Biomarker Analysis Services for Pulmonary Arterial Hypertension
At Protheragen, we offer specialized biomarker analysis services dedicated to advancing drug discovery and preclinical development for Pulmonary Arterial Hypertension (PAH). Our comprehensive biomarker panel is designed to facilitate a deep understanding of PAH pathophysiology, supporting the identification and characterization of molecular targets relevant to disease mechanisms. Please note that all our services are exclusively focused on research applications for drug discovery and preclinical development stages; we do not provide clinical diagnostic services.
Effective therapeutic intervention for Pulmonary Arterial Hypertension begins with the robust discovery and identification of relevant biomarkers. Protheragen’s biomarker discovery services are tailored to support early-stage drug development by uncovering molecular indicators associated with disease onset, progression, and therapeutic response. Our approach integrates high-throughput screening of biological samples and comprehensive validation workflows to ensure the reliability and reproducibility of candidate biomarkers. The process involves iterative screening, data-driven selection, and rigorous experimental validation to confirm biomarker relevance for PAH research.
Multi Omics: Our multi-omics platform leverages cutting-edge technologies in genomics, transcriptomics, proteomics, and metabolomics to enable a holistic analysis of biological systems implicated in Pulmonary Arterial Hypertension. By integrating data from DNA sequencing, RNA expression profiling, protein quantification, and metabolite analysis, we systematically identify biomarkers at multiple molecular levels. This approach enables the elucidation of complex disease pathways, including those involving bone morphogenetic protein signaling, vascular remodeling, and endothelial dysfunction, which are central to PAH pathogenesis.
Candidate Validation: Candidate biomarker validation at Protheragen is grounded in rigorous experimental strategies designed to establish robust associations with Pulmonary Arterial Hypertension pathophysiology. Our validation process includes preliminary screening using high-sensitivity assays, reproducibility assessments across biological replicates, and correlation with disease-relevant phenotypes. Promising candidates are prioritized based on criteria such as specificity to PAH-related pathways, expression patterns in relevant tissues, and potential utility in monitoring disease progression or therapeutic intervention.
Diverse Technological Platforms: Protheragen provides custom assay development capabilities across a diverse array of technological platforms. Our laboratory infrastructure allows for the adaptation and optimization of analytical platforms to suit specific biomarker detection requirements, including high-sensitivity immunoassays, quantitative mass spectrometry, multiparametric flow cytometry, advanced molecular diagnostics, and histopathological imaging. Each platform is selected and tailored to maximize analytical performance for PAH biomarker research.
Immunoassays: We offer a suite of immunoassay technologies, including ELISA, chemiluminescent assays, and multiplex bead-based platforms, for sensitive and specific quantification of protein biomarkers.
Mass Spectrometry: Our LC-MS/MS workflows enable precise identification and quantification of proteins and peptides, supporting both targeted and discovery-based biomarker analyses.
Flow Cytometry: Flow cytometry is employed for the multiparametric analysis of cellular biomarkers, including surface and intracellular markers relevant to vascular and immune cell populations.
Molecular Diagnostics: We develop and implement nucleic acid-based assays, such as qPCR and digital PCR, for the detection and quantification of gene expression and genetic variants associated with PAH.
Histopathology And Imaging: Advanced histopathology and imaging techniques, including immunohistochemistry and digital image analysis, are utilized for spatial localization and quantification of biomarkers in tissue samples.
Rigorous Method Validation: All analytical methods developed at Protheragen undergo rigorous validation in accordance with established research guidelines. Validation parameters include accuracy, precision, sensitivity, specificity, linearity, and reproducibility. Comprehensive quality control measures are integrated at each stage, including the use of reference standards, internal controls, and inter-assay comparisons to ensure data integrity and reliability for preclinical research applications.
Our quantitative analysis capabilities encompass both absolute and relative quantification of biomarker levels in diverse biological matrices. We employ robust calibration strategies, internal standards, and validated reference materials to ensure high data quality. Quantitative outputs support hypothesis-driven research, biomarker ranking, and the generation of actionable insights for PAH drug discovery.
Sample Analysis: Protheragen processes a wide range of sample types, including plasma, serum, tissue lysates, and cell cultures, using standardized protocols tailored for biomarker preservation and detection. Each analysis incorporates stringent quality assurance steps, such as sample integrity assessment, contamination checks, and process controls, to maintain analytical consistency and reproducibility throughout the workflow.
High Throughput Capabilities: Our high-throughput analytical platforms enable the simultaneous analysis of multiple biomarkers across large sample cohorts. Multiplexed assay formats and automated sample handling increase efficiency, reduce turnaround times, and conserve valuable biological material. This approach is especially advantageous for exploratory studies requiring broad biomarker coverage and large-scale screening in PAH research.
| Gene Target | Biological Function | Application as a Biomarker |
|---|---|---|
| Pim-1 proto-oncogene, serine/threonine kinase (PIM1) | PIM1 encodes a serine/threonine kinase that is involved in the regulation of cell survival, proliferation, and differentiation. It functions as a proto-oncogene, playing a role in the control of cell cycle progression and inhibition of apoptosis. PIM1 is activated downstream of cytokine signaling, particularly in hematopoietic cells, and can phosphorylate various substrates involved in cell cycle regulation, such as cell cycle inhibitors and pro-apoptotic proteins. Its activity is regulated at the transcriptional and post-translational levels, and it has been implicated in the modulation of transcription factors, protein translation, and cellular metabolism. | PIM1 expression has been investigated as a biomarker in several cancer types, including prostate cancer, hematological malignancies, and solid tumors. Elevated PIM1 levels have been associated with tumor progression, higher tumor grade, and poor prognosis in certain contexts. Its detection in tissue samples or blood has been explored for potential use in cancer diagnosis, prognosis, and therapeutic response monitoring. PIM1 has also been studied as a potential target for kinase inhibitor therapies. |
| TNF receptor superfamily member 11b (TNFRSF11B) | TNF receptor superfamily member 11b (TNFRSF11B), also known as osteoprotegerin (OPG), is a secreted glycoprotein that functions as a decoy receptor for the receptor activator of nuclear factor kappa-B ligand (RANKL) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL). By binding to RANKL, TNFRSF11B inhibits the interaction between RANKL and its receptor RANK on the surface of osteoclast precursors, thereby suppressing osteoclast differentiation and activity. This regulatory mechanism plays a crucial role in bone remodeling and homeostasis by inhibiting bone resorption. Additionally, TNFRSF11B has been implicated in vascular biology, as it can bind to TRAIL and modulate vascular calcification processes. | TNFRSF11B has been utilized as a biomarker in clinical and research settings to assess bone metabolism and turnover. Elevated or reduced circulating levels of TNFRSF11B have been reported in conditions associated with altered bone remodeling, such as osteoporosis, Paget's disease of bone, and rheumatoid arthritis. Furthermore, changes in TNFRSF11B concentrations have been studied in relation to cardiovascular diseases, particularly in the context of vascular calcification. Measurement of TNFRSF11B in serum or plasma can provide information about bone resorption activity and may aid in monitoring disease progression or response to therapy in disorders affecting bone and vascular tissues. |
| apolipoprotein A1 (APOA1) | Apolipoprotein A1 (APOA1) is the major protein component of high-density lipoprotein (HDL) particles in plasma. It plays a central role in lipid metabolism, particularly in the reverse transport of cholesterol from peripheral tissues to the liver for excretion. APOA1 acts as a cofactor for lecithin-cholesterol acyltransferase (LCAT), an enzyme essential for the esterification of cholesterol on HDL particles. This process facilitates the maturation of HDL and the efficient removal of excess cholesterol from cells. Additionally, APOA1 has been implicated in anti-inflammatory and antioxidant activities associated with HDL. | APOA1 is commonly measured in clinical and research settings as an indicator of HDL quantity and function. Its plasma concentration is used in the assessment of cardiovascular risk, as lower levels of APOA1 are associated with an increased risk of atherosclerotic cardiovascular disease. Beyond cardiovascular applications, alterations in APOA1 levels have been reported in a variety of conditions, including liver disease, metabolic syndrome, and certain inflammatory disorders. Quantification of APOA1 is typically performed using immunoassays or mass spectrometry-based methods. |
| aryl hydrocarbon receptor (AHR) | The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor belonging to the basic helix-loop-helix Per-ARNT-Sim (bHLH-PAS) family. AHR is primarily known for mediating the biological response to a range of environmental xenobiotics, including polycyclic aromatic hydrocarbons and dioxins. Upon ligand binding, AHR translocates from the cytoplasm to the nucleus, where it dimerizes with the aryl hydrocarbon receptor nuclear translocator (ARNT). The AHR-ARNT complex binds to specific DNA sequences known as xenobiotic response elements (XREs), regulating the transcription of target genes involved in xenobiotic metabolism, such as cytochrome P450 enzymes (e.g., CYP1A1, CYP1B1). Beyond xenobiotic metabolism, AHR is implicated in various physiological processes, including immune system regulation, cell proliferation, and development. | AHR expression and activity have been studied as indicators of exposure to environmental contaminants, particularly dioxins and related compounds. Its induction or activation status in biological samples can serve as a biomarker of exposure to specific xenobiotics. Additionally, altered AHR expression or signaling has been investigated in the context of immune function, inflammation, and certain cancers, supporting its utility in monitoring disease-associated molecular changes. |
| bone morphogenetic protein receptor type 2 (BMPR2) | Bone morphogenetic protein receptor type 2 (BMPR2) is a transmembrane serine/threonine kinase that functions as a receptor for bone morphogenetic proteins (BMPs), which are members of the transforming growth factor-beta (TGF-β) superfamily. BMPR2 mediates BMP signaling by binding BMP ligands, leading to phosphorylation and activation of downstream SMAD transcription factors and other signaling pathways. This signaling is involved in the regulation of cellular processes such as proliferation, differentiation, apoptosis, and development, particularly in vascular endothelial and smooth muscle cells. BMPR2 plays a critical role in vascular homeostasis, embryonic development, and tissue remodeling. | BMPR2 is utilized as a biomarker in the context of pulmonary arterial hypertension (PAH). Mutations and reduced expression of BMPR2 have been identified in a significant proportion of familial and idiopathic PAH cases. Assessment of BMPR2 gene mutations or protein levels can provide information regarding genetic predisposition, potential disease mechanisms, and risk stratification in individuals with or suspected of having PAH. BMPR2 status is also used in research settings to study the molecular pathogenesis of PAH and to identify candidates for targeted therapies. |
| endoglin (ENG) | Endoglin (ENG) is a transmembrane glycoprotein that functions as part of the transforming growth factor-beta (TGF-β) receptor complex. It is predominantly expressed on vascular endothelial cells and plays a critical role in angiogenesis, vascular development, and vascular remodeling. ENG modulates TGF-β signaling pathways, influencing cellular proliferation, migration, and extracellular matrix production. Mutations in the ENG gene are associated with hereditary hemorrhagic telangiectasia type 1 (HHT1), a disorder characterized by vascular malformations. | Endoglin has been utilized as a biomarker in several clinical contexts. Its expression levels are assessed to evaluate angiogenic activity, particularly in tumor vasculature, where elevated endoglin is observed in proliferating endothelial cells. It is used in research and clinical studies as a marker for neovascularization in cancer, and increased levels of soluble endoglin in plasma have been associated with preeclampsia, a hypertensive disorder of pregnancy. Endoglin is also studied in the context of cardiovascular diseases and vascular pathologies. |
| fibroblast growth factor 7 (FGF7) | Fibroblast growth factor 7 (FGF7), also known as keratinocyte growth factor (KGF), is a member of the fibroblast growth factor family. It is primarily produced by mesenchymal cells and acts in a paracrine manner on epithelial cells by binding to the FGFR2b receptor isoform. FGF7 plays a crucial role in the regulation of epithelial cell proliferation, differentiation, migration, and survival. It is involved in embryonic development, wound healing, and tissue repair, particularly in epithelial tissues such as the skin, lung, and gastrointestinal tract. FGF7 signaling contributes to the maintenance of epithelial integrity and homeostasis. | FGF7 has been investigated as a biomarker in several clinical contexts. Elevated levels of FGF7 have been observed in certain cancers, such as breast, ovarian, and prostate cancer, and have been studied in relation to tumor progression and prognosis. In addition, FGF7 expression has been evaluated in diseases involving epithelial injury or regeneration, including pulmonary fibrosis and inflammatory bowel disease. Measurements of FGF7 in tissue or body fluids have been used in research to assess disease activity, tissue repair, or response to therapy. |
| growth differentiation factor 2 (GDF2) | Growth differentiation factor 2 (GDF2), also known as bone morphogenetic protein 9 (BMP9), is a member of the transforming growth factor-beta (TGF-β) superfamily. GDF2 is primarily produced in the liver and circulates in the bloodstream. It plays a key role in vascular biology, where it regulates endothelial cell function, promotes vascular quiescence, and inhibits excessive angiogenesis. GDF2 also contributes to the regulation of iron metabolism and has osteogenic properties, stimulating bone formation through the induction of osteoblast differentiation. Its signaling is mediated mainly via the activin receptor-like kinase 1 (ALK1) and other type I and type II serine/threonine kinase receptors. | GDF2 has been studied as a circulating biomarker in several vascular and hematological conditions. Reduced levels of GDF2 in plasma have been associated with hereditary hemorrhagic telangiectasia (HHT) and pulmonary arterial hypertension (PAH). Altered GDF2 concentrations have also been observed in certain liver diseases and in the context of abnormal bone metabolism. Measurement of GDF2 levels in biological fluids has been investigated for its potential to reflect endothelial dysfunction, vascular remodeling, and disease severity in these conditions. |
| kinase insert domain receptor (KDR) | Kinase insert domain receptor (KDR), also known as vascular endothelial growth factor receptor 2 (VEGFR-2), is a receptor tyrosine kinase that plays a central role in the regulation of angiogenesis. KDR is primarily expressed on endothelial cells and binds to members of the vascular endothelial growth factor (VEGF) family, particularly VEGF-A. Upon ligand binding, KDR undergoes dimerization and autophosphorylation, initiating multiple downstream signaling pathways that promote endothelial cell proliferation, migration, survival, and increased vascular permeability. These processes are essential for the formation of new blood vessels during embryonic development, wound healing, and in response to tissue ischemia. | KDR expression and activity have been used as biomarkers in various clinical and research settings. Elevated levels of KDR, or its phosphorylated form, have been observed in several malignancies, including colorectal, lung, and renal cell carcinomas, where it is associated with tumor angiogenesis. Measurement of KDR expression in tumor tissues or circulating endothelial cells can provide information on the angiogenic status of tumors and may be used to assess response to anti-angiogenic therapies targeting the VEGF pathway. Additionally, KDR is evaluated in the context of certain non-malignant diseases characterized by abnormal vascular growth or function. |
| platelet derived growth factor subunit B (PDGFB) | Platelet derived growth factor subunit B (PDGFB) encodes one of the two polypeptide chains that form the dimeric platelet-derived growth factor (PDGF) family of growth factors. PDGFB primarily functions as a mitogen for cells of mesenchymal origin, including fibroblasts, smooth muscle cells, and pericytes. The PDGFB protein usually forms a homodimer (PDGF-BB) or a heterodimer with PDGFA (PDGF-AB), and exerts its biological effects by binding to and activating PDGF receptor beta (PDGFRβ), a receptor tyrosine kinase. PDGFB signaling is critical for embryonic development, especially in the formation of blood vessels (angiogenesis), recruitment of pericytes to the developing vasculature, and wound healing. Dysregulation of PDGFB expression or signaling has been associated with various pathological processes, including proliferative disorders and fibrosis. | PDGFB has been investigated as a biomarker in several clinical contexts. Its expression levels and gene rearrangements have been studied in certain malignancies, such as dermatofibrosarcoma protuberans (DFSP), where the presence of the COL1A1-PDGFB fusion gene is a characteristic molecular feature. PDGFB expression has also been evaluated in the context of tumor angiogenesis and as a potential indicator of disease progression in cancers and fibrotic diseases. Additionally, PDGFB levels have been explored as a marker of vascular remodeling and injury in cardiovascular and renal diseases. |
Explore Research Opportunities with Protheragen. Our biomarker research services for Pulmonary Arterial Hypertension are designed to support exploratory and preclinical research into disease mechanisms and therapeutic targets. We offer a full suite of analytical capabilities, from discovery through validation, leveraging advanced -omics and assay technologies. Please note that all biomarkers discussed are considered research targets only; we do not claim any as validated or mandatory for PAH studies. Our expertise is focused exclusively on preclinical research stages, and we maintain a commitment to scientific objectivity and methodological rigor.
We invite you to discuss your biomarker research interests with Protheragen. Our approach emphasizes the exploratory nature of biomarker discovery and development, fostering scientific collaboration and knowledge exchange in the field of Pulmonary Arterial Hypertension. Let’s work together to advance understanding and innovation in preclinical research.
Make Order
Experimental Scheme
Implementation
Conclusion
