Biomarker Analysis Services for Spinal Muscular Atrophy
At Protheragen, we offer specialized biomarker analysis services tailored exclusively for Spinal Muscular Atrophy (SMA) research and therapeutic development. Our comprehensive biomarker panel is designed to advance the understanding of SMA pathophysiology and accelerate drug discovery through preclinical development stages. Please note that all of our services are strictly dedicated to research applications and drug discovery; we do not provide clinical diagnostic services.
The foundation of effective therapeutic intervention lies in the identification of robust, disease-relevant biomarkers. Protheragen’s biomarker discovery services are integral to the preclinical drug development pipeline, enabling the systematic identification of molecular signatures associated with SMA. Our approach encompasses high-throughput screening of candidate biomarkers, rigorous validation in relevant biological models, and the integration of multi-dimensional data to prioritize targets for further investigation. Through these processes, we support the elucidation of disease mechanisms and facilitate the selection of promising therapeutic strategies.
Multi Omics: Leveraging cutting-edge -omics technologies—including genomics, transcriptomics, and proteomics—Protheragen enables the comprehensive study of biological systems involved in Spinal Muscular Atrophy. Our multi-omics approach allows for the identification and characterization of DNA, RNA, protein, and metabolite biomarkers that reflect the complexity of SMA pathogenesis. By interrogating relevant disease pathways such as SMN protein biogenesis, pre-mRNA splicing, and motor neuron survival, we provide a holistic perspective on molecular alterations and potential therapeutic targets in SMA.
Candidate Validation: Our candidate validation and prioritization strategies employ a combination of experimental and computational methods to confirm biomarker relevance to Spinal Muscular Atrophy pathophysiology. We conduct preliminary screening in disease-relevant models, assess biomarker associations with molecular and cellular phenotypes, and apply stringent criteria—such as specificity, reproducibility, and biological plausibility—to select the most promising candidates for further development. This process ensures that only the most informative biomarkers advance to subsequent stages of assay development.
Diverse Technological Platforms: Protheragen offers custom assay development capabilities across a spectrum of technological platforms, each adaptable to specific research requirements in SMA. Our portfolio includes immunoassays, mass spectrometry, flow cytometry, molecular diagnostics, and histopathology/imaging platforms. We tailor each platform to accommodate unique analytical needs, sample types, and throughput demands, ensuring optimal performance and data quality.
Immunoassays: We develop and optimize enzyme-linked immunosorbent assays (ELISA), chemiluminescent immunoassays, and multiplex immunoassay formats for quantitative and qualitative biomarker detection.
Mass Spectrometry: Our LC-MS/MS platforms enable high-sensitivity, high-specificity quantification of proteins and peptides relevant to SMA research.
Flow Cytometry: We utilize advanced flow cytometry for the analysis of cell surface and intracellular biomarkers, enabling multiparametric assessment of cellular phenotypes.
Molecular Diagnostics: Techniques such as quantitative PCR and digital PCR are applied for the detection and quantification of gene copy number variations, mutations, and transcript levels.
Histopathology And Imaging: We employ immunohistochemistry, in situ hybridization, and advanced imaging modalities to localize and quantify biomarkers within tissue contexts.
Rigorous Method Validation: All analytical methods undergo rigorous validation in accordance with established research guidelines. We assess method performance characteristics including sensitivity, specificity, accuracy, precision, linearity, and reproducibility. Comprehensive quality control measures are implemented throughout the validation process to ensure data integrity and reliability for preclinical research applications.
Our quantitative analysis capabilities encompass the precise measurement of biomarker levels in a variety of sample matrices. Utilizing validated analytical platforms, we deliver robust, reproducible, and sensitive quantification to support biomarker-driven research in SMA.
Sample Analysis: Protheragen processes a diverse range of sample types—including cell lysates, tissue homogenates, blood, and biofluids—using standardized protocols optimized for each matrix. All analyses are conducted under stringent quality control procedures to ensure consistency, accuracy, and reproducibility of results.
High Throughput Capabilities: Our high-throughput analytical platforms enable the simultaneous analysis of multiple biomarkers across large sample cohorts. Multiplexed assay formats increase efficiency, conserve valuable samples, and accelerate data generation, thereby supporting rapid iteration in biomarker research and preclinical studies.
| Gene Target | Biological Function | Application as a Biomarker |
|---|---|---|
| BCL2 apoptosis regulator (BCL2) | BCL2 (B-cell lymphoma 2) is an integral membrane protein located primarily on the outer mitochondrial membrane. It functions as a key regulator of the intrinsic (mitochondrial) pathway of apoptosis. BCL2 inhibits apoptosis by preventing the release of cytochrome c and other pro-apoptotic factors from mitochondria, thereby blocking the activation of downstream caspases. It achieves this function through interactions with other members of the BCL2 family, including both pro-apoptotic (e.g., BAX, BAK) and anti-apoptotic proteins, thereby maintaining cellular homeostasis and promoting cell survival under physiological conditions. | BCL2 is utilized as a biomarker in several clinical and research contexts, particularly in hematological malignancies such as follicular lymphoma, diffuse large B-cell lymphoma, and chronic lymphocytic leukemia. Its expression levels, typically assessed by immunohistochemistry, can aid in the diagnosis, classification, and prognosis of certain lymphomas. In some cancers, overexpression of BCL2 is associated with resistance to apoptosis and may correlate with treatment response or disease progression. BCL2 status is also considered in the context of targeted therapies that inhibit its function. |
| VRK serine/threonine kinase 1 (VRK1) | VRK serine/threonine kinase 1 (VRK1) is a member of the vaccinia-related kinase family of serine/threonine protein kinases. VRK1 is predominantly localized in the nucleus and is involved in a variety of cellular processes, including cell cycle regulation, chromatin remodeling, and DNA damage response. It phosphorylates several substrates, such as histone H3, p53, and barrier-to-autointegration factor (BAF), thereby influencing gene expression, mitotic progression, and nuclear envelope dynamics. VRK1 activity has been linked to cell proliferation and has a role in the regulation of G1/S and G2/M cell cycle transitions. | VRK1 expression has been studied in the context of various cancers and proliferative disorders. Increased VRK1 levels have been observed in several tumor types, including breast, lung, and liver cancers, where its expression correlates with higher proliferative activity. As such, VRK1 has been investigated as a potential biomarker for tumor cell proliferation and disease prognosis. Its expression patterns may also be useful in distinguishing between malignant and non-malignant tissues in certain contexts. |
| acylaminoacyl-peptide hydrolase (APEH) | Acylaminoacyl-peptide hydrolase (APEH) is a serine protease enzyme involved in the degradation of N-acylated peptides. It catalyzes the removal of N-acylated amino acids from the N-terminus of oligopeptides, thereby facilitating further degradation by other peptidases. APEH is ubiquitously expressed in human tissues and is implicated in the regulation of protein turnover and the removal of potentially toxic N-acylated peptides that can accumulate during cellular metabolism. The enzyme plays a role in maintaining cellular protein homeostasis and may contribute to the degradation of oxidatively damaged proteins. | APEH activity and expression levels have been investigated in the context of various diseases, including cancer and neurodegenerative disorders. Altered APEH expression has been reported in certain tumor tissues and in conditions associated with oxidative stress. For example, studies have examined APEH as a potential marker for oxidative damage in Alzheimer's disease and as a candidate for distinguishing cancerous from non-cancerous tissues. In these applications, APEH is typically assessed in tissue samples, blood, or cerebrospinal fluid to explore its association with disease states. |
| amyloid beta precursor protein (APP) | Amyloid beta precursor protein (APP) is a transmembrane glycoprotein expressed in many tissues, with particularly high levels in the central nervous system. APP undergoes proteolytic processing via two main pathways: the non-amyloidogenic pathway, resulting in the production of soluble APP fragments with neuroprotective roles, and the amyloidogenic pathway, which generates amyloid-beta (Aβ) peptides. These Aβ peptides are produced through sequential cleavage by beta- and gamma-secretases. While the precise physiological functions of APP remain under investigation, established roles include involvement in neuronal growth, synaptic formation and repair, cell adhesion, and intracellular signaling. | APP and its proteolytic fragments, particularly amyloid-beta peptides derived from APP processing, have been widely studied as biomarkers in neurodegenerative diseases, most notably Alzheimer's disease. Quantification of amyloid-beta peptides (such as Aβ42 and Aβ40) in cerebrospinal fluid and imaging of amyloid deposition in the brain are used in research and clinical settings to assess amyloid pathology. Alterations in APP processing and the resulting changes in amyloid-beta levels are associated with disease progression and are used to support diagnosis and monitor response to therapeutic interventions. |
| chloride voltage-gated channel 1 (CLCN1) | Chloride voltage-gated channel 1 (CLCN1) encodes a protein that forms the major chloride channel in the skeletal muscle cell membrane. This channel is responsible for the passive flow of chloride ions across the sarcolemma, which plays a crucial role in stabilizing the resting membrane potential and controlling muscle excitability. The proper function of CLCN1 channels helps to terminate muscle contraction and prevent hyperexcitability after action potentials. Mutations in CLCN1 are associated with altered channel function, leading to conditions such as myotonia congenita, characterized by delayed muscle relaxation. | CLCN1 has been utilized as a genetic marker in the diagnosis of myotonia congenita, both in autosomal dominant (Thomsen disease) and autosomal recessive (Becker disease) forms. Genetic analysis of the CLCN1 gene is employed to confirm clinical suspicion of these channelopathies and to differentiate them from other neuromuscular disorders with similar presentations. Detection of pathogenic variants in CLCN1 can aid in genetic counseling, prognosis, and, in some cases, inform therapeutic decisions. |
| microRNA 324 (MIR324) | microRNA 324 (MIR324) encodes a microRNA that regulates gene expression post-transcriptionally by binding to complementary sequences in target messenger RNAs (mRNAs), leading to mRNA degradation or translational repression. MIR324 is involved in multiple biological processes, including the regulation of cell proliferation, differentiation, and apoptosis. It has been shown to modulate signaling pathways such as the Hedgehog and Wnt pathways by targeting specific mRNAs involved in these cascades. MIR324 is expressed in various tissues, with notable roles reported in neural development and function. | MIR324 has been studied as a potential biomarker in several disease contexts, particularly in oncology and neurology. Altered expression levels of MIR324 have been observed in various cancers, including gliomas, hepatocellular carcinoma, and colorectal cancer, where its expression may correlate with tumor progression, prognosis, or response to therapy. Additionally, changes in MIR324 levels have been reported in neurological disorders. Its detectability in tissue and biofluids such as blood and cerebrospinal fluid enables its investigation as a non-invasive biomarker for disease diagnosis, prognosis, and monitoring. |
| mitogen-activated protein kinase 1 (MAPK1) | Mitogen-activated protein kinase 1 (MAPK1), also known as ERK2, is a serine/threonine kinase that is a key component of the MAPK/ERK signaling pathway. This pathway transduces extracellular signals, such as growth factors and mitogens, into intracellular responses that regulate diverse cellular processes. MAPK1 is activated by dual phosphorylation on threonine and tyrosine residues through the action of upstream kinases MEK1/2. Once activated, MAPK1 translocates to the nucleus where it phosphorylates a variety of substrates, including transcription factors, thereby influencing gene expression. Biological processes regulated by MAPK1 include cell proliferation, differentiation, survival, development, and response to stress. | MAPK1 has been studied as a biomarker in several contexts, particularly in oncology. Its expression level and phosphorylation status have been assessed in tumor tissues to evaluate pathway activation. Elevated MAPK1 activity has been associated with certain cancers, and its detection can provide information on tumor biology, prognosis, and potential responsiveness to targeted therapies that inhibit the MAPK/ERK pathway. In addition, MAPK1 has been examined as a pharmacodynamic biomarker to monitor the effects of MAPK pathway inhibitors in clinical trials. |
| myostatin (MSTN) | Myostatin (MSTN), also known as growth differentiation factor 8 (GDF-8), is a member of the transforming growth factor-beta (TGF-β) superfamily. It is predominantly expressed in skeletal muscle tissue, where it functions as a negative regulator of muscle growth. Myostatin inhibits myoblast proliferation and differentiation, thereby restricting skeletal muscle mass during development and in adult organisms. Loss-of-function mutations or reduced activity of myostatin result in increased muscle mass, as observed in certain animal models and rare human cases. Myostatin signaling involves binding to activin type II receptors, leading to the activation of SMAD transcription factors that modulate the expression of genes involved in muscle cell growth and differentiation. | Myostatin levels have been investigated as a biomarker for skeletal muscle mass and function. Circulating myostatin concentrations may reflect muscle wasting or atrophy in conditions such as sarcopenia, cachexia, and muscular dystrophies. Measurement of myostatin has been explored in clinical and research settings to assess muscle health, monitor disease progression, and evaluate the response to therapeutic interventions aimed at preserving or increasing muscle mass. |
| survival of motor neuron 1, telomeric (SMN1) | The survival of motor neuron 1, telomeric (SMN1) gene encodes the SMN protein, which is a critical component of the SMN complex involved in the biogenesis of small nuclear ribonucleoproteins (snRNPs). snRNPs are essential for pre-mRNA splicing, a process required for the maturation of messenger RNA in eukaryotic cells. The SMN protein is ubiquitously expressed and plays a key role in the assembly of snRNPs by facilitating the transfer of Sm proteins onto snRNA. Loss or deficiency of functional SMN protein, primarily due to deletions or mutations in the SMN1 gene, leads to impaired snRNP assembly and widespread defects in RNA processing, particularly affecting motor neurons. | SMN1 gene status, including gene copy number and the presence of pathogenic mutations, is used as a molecular biomarker in the diagnosis of spinal muscular atrophy (SMA), an autosomal recessive neuromuscular disorder. Genetic testing for SMN1 deletions or mutations can confirm a diagnosis of SMA and is also utilized in carrier screening and newborn screening programs. Quantification of SMN1 copy number is informative for assessing genetic risk and for distinguishing between affected individuals, carriers, and unaffected individuals. |
| survival of motor neuron 2, centromeric (SMN2) | The survival of motor neuron 2, centromeric (SMN2) gene encodes the SMN protein, which is crucial for the assembly of small nuclear ribonucleoproteins (snRNPs) and pre-mRNA splicing in all eukaryotic cells. SMN2 is a paralog of the SMN1 gene and differs by a few nucleotides, most notably a C to T transition in exon 7. This change leads to alternative splicing that results in the majority of SMN2 transcripts lacking exon 7, producing a truncated and less stable protein. Only a small proportion of full-length, functional SMN protein is produced from SMN2. The SMN protein is essential for motor neuron survival, and its deficiency leads to motor neuron degeneration. | SMN2 is used as a genetic biomarker in the context of spinal muscular atrophy (SMA). The copy number of the SMN2 gene is inversely correlated with disease severity; individuals with more copies of SMN2 generally produce higher levels of functional SMN protein and tend to have milder SMA phenotypes. Assessment of SMN2 copy number is applied in the prognostic evaluation of SMA patients and can inform clinical management decisions. Additionally, SMN2 copy number is often included in genetic testing panels for SMA diagnosis and carrier screening. |
Explore Research Opportunities with Protheragen. Our biomarker research services for Spinal Muscular Atrophy offer advanced technologies and scientific expertise to support exploratory studies in drug discovery and preclinical development. All biomarkers discussed are considered research targets only; Protheragen does not claim any biomarker as validated or mandatory for any application. Our services are strictly limited to preclinical research, and we maintain scientific objectivity in all collaborative efforts.
We invite you to connect with Protheragen to discuss your exploratory biomarker research needs for Spinal Muscular Atrophy. Our team is dedicated to scientific collaboration and knowledge exchange, supporting your research objectives with professionalism and technical rigor.
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