Biomarker Analysis Services for Glioma
At Protheragen, we provide specialized biomarker analysis services tailored for Glioma research and therapeutic development. Our comprehensive biomarker panel is designed to advance the understanding of Glioma pathophysiology, supporting drug discovery and preclinical development initiatives. Please note that all our services are exclusively focused on research and drug development through preclinical stages and do not include any clinical diagnostic applications.
Effective therapeutic intervention for Glioma is grounded in the discovery and identification of robust biomarkers. Protheragen’s biomarker discovery services are dedicated to supporting drug development by uncovering novel molecular targets and signatures associated with Glioma. Our integrated approach encompasses high-throughput screening, bioinformatic analysis, and systematic validation to ensure the selection of high-confidence biomarker candidates. Rigorous screening and validation processes are employed to confirm the relevance and reproducibility of identified markers within the context of Glioma biology.
Multi Omics: Leveraging cutting-edge -omics technologies, including genomics, transcriptomics, proteomics, and metabolomics, Protheragen enables a comprehensive exploration of biological systems implicated in Glioma. Through the integration of high-resolution sequencing, gene expression profiling, quantitative proteomics, and metabolite analysis, we identify DNA, RNA, protein, and metabolite biomarkers relevant to Glioma progression and treatment response. Our multi-omics approach facilitates the dissection of key pathways such as the PI3K/AKT, MAPK/ERK, and angiogenic signaling cascades, providing a systems-level understanding of disease mechanisms.
Candidate Validation: Our candidate validation strategies employ a combination of in vitro and in silico approaches to establish the association of potential biomarkers with Glioma pathophysiology. Preliminary screening includes quantitative and qualitative analyses using multiple assay platforms. Promising candidates are prioritized based on criteria such as disease relevance, biological plausibility, analytical detectability, and reproducibility across diverse sample sets. This ensures that only the most relevant markers progress into downstream assay development.
Diverse Technological Platforms: Protheragen offers custom assay development capabilities across a spectrum of advanced technological platforms. Our team adapts assay design to meet specific research requirements, including the integration of immunoassays, mass spectrometry, flow cytometry, molecular diagnostics, and histopathology/imaging platforms. This flexibility enables precise quantification and characterization of biomarkers relevant to Glioma research.
Immunoassays: We develop and apply ELISA, chemiluminescent, and multiplex immunoassays for sensitive and specific detection of protein biomarkers in various sample types.
Mass Spectrometry: Our LC-MS/MS platforms facilitate high-resolution quantification and characterization of proteins, peptides, and metabolites associated with Glioma.
Flow Cytometry: We utilize flow cytometry for multiparametric analysis of cell surface and intracellular biomarkers at the single-cell level.
Molecular Diagnostics: Our molecular diagnostics capabilities include PCR, qPCR, digital PCR, and sequencing-based assays for the detection of genetic and epigenetic biomarkers.
Histopathology And Imaging: We perform immunohistochemistry, in situ hybridization, and advanced imaging to localize and quantify biomarkers within tissue sections.
Rigorous Method Validation: All analytical methods undergo a rigorous validation process in accordance with established research guidelines. We assess performance characteristics including sensitivity, specificity, accuracy, precision, linearity, and reproducibility. Comprehensive quality control measures are implemented at each stage to ensure data integrity and reliability, supporting robust biomarker analysis for preclinical research applications.
Our quantitative analysis capabilities support the accurate measurement of biomarker levels across a variety of biological matrices. Advanced analytical platforms enable absolute and relative quantification, facilitating biomarker comparison, kinetic studies, and longitudinal monitoring within preclinical Glioma models.
Sample Analysis: Protheragen processes a wide range of sample types, including cell lines, primary tissues, xenograft models, and biofluids. Standardized protocols are applied for sample preparation, storage, and analysis to minimize variability. Stringent quality control procedures are in place to ensure sample integrity and data reproducibility throughout the analytical workflow.
High Throughput Capabilities: High-throughput, multiplexed analytical platforms allow for the simultaneous analysis of multiple biomarkers in limited sample volumes. This enhances efficiency, conserves valuable samples, and accelerates the data generation process, supporting large-scale Glioma research studies.
| Gene Target | Biological Function | Application as a Biomarker |
|---|---|---|
| AKT serine/threonine kinase 3 (AKT3) | AKT serine/threonine kinase 3 (AKT3) is a member of the AKT family of serine/threonine kinases, which are key mediators of the phosphatidylinositol 3-kinase (PI3K) signaling pathway. AKT3 is involved in the regulation of various cellular processes, including cell proliferation, survival, metabolism, and growth. While all AKT isoforms share considerable structural similarity, AKT3 exhibits tissue-specific expression, with relatively high levels in the brain and testes. In neural tissues, AKT3 has been implicated in brain development, neuronal survival, and myelination. It exerts its effects by phosphorylating a wide range of substrates involved in apoptosis inhibition, glucose metabolism, and cell cycle progression. | AKT3 expression and activity have been investigated as potential biomarkers in several disease contexts. In oncology, altered AKT3 expression or gene amplification has been reported in certain cancers, such as glioblastoma and melanoma, where it may be associated with tumor progression and therapeutic resistance. In neurological disorders, changes in AKT3 signaling have been studied in relation to neurodevelopmental conditions and brain injury. Measurement of AKT3 levels or activity in tissue samples has been utilized in research to help characterize disease subtypes and to explore associations with clinical outcomes. |
| B-Raf proto-oncogene, serine/threonine kinase (BRAF) | The B-Raf proto-oncogene, serine/threonine kinase (BRAF), encodes a protein that is a member of the RAF family of serine/threonine protein kinases. BRAF functions as a key component of the RAS-RAF-MEK-ERK signaling pathway, also known as the MAPK/ERK pathway, which transmits signals from cell surface receptors to the nucleus. This pathway regulates critical cellular processes including growth, differentiation, and survival. Upon activation by RAS, BRAF phosphorylates and activates MEK1 and MEK2, which in turn activate ERK1/2, leading to the regulation of gene expression. Mutations in BRAF, particularly the V600E substitution, can result in constitutive kinase activity and aberrant signaling, contributing to oncogenesis. | BRAF is utilized as a biomarker in oncology, particularly in the context of malignancies such as melanoma, colorectal cancer, and thyroid carcinoma. Detection of BRAF mutations, most notably the V600E mutation, is used to inform prognosis and guide therapeutic decision-making, including the selection of patients for targeted therapies with BRAF or MEK inhibitors. The presence of BRAF mutations can also aid in the differential diagnosis of certain tumor types and may provide information regarding disease progression and response to treatment. |
| MET proto-oncogene, receptor tyrosine kinase (MET) | The MET proto-oncogene encodes a receptor tyrosine kinase known as MET or hepatocyte growth factor receptor (HGFR). MET is primarily expressed on the surface of epithelial and some mesenchymal cells. Upon binding to its ligand, hepatocyte growth factor (HGF), MET undergoes dimerization and autophosphorylation, which activates multiple downstream signaling pathways, including the RAS-MAPK, PI3K-AKT, and STAT3 cascades. These pathways regulate various cellular processes such as proliferation, survival, motility, morphogenesis, and angiogenesis. MET signaling plays a critical role in embryonic development, tissue regeneration, and wound healing. Aberrant activation of MET, through overexpression, gene amplification, or mutations, has been implicated in oncogenic transformation and tumor progression. | MET is utilized as a biomarker in oncology, particularly in the context of solid tumors such as non-small cell lung cancer, gastric cancer, and papillary renal cell carcinoma. Assessment of MET gene amplification, protein overexpression, or activating mutations may inform prognosis and guide therapeutic decisions, especially regarding the use of MET inhibitors or multi-kinase inhibitors. Detection methods include immunohistochemistry, fluorescence in situ hybridization, and sequencing-based assays. The presence of MET alterations has been associated with tumor aggressiveness and, in some cases, resistance to targeted therapies. |
| epidermal growth factor receptor (EGFR) | Epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein and member of the ErbB family of receptor tyrosine kinases. Upon binding of its ligands, such as epidermal growth factor (EGF) or transforming growth factor-alpha (TGF-α), EGFR undergoes dimerization and autophosphorylation of its intracellular tyrosine kinase domain. This activates downstream signaling pathways, including the RAS-RAF-MEK-ERK and PI3K-AKT cascades, which regulate cellular processes such as proliferation, differentiation, survival, and migration. EGFR is expressed in various epithelial tissues and plays a key role in normal cellular homeostasis as well as in tissue repair. | EGFR is utilized as a biomarker in several clinical contexts, particularly in oncology. Overexpression, gene amplification, or specific mutations in EGFR are observed in multiple tumor types, including non-small cell lung cancer (NSCLC), colorectal cancer, and glioblastoma. Assessment of EGFR status can inform prognosis and guide therapeutic decisions, especially regarding the use of EGFR-targeted therapies such as tyrosine kinase inhibitors or monoclonal antibodies. EGFR mutation testing is commonly performed to identify patients who may benefit from these targeted treatments. |
| isocitrate dehydrogenase (NADP(+)) 1 (IDH1) | Isocitrate dehydrogenase (NADP(+)) 1 (IDH1) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate (also known as 2-oxoglutarate) in the cytoplasm and peroxisomes, using NADP+ as a cofactor. This reaction produces NADPH, which is important for cellular redox balance and biosynthetic processes. IDH1 plays a role in the tricarboxylic acid (TCA) cycle, lipid metabolism, and protection against oxidative stress by providing reducing equivalents for glutathione regeneration. | Mutations in the IDH1 gene, particularly the R132H substitution, have been identified in various types of tumors, most notably in diffuse gliomas and secondary glioblastomas, as well as in some cases of acute myeloid leukemia (AML) and other cancers. The presence of IDH1 mutations is used to assist in the classification, diagnosis, and prognostic assessment of these tumors. Detection of IDH1 mutations can be performed using molecular genetic methods or immunohistochemistry, and is integrated into the diagnostic criteria for certain central nervous system tumors. |
| isocitrate dehydrogenase (NADP(+)) 2 (IDH2) | Isocitrate dehydrogenase (NADP(+)) 2 (IDH2) is a mitochondrial enzyme that catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate, producing NADPH from NADP+ in the process. This reaction is a key step in the tricarboxylic acid (TCA) cycle, contributing to cellular energy production and redox balance. The NADPH generated by IDH2 is important for protecting cells against oxidative stress by maintaining the reduced state of glutathione and supporting other biosynthetic processes. IDH2 functions as a homodimer and is localized in the mitochondrial matrix. | Mutations in the IDH2 gene, particularly at residues R140 and R172, have been identified in various malignancies, including acute myeloid leukemia (AML), gliomas, and other cancers. These mutations result in a neomorphic enzyme activity that produces the oncometabolite D-2-hydroxyglutarate, which is associated with altered cellular metabolism and epigenetic dysregulation. Detection of IDH2 mutations is used in the molecular characterization of tumors, providing diagnostic, prognostic, and, in some contexts, predictive information regarding disease classification and potential therapeutic responsiveness. |
| phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha (PIK3CA) | Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha (PIK3CA) encodes the p110α catalytic subunit of class I phosphoinositide 3-kinases (PI3Ks). PI3Ks are lipid kinases that phosphorylate phosphatidylinositol-4,5-bisphosphate (PIP2) to generate phosphatidylinositol-3,4,5-trisphosphate (PIP3), a second messenger involved in the activation of downstream signaling pathways. PIK3CA-mediated PI3K activation regulates diverse cellular processes, including cell growth, proliferation, survival, metabolism, and motility. The PI3K/AKT signaling pathway, in which PIK3CA plays a central role, is critical for normal cellular function and is tightly regulated under physiological conditions. | Somatic mutations in PIK3CA have been identified in various human cancers, including breast, colorectal, endometrial, and other tumor types. The presence of PIK3CA mutations has been associated with oncogenic activation of the PI3K/AKT pathway. In clinical settings, detection of PIK3CA mutations can inform diagnosis, prognosis, and therapeutic decision-making, particularly in the context of targeted therapies such as PI3K inhibitors. PIK3CA mutation status is also used in some cases to stratify patients for clinical trials and to monitor disease progression and treatment response. |
| platelet derived growth factor receptor alpha (PDGFRA) | Platelet derived growth factor receptor alpha (PDGFRA) is a cell surface receptor tyrosine kinase that binds members of the platelet-derived growth factor (PDGF) family. Upon ligand binding, PDGFRA undergoes dimerization and autophosphorylation, initiating downstream signaling cascades such as the PI3K-AKT, RAS-MAPK, and PLCγ pathways. These signaling events regulate cellular processes including proliferation, differentiation, migration, and survival. PDGFRA is expressed in various mesenchymal cell types and plays a critical role in embryonic development, tissue repair, and maintenance of connective tissues. | PDGFRA is utilized as a biomarker in the context of certain malignancies, particularly gastrointestinal stromal tumors (GISTs), where mutations or overexpression can be detected. The presence of PDGFRA mutations has clinical relevance for diagnosis, prognosis, and therapeutic decision-making, especially with regard to the use of tyrosine kinase inhibitors. Additionally, PDGFRA expression or mutation status is assessed in other tumor types and in research evaluating targeted therapies. |
| tumor protein p53 (TP53) | Tumor protein p53 (TP53) encodes a transcription factor that plays a critical role in regulating the cell cycle, maintaining genomic stability, and inducing apoptosis in response to cellular stress and DNA damage. p53 functions as a tumor suppressor by activating genes involved in cell cycle arrest, DNA repair, senescence, and programmed cell death. In normal cells, p53 activity is tightly controlled and maintained at low levels; upon DNA damage or oncogenic stress, p53 is stabilized and activated, leading to the transcription of target genes that prevent the propagation of damaged DNA. | TP53 status, including mutations and protein expression levels, is widely used in research and clinical settings to assess tumor characteristics. Mutations in TP53 are among the most common genetic alterations in human cancers and are associated with tumor development, progression, and response to therapy. Analysis of TP53 mutations or abnormal p53 protein accumulation can provide information on prognosis, predict therapeutic responses, and assist in the molecular classification of various malignancies. |
| 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 binds to specific tyrosine kinase receptors, primarily VEGF receptor 1 (VEGFR-1) and VEGF receptor 2 (VEGFR-2), on the surface of endothelial cells. This binding activates downstream signaling pathways that promote endothelial cell proliferation, migration, and survival, as well as increased vascular permeability. VEGFA plays essential roles in embryonic development, wound healing, and tissue regeneration, and is also implicated in pathological conditions characterized by abnormal blood vessel growth. | VEGFA is utilized as a biomarker in various clinical and research settings, particularly in oncology and ophthalmology. In cancer, elevated VEGFA levels in blood or tissue samples have been associated with tumor angiogenesis, progression, and prognosis in several malignancies, including colorectal, lung, and breast cancers. In ophthalmology, VEGFA is measured in the context of diseases characterized by abnormal neovascularization, such as age-related macular degeneration and diabetic retinopathy. Additionally, VEGFA levels are monitored to assess response to anti-angiogenic therapies targeting the VEGF pathway. |
Explore Research Opportunities with Protheragen. Our biomarker research services for Glioma leverage advanced analytical platforms and a comprehensive biomarker panel to support drug discovery and preclinical development. We emphasize the exploratory and research-focused nature of our work, offering robust capabilities for biomarker discovery, validation, and assay development. Please note that all biomarkers discussed are research targets only; we do not claim any as validated or mandatory for Glioma studies. Our services are strictly limited to preclinical research stages, and we maintain scientific objectivity in all collaborations.
We invite you to connect with Protheragen to discuss collaborative opportunities in Glioma biomarker research. Our team is committed to advancing scientific knowledge through exploratory studies and open exchange of ideas—reach out to explore how we can support your preclinical research objectives.
Make Order
Experimental Scheme
Implementation
Conclusion
