Biomarker Analysis Services for Kidney Transplant Rejection
Protheragen offers specialized biomarker analysis services tailored to support research and drug discovery for Kidney Transplant Rejection. Our comprehensive biomarker panel is designed to advance the understanding of disease pathophysiology, providing foundational insights for the development of novel therapeutics. All services are exclusively focused on preclinical research and drug discovery, and do not encompass clinical diagnostic applications.
The foundation of effective therapeutic intervention lies in the precise discovery and identification of biomarkers relevant to disease mechanisms. At Protheragen, our biomarker discovery services integrate advanced screening and validation strategies to identify molecular signatures associated with Kidney Transplant Rejection. Through systematic candidate selection and rigorous screening, we enable the early identification of potential biomarkers that inform drug development pipelines. Our validation process includes both in silico and experimental approaches to confirm biomarker relevance and reproducibility.
Multi Omics: Leveraging cutting-edge -omics technologies—including genomics, transcriptomics, and proteomics—Protheragen delivers comprehensive analyses of biological systems implicated in Kidney Transplant Rejection. Our multi-omics approach facilitates the identification of DNA, RNA, protein, and metabolite biomarkers, offering a holistic view of disease-associated pathways. This integrated strategy enables the elucidation of complex immune, inflammatory, and tissue injury mechanisms central to transplant rejection, supporting hypothesis-driven research and target discovery.
Candidate Validation: Protheragen employs robust validation strategies to assess the association of candidate biomarkers with Kidney Transplant Rejection pathophysiology. Our process includes preliminary screening using high-throughput assays, evaluation of expression patterns, and correlation with disease-relevant cellular and molecular events. Criteria for prioritizing promising candidates include biological plausibility, reproducibility, and technical feasibility for downstream assay development.
Diverse Technological Platforms: Our custom assay development capabilities span a broad spectrum of technological platforms, allowing adaptation to the specific requirements of each biomarker and research objective. We develop and optimize analytical platforms for protein, nucleic acid, and cellular biomarkers, ensuring compatibility with diverse sample types and throughput needs.
Immunoassays: We offer a suite of immunoassays, including ELISA, chemiluminescent, and multiplex immunoassay formats, for sensitive and quantitative detection of protein biomarkers.
Mass Spectrometry: Our LC-MS/MS platforms enable high-resolution, quantitative analysis of proteins and metabolites, supporting discovery and validation of novel biomarker candidates.
Flow Cytometry: Flow cytometry is utilized for detailed immunophenotyping of lymphoid and myeloid cell populations, including surface marker analysis relevant to immune activation and rejection processes.
Molecular Diagnostics: We provide molecular diagnostic techniques such as qPCR and digital PCR for quantification of gene expression and detection of nucleic acid biomarkers.
Histopathology And Imaging: Histopathological and imaging analyses, including immunohistochemistry, support spatial localization and tissue-specific assessment of biomarker expression.
Rigorous Method Validation: All analytical methods undergo rigorous validation in accordance with established research guidelines, including assessment of sensitivity, specificity, linearity, reproducibility, and robustness. Comprehensive quality control measures are implemented at each stage to ensure the reliability and accuracy of assay results.
Our quantitative analysis capabilities enable precise measurement of biomarker abundance across multiple platforms. We apply validated protocols for calibration, normalization, and statistical analysis, supporting robust interpretation of research data.
Sample Analysis: Protheragen handles a wide range of sample types, including blood, tissue, and cell lysates, with established protocols for preparation, storage, and processing. Each analysis is conducted under stringent quality measures to maintain sample integrity and reproducibility, with appropriate controls integrated throughout the workflow.
High Throughput Capabilities: We utilize multiplexed analytical platforms to maximize efficiency and data output, enabling simultaneous quantification of multiple biomarkers from limited sample volumes. This high-throughput capacity conserves valuable samples while accelerating research timelines.
| Gene Target | Biological Function | Application as a Biomarker |
|---|---|---|
| CD38 molecule (CD38) | CD38 is a multifunctional transmembrane glycoprotein expressed on the surface of various immune cells, including plasma cells, activated T and B lymphocytes, natural killer (NK) cells, and some non-hematopoietic tissues. It functions primarily as an ectoenzyme with ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities, catalyzing the conversion of NAD+ to cyclic ADP-ribose (cADPR), which plays a role in calcium signaling. CD38 is also involved in cell adhesion, signal transduction, and regulation of immune cell activation and proliferation. | CD38 is used as a biomarker in hematological malignancies, particularly in the identification and characterization of plasma cells in multiple myeloma and related disorders. Its expression is also evaluated in chronic lymphocytic leukemia (CLL), where higher surface levels have been associated with disease characteristics. Additionally, CD38 is utilized in flow cytometry panels for immunophenotyping of lymphoid and myeloid cells. |
| CD8 subunit alpha (CD8A) | CD8 subunit alpha (CD8A) is a glycoprotein that forms part of the CD8 co-receptor, typically expressed on the surface of cytotoxic T lymphocytes (CD8+ T cells). CD8A pairs with the CD8 beta chain (CD8B) to form a CD8αβ heterodimer, although CD8αα homodimers can also be present in certain cell types. The CD8 co-receptor binds to the non-polymorphic regions of major histocompatibility complex class I (MHC I) molecules on antigen-presenting cells. This interaction enhances the sensitivity of T cell receptor (TCR) recognition of antigenic peptides presented by MHC I, facilitating effective activation and cytotoxic function of CD8+ T cells. CD8A thus plays a central role in immune surveillance and the elimination of infected or malignant cells. | CD8A is widely used as a marker to identify and quantify cytotoxic T lymphocytes in various biological samples, including tissue sections and peripheral blood. Its expression is assessed in immunohistochemistry, flow cytometry, and gene expression analyses to evaluate the presence, abundance, or distribution of CD8+ T cells. In oncology, CD8A is often measured to assess tumor-infiltrating lymphocytes (TILs), which can provide information about the immune response within the tumor microenvironment. CD8A expression is also utilized in studies of infectious diseases, transplantation, and autoimmune conditions to monitor cytotoxic T cell populations. |
| cadherin 16 (CDH16) | Cadherin 16 (CDH16), also known as kidney-specific cadherin, is a member of the cadherin superfamily of calcium-dependent cell adhesion molecules. CDH16 is predominantly expressed in the kidney, particularly in the epithelial cells of renal tubules. It mediates homophilic cell-cell adhesion, contributing to the structural integrity and polarization of renal tubular epithelial cells. CDH16 plays a role in maintaining the architecture and function of the nephron by facilitating cell adhesion and communication within renal tissues. | CDH16 is used as a tissue-specific marker for renal epithelial cells in immunohistochemical analyses. Its expression is leveraged to aid in the identification of primary and metastatic renal cell carcinomas, as well as to distinguish renal origin in tumors of unknown primary. CDH16 immunostaining is also utilized in differentiating renal neoplasms from tumors of other origins in histopathological examinations. |
| complement C1s (C1S) | Complement C1s (C1S) is a serine protease that is a component of the C1 complex, the first component of the classical pathway of the complement system. C1S, together with C1q and C1r, forms the C1 complex, which is responsible for the recognition and initiation of the classical complement activation cascade upon binding to antigen-antibody complexes. Upon activation, C1S cleaves complement proteins C4 and C2, leading to the formation of the C3 convertase and subsequent downstream complement activation, resulting in opsonization, inflammation, and cell lysis. C1S thus plays a critical role in innate immunity, host defense, and the clearance of immune complexes. | C1S has been investigated as a biomarker in various clinical contexts, particularly in immune-mediated and inflammatory diseases. Altered levels or activity of C1S have been reported in conditions such as systemic lupus erythematosus, hereditary angioedema, and certain infections. Measurement of C1S, often alongside other complement components, can provide information about complement system activation and may assist in the assessment of disease activity or progression in relevant disorders. |
| complement C3 (C3) | Complement C3 (C3) is a central component of the complement system, which is a key part of the innate immune response. C3 is a glycoprotein that, upon activation by proteolytic cleavage, generates C3a and C3b fragments. These fragments mediate multiple immunological processes: C3a acts as an anaphylatoxin involved in inflammation, while C3b functions as an opsonin, promoting phagocytosis of pathogens, and participates in the formation of the membrane attack complex. C3 is activated through all three complement pathways—classical, alternative, and lectin—making it essential for pathogen recognition, clearance of immune complexes, and modulation of adaptive immunity. | C3 levels and activation products are measured in clinical and research settings to assess immune system activity and complement pathway involvement. Altered C3 concentrations have been observed in conditions such as autoimmune diseases (e.g., systemic lupus erythematosus), infections, and certain kidney disorders (e.g., glomerulonephritis). Measurement of C3 can aid in disease characterization, monitoring progression, and evaluating response to therapy. |
| major histocompatibility complex, class I, A (HLA-A) | HLA-A is a gene that encodes a major histocompatibility complex (MHC) class I molecule. MHC class I molecules are cell surface glycoproteins that present endogenously derived peptide antigens to CD8+ cytotoxic T lymphocytes. This antigen presentation is critical for immune surveillance, enabling the immune system to recognize and eliminate cells infected by viruses or transformed by malignancy. HLA-A molecules are expressed on nearly all nucleated cells and are highly polymorphic, contributing to individual variability in immune response. | HLA-A alleles are widely used in transplantation medicine for tissue typing to assess compatibility between donors and recipients, particularly in organ and hematopoietic stem cell transplantation. Specific HLA-A variants have been studied in association with susceptibility or resistance to certain infectious diseases, autoimmune disorders, and adverse drug reactions. HLA-A expression levels and allelic variants are also investigated in oncology, including their role in tumor immune evasion and as potential predictors of response to immunotherapies. |
| membrane spanning 4-domains A1 (MS4A1) | Membrane spanning 4-domains A1 (MS4A1), also known as CD20, is a transmembrane protein primarily expressed on the surface of B lymphocytes. It plays a role in the regulation of B cell development, differentiation, and activation. MS4A1 is involved in B cell receptor (BCR) signaling, although it does not have a known ligand or intrinsic enzymatic activity. Instead, it is thought to function as part of a membrane-associated complex that modulates calcium influx following antigen stimulation, thereby influencing B cell proliferation and survival. MS4A1 expression is initiated during the pre-B cell stage and is maintained until the plasma cell stage, where it is typically lost. | MS4A1 (CD20) is widely utilized as a biomarker for the identification and quantification of B cells in both research and clinical settings. Its cell surface expression is used in immunophenotyping to distinguish B cell populations via flow cytometry or immunohistochemistry. In clinical practice, MS4A1 is applied in the diagnosis and classification of B cell lymphomas and leukemias, as its expression is characteristic of most mature B cell neoplasms. Additionally, MS4A1 serves as a target for monoclonal antibody therapies in B cell malignancies and some autoimmune diseases. |
| protein kinase C beta (PRKCB) | Protein kinase C beta (PRKCB) is a member of the protein kinase C (PKC) family of serine/threonine kinases. PRKCB is activated by signals such as increased concentrations of diacylglycerol (DAG) and calcium ions, leading to its translocation to cell membranes where it phosphorylates a variety of protein substrates. It plays a central role in multiple cellular processes, including regulation of cell proliferation, differentiation, apoptosis, and immune responses. PRKCB is particularly important in B-cell receptor signaling, vascular endothelial cell function, and insulin signaling pathways. Its activity is implicated in the modulation of oxidative stress, angiogenesis, and inflammatory responses. | PRKCB has been investigated as a biomarker in several contexts. Altered expression or activity of PRKCB has been associated with certain hematological malignancies, such as chronic lymphocytic leukemia, where it may correlate with disease progression and prognosis. In addition, increased PRKCB activity has been observed in diabetic complications, especially diabetic nephropathy and retinopathy, where it is linked to vascular dysfunction. PRKCB has also been studied in the context of cardiovascular diseases, where its expression or activation state may reflect pathological changes in vascular tissues. |
| protein kinase C delta (PRKCD) | Protein kinase C delta (PRKCD) is a member of the novel protein kinase C (PKC) subfamily of serine/threonine kinases. It is activated by diacylglycerol (DAG) and phospholipids but is independent of calcium. PRKCD is involved in regulating a variety of cellular processes, including apoptosis, cell proliferation, differentiation, and immune responses. It participates in signal transduction pathways by phosphorylating target proteins involved in these processes. In particular, PRKCD has been shown to play roles in the regulation of cell death (apoptosis) and survival, modulation of immune cell function, and the cellular response to oxidative stress. | PRKCD expression and/or activation status has been investigated as a biomarker in several contexts. In oncology, altered PRKCD levels or activity have been reported in various cancers and have been correlated with disease progression, prognosis, and response to therapy in some studies. In autoimmune and inflammatory diseases, PRKCD has been studied for its association with immune cell regulation and disease activity. Additionally, PRKCD has been explored as a potential marker in cardiovascular diseases due to its role in vascular and myocardial cell signaling. Its application as a biomarker is based on these associations, as documented in established research. |
| toll like receptor 2 (TLR2) | Toll-like receptor 2 (TLR2) is a member of the toll-like receptor family, which plays a crucial role in the innate immune system. TLR2 is primarily expressed on the surface of immune cells such as monocytes, macrophages, dendritic cells, and some epithelial cells. It recognizes a broad range of pathogen-associated molecular patterns (PAMPs), including components from Gram-positive bacteria (such as lipoteichoic acid and peptidoglycan), fungi, mycobacteria, and certain viruses. Upon ligand binding, TLR2 forms heterodimers with other TLRs (notably TLR1 or TLR6), which initiates intracellular signaling cascades leading to the activation of NF-κB and the production of pro-inflammatory cytokines, chemokines, and type I interferons. This process facilitates the early immune response to infection and helps to shape adaptive immunity. | TLR2 expression and activity have been investigated as biomarkers in various infectious and inflammatory diseases. Changes in TLR2 levels or signaling have been associated with conditions such as sepsis, tuberculosis, autoimmune disorders, and certain cancers. Measurement of TLR2 expression on immune cells, or detection of TLR2-related gene transcripts in blood or tissue samples, has been used in studies to assess immune activation, disease progression, or response to therapy. Additionally, TLR2 has been explored as a potential marker for distinguishing between different types of infections and for monitoring the immune status in clinical settings. |
Explore Research Opportunities with Protheragen. Our biomarker research services offer a comprehensive platform for the identification, characterization, and analysis of molecular targets relevant to Kidney Transplant Rejection. All biomarkers discussed are strictly considered research targets, with no claims of validation or mandatory status. Our capabilities are focused exclusively on preclinical research stages, supporting exploratory studies and hypothesis generation. We emphasize scientific objectivity and a collaborative approach to advancing biomarker science.
We invite you to connect with Protheragen to discuss exploratory biomarker research opportunities. Our team is committed to scientific collaboration, knowledge exchange, and the advancement of preclinical research in Kidney Transplant Rejection. Let’s work together to explore the potential of biomarker discovery and validation in your research programs.
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