modifications, including phosphorylation, which can influence its binding affinity to microtubules and its functional properties. | MAPT and its protein product, tau, are utilized as biomarkers in the context of neurodegenerative diseases, particularly Alzheimer's disease and other tauopathies. Elevated levels of total tau and phosphorylated tau in cerebrospinal fluid (CSF) are associated with neuronal injury and tau pathology. Measurement of these tau species in CSF, and more recently in blood, is applied in research and clinical settings to support the diagnosis, prognosis, and monitoring of disease progression in Alzheimer's disease and related disorders. |
| sequestosome 1 (SQSTM1) | Sequestosome 1 (SQSTM1), also known as p62, is a multifunctional adaptor protein involved in several cellular processes, including autophagy, signal transduction, and protein degradation. SQSTM1 acts as a selective autophagy receptor by binding ubiquitinated proteins through its ubiquitin-associated (UBA) domain and interacting with the autophagy protein LC3 via its LC3-interacting region (LIR). This facilitates the delivery of ubiquitinated cargo to the autophagosome for degradation. SQSTM1 also participates in signaling pathways such as NF-κB activation by interacting with various signaling intermediates. Additionally, SQSTM1 is implicated in oxidative stress response, apoptosis regulation, and bone metabolism. | SQSTM1 has been studied as a biomarker in several contexts. Accumulation of SQSTM1 is commonly used as an indicator of impaired autophagic flux in cells and tissues. Elevated levels of SQSTM1 have been reported in neurodegenerative diseases, certain cancers, and liver diseases, reflecting alterations in autophagy or proteostasis. In bone disorders such as Paget's disease of bone, mutations in the SQSTM1 gene are associated with disease pathogenesis and have been investigated in genetic testing. Immunohistochemical detection of SQSTM1 in tissue samples is also utilized in research to assess autophagy status. |
| superoxide dismutase 1 (SOD1) | Superoxide dismutase 1 (SOD1) is an antioxidant enzyme that catalyzes the dismutation of superoxide radicals (O2•−) into molecular oxygen (O2) and hydrogen peroxide (H2O2). This reaction is a critical component of cellular defense against oxidative stress, as superoxide radicals are reactive oxygen species that can damage cellular components such as DNA, proteins, and lipids. SOD1 is primarily localized in the cytoplasm but is also found in the mitochondrial intermembrane space. By controlling superoxide levels, SOD1 plays an essential role in maintaining redox homeostasis and protecting cells from oxidative injury. | Alterations in SOD1 expression, activity, or mutation status have been investigated as biomarkers in several contexts. Most notably, mutations in the SOD1 gene are associated with familial forms of amyotrophic lateral sclerosis (ALS), and SOD1 protein levels or activity may be measured in blood, cerebrospinal fluid, or tissues in research and diagnostic settings related to ALS. Changes in SOD1 activity or expression have also been studied as indicators of oxidative stress in various diseases, including neurodegenerative disorders, cardiovascular diseases, and certain cancers. Thus, SOD1 has been used as a marker to assess oxidative stress status and to investigate disease mechanisms in clinical and experimental research. |
| valosin containing protein (VCP) | Valosin containing protein (VCP), also known as p97, is a highly conserved and ubiquitously expressed member of the AAA+ (ATPases Associated with diverse cellular Activities) family of ATPases. VCP plays a central role in various cellular processes, including protein homeostasis, endoplasmic reticulum-associated degradation (ERAD), ubiquitin-dependent protein degradation, membrane fusion, and cell cycle regulation. It functions as a molecular chaperone, facilitating the extraction of ubiquitinated proteins from cellular structures such as the endoplasmic reticulum membrane, thereby targeting them for degradation by the proteasome. VCP is also involved in autophagy, DNA damage response, and the regulation of organelle biogenesis. Mutations in VCP have been associated with multisystem proteinopathy, inclusion body myopathy, Paget disease of bone, and frontotemporal dementia. | VCP has been investigated as a biomarker in several contexts. Altered expression levels of VCP have been observed in various malignancies, including colorectal, breast, and hepatocellular carcinomas, where its upregulation has been associated with tumor progression and prognosis. In neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia, mutations in the VCP gene are used as molecular markers for disease subtypes. Additionally, VCP protein levels and activity have been studied in the context of protein aggregation disorders and muscle diseases, supporting its utility in research and potential clinical applications. |
| vascular endothelial growth factor A (VEGFA) | Vascular endothelial growth factor A (VEGFA) is a key signaling protein involved in the regulation of angiogenesis, the process by which new blood vessels form from pre-existing vasculature. VEGFA primarily acts by binding to its receptors (VEGFR-1 and VEGFR-2) on endothelial cells, stimulating their proliferation, migration, and survival. This activity is critical for normal physiological processes such as embryonic development, wound healing, and the menstrual cycle. Additionally, VEGFA increases vascular permeability and plays a role in the maintenance of the vascular system. | VEGFA has been utilized as a biomarker in various clinical and research settings due to its involvement in pathological angiogenesis. Elevated levels of VEGFA have been observed in several cancers, including colorectal, breast, and lung cancers, and are associated with tumor growth and metastasis. It has also been measured in ocular diseases such as age-related macular degeneration and diabetic retinopathy, where abnormal blood vessel formation is a hallmark. In these contexts, VEGFA levels in tissue, serum, or plasma are used to assess disease presence, progression, or response to anti-angiogenic therapies. |
Explore Research Opportunities with Protheragen. Our biomarker research services offer comprehensive, exploratory solutions for Amyotrophic Lateral Sclerosis, supporting preclinical drug discovery and mechanistic studies. The biomarkers discussed herein are research targets only and are not claimed as validated or mandatory for any application. Our expertise spans advanced analytical platforms and multi-omics approaches, all focused on the early, preclinical stages of ALS research. Protheragen maintains scientific objectivity and does not assert any biomarker as definitive or required.
We invite you to connect with Protheragen to discuss collaborative opportunities in ALS biomarker research. Our focus is on scientific exploration, knowledge exchange, and advancing understanding through preclinical research—without making claims about biomarker validation or necessity. Let’s work together to drive innovation in ALS research.
Make Order
Experimental Scheme
Implementation
Conclusion
