Cancer Diagnostics Solutions
p120 Catenin, a member of the Armadillo protein family, functions in intercellular adhesion and signal transduction. By binding to classical cadherins, p120 Catenin forms part of a multiprotein complex that links cadherins to the actin cytoskeleton, a process critical for maintaining cell?cell adhesion. Aberrant cytoplasmic accumulation of p120 Catenin has been reported in multiple malignancies, including lung, pancreatic, gastric, and colorectal carcinomas, and in colorectal cancer is associated with adverse clinical prognosis.
In breast pathology, immunohistochemical analysis demonstrates distinct staining patterns: lobular neoplasia exhibits a diffuse cytoplasmic distribution of p120 Catenin, whereas ductal neoplasia retains membranous localization. These differential staining patterns make p120 Catenin a valuable diagnostic marker for distinguishing lobular carcinoma from ductal carcinoma of the breast and for identifying early lesions of lobular neoplasia.
p16INK4a is a tumor suppressor protein. It is a specific inhibitor of cdk4/cdk6, and a tumor suppressor involved in the pathogenesis of a variety of malignancies. Recent analyses of the p16INK4a gene revealed homozygous deletions, nonsense, missense, or frameshift mutations in several human cancers. Although the frequency of p16INK4a abnormalities is higher in tumor-derived cell lines than in unselected primary tumors, significant subsets of clinical cases with aberrant p16INK4a gene have been reported among melanomas, gliomas, esophageal, pancreatic, lung, and urinary bladder carcinomas, and some types of leukemia.
Alkaline phosphatases (ALPs) are dimeric enzymes anchored to the cell membrane via glycosylphosphatidylinositol (GPI) linkages. There are four major isoforms: placental alkaline phosphatase (PLAP), germ cell alkaline phosphatase (GCAP or PLAP-like), intestinal alkaline phosphatase (IAP), and tissue non-specific alkaline phosphatase (TNAP). These isoenzymes are implicated in various physiological functions, including guidance of migratory cells, transmembrane transport of molecules such as lipids and immunoglobulins, and detoxification of lipopolysaccharides to protect against microbial invasion of the gastrointestinal mucosa. This antibody exhibits specificity for PLAP and GCAP. PLAP is physiologically expressed in the human placenta starting in the late first trimester of gestation. GCAP is present in normal tissues such as the endocervix and fallopian tube. Aberrant expression of GCAP is characteristic of several germ cell tumors, including intratubular germ cell neoplasia, unclassified (IGCNU), seminoma, embryonal carcinoma, and choriocarcinoma. PLAP serves as a diagnostic marker for germ cell tumors and is particularly useful in identifying primary intracranial germinomas.
P40 is a squamous cell carcinoma ?specific? antibody. It reacts with the vast majority of cases of squamous cell carcinomas of various origins, but not with adenocarcinomas. It is particularly useful in differentiating lung squamous cell carcinoma from lung poorly differentiated adenocarcinoma. P40 antibody can also be used as an alternative basal cell/myoepithelial cell marker, which has similar sensitivity and specificity as that of p63 antibody. Therefore, p40 antibody may also be used as an alternative immunohistochemical marker for determining prostate adenocarcinoma vs. benign prostate glands and for determining breast intraductal carcinoma vs. invasive breast ductal carcinoma.
P40 is a squamous cell carcinoma ?specific? antibody. It reacts with the vast majority of cases of squamous cell carcinomas of various origins, but not with adenocarcinomas. It is particularly useful in differentiating lung squamous cell carcinoma from lung poorly differentiated adenocarcinoma.
P40 antibody can also be used as an alternative basal cell/myoepithelial cell marker, which has similar sensitivity and specificity as that of p63 antibody. Therefore, p40 antibody may also be used as an alternative immunohistochemical marker for determining prostate adenocarcinoma vs. benign prostate glands and for determining breast intraductal carcinoma vs. invasive breast ductal carcinoma.
P53 is a tumor suppressor gene expressed in a wide variety of tissue types and is involved in regulating cell growth, replication, and apoptosis. It binds to mdm2, SV40 T antigen and human papilloma virus E6 protein P53 senses DNA damage and possibly facilitating repair. Mutation involving P53 is found in a wide variety of malignant tumors, including breast, ovarian, bladder, colon, lung, and melanoma
The anti-p53 tumor suppressor protein antibody specifically binds to a 53 kDa phosphoprotein, corresponding to the p53 gene product. This antibody demonstrates reactivity with both wild-type and mutant forms of p53; however, its diagnostic utility in immunohistochemistry (IHC) primarily relies on the accumulation of the mutant p53 protein, attributed to its prolonged half-life. Nuclear immunoreactivity with this antibody has been consistently observed in various malignancies, including breast carcinoma, lung carcinoma, colorectal carcinoma, and urothelial carcinoma
P57 is a tumor suppressor gene located on chromosome 11p15.5. Immunohistochemical detection using anti-p57 antibody is a valuable diagnostic tool in distinguishing complete hydatidiform mole (CHM) from partial hydatidiform mole (PHM) and hydropic abortion. In CHM, there is a complete absence of nuclear immunoreactivity in cytotrophoblasts and villous stromal cells, whereas PHM and hydropic abortions exhibit nuclear staining in these cell populations. In histologically normal placental tissue, anti-p57 antibody demonstrates nuclear positivity in cytotrophoblasts, intermediate trophoblasts, decidual cells, and villous stromal cells. Intervillous trophoblastic islands consistently show nuclear labeling across all entities and serve as an internal positive control.
P63 is a homolog of the tumor suppressor p53. It is identified in basal cells in the epithelial layers of a variety of tissues, including epidermis, cervix, urothelium, breast and prostate. P63 was detected in nuclei of the basal epithelium in normal prostate glands; however, it was not expressed in malignant tumors of the prostate. As a result, p63 has been reported as a useful marker for differentiating benign from malignant lesions in the prostate, particularly when used in combination with markers of high molecular weight cytokeratins and the prostate-specific marker AMACR (P504S). P63 antibody to human p63 protein labels an epitope common to all six p63 isotypes (TAp63?, TAp63?, TAp63?, ?Np63?, ?Np63?, ?Np63?). p63 labels the nuclei of myoepithelial cells in the prostate gland as well as breast tissue, making it useful in differentiating benign vs. malignant prostate lesions and breast lesions.
PAX-2 is a homeobox gene that is highly expressed during renal organogenesis. Following ureteric bud induction, PAX-2 is activated in the metanephric mesenchyme, where it plays a critical role in driving the mesenchymal-to-epithelial transition. Transgenic animal models overexpressing PAX-2 exhibit profound renal malformations and cystic changes, although they do not develop solid neoplastic lesions. Immunohistochemically, PAX-2 serves as a useful diagnostic marker. PAX-2 expression is typically observed in ovarian serous papillary carcinoma, whereas primary breast carcinoma lacks expression. Additionally, PAX-2 positivity in clear cell renal cell carcinoma, in contrast to its absence in hepatocellular carcinoma, provides a valuable tool for differential diagnosis.
The specificity of this monoclonal antibody to its intended target was validated using the HuProt? Array, which contains over 21,000 full-length human proteins. The PAX5 gene is part of the paired box (PAX) family of transcription factors. This gene family is characterized by a unique and highly conserved DNA-binding domain known as the paired box. PAX proteins are crucial regulators in early development, and changes in their gene expression are believed to contribute to neoplastic transformation. The PAX5 gene encodes the B-cell lineage-specific activator protein (BSAP), which is expressed in the early stages of B-cell differentiation, but not in later stages. Additionally, PAX5 expression has been observed in the developing central nervous system (CNS) and testis. Therefore, the PAX5 gene product may play a significant role not only in B-cell differentiation but also in neural development and spermatogenesis
Paired box protein 8 (PAX8) is a transcription factor belonging to the PAX family, with critical roles in embryonic organogenesis of the kidney, thyroid, and paramesonephric ducts, ultimately contributing to the development of urogenital structures including the seminal vesicles, vas deferens, ureter, uterus, and fallopian tubes. Beyond its developmental functions, persistent expression of PAX8 in adult kidney, thyroid, breast, and seminal vesicle, ovarian, cervical, and endometrial epithelia suggests an additional role in the maintenance of epithelial homeostasis. Immunohistochemical studies demonstrate predominantly nuclear localization with minimal cytoplasmic staining.
Due to its restricted distribution in normal tissues, PAX8 has emerged as a sensitive and specific immunohistochemical marker for primary and metastatic neoplasms arising from the aforementioned organs. PAX8 expression is consistently detected in clear cell, papillary, and chromophobe subtypes of renal cell carcinoma, as well as in endometrioid and serous ovarian carcinomas and in thyroid malignancies. However, its expression in lymphoid tissues remains a matter of controversy. Reports of PAX8 immunoreactivity in malignant lymphomas have been attributed to cross-reactivity of N-terminal polyclonal antibodies with PAX5, likely due to a high degree of sequence homology (~70%) in their N-terminal domains. Consequently, the diagnostic utility of PAX8 in hematolymphoid malignancies requires cautious interpretation.
PAX8 is a 62kDa protein belonging to the paired box (PAX) family of transcription factors. This nuclear protein plays a crucial role in the development of thyroid follicular cells and regulates the expression of thyroid-specific genes. Mutations in the PAX8 gene are linked to thyroid dysgenesis, thyroid follicular carcinomas, and atypical thyroid adenomas. PAX8 is expressed in the thyroid and its carcinomas, as well as in the non-ciliated mucosal cells of the fallopian tubes and simple ovarian inclusion cysts. However, it is not expressed in normal ovarian surface epithelial cells. A high percentage of ovarian serous, endometrioid, and clear cell carcinomas show PAX8 expression, while primary ovarian mucinous adenocarcinomas rarely do. PAX8 expression is also observed in renal tubules, renal cell carcinoma, nephroblastoma, and seminoma. Thus, PAX8 antibodies can be used as an additional immunohistochemical marker for identifying renal epithelial tumors.
Recognizes a protein of 42kDa, which is identified as PAX2. It is a member of the paired box family of transcription factors, which is required for development and proliferation of the kidney, brain, and millerian organs. PAX2 genes contain a highly conserved DNA sequence within the paired box region, which encodes a DNA-binding domain, enabling PAX proteins to bind the promoters of specific genes to transcriptionally regulate their expression.
PAX2 is specifically expressed in the developing central nervous system, eye, ear, and urogenital tract, and is essential for the development of these organs. In normal adult tissues PAX2 was mainly detected in the urogenital system, including kidney, ureteric epithelium, fallopian tube epithelium, ovary and uterus. In tumors, PAX2 has been detected in renal cell carcinomas, Wilms' tumors, nephrogenic adenomas and papillary serous carcinoma of the ovary. PAX2 has been used as a marker for the identification of renal cell carcinoma and ovarian carcinoma by immunohistochemistry
PAX5 is a transcription factor belonging to the paired box (PAX) gene family, which encodes proteins that function as key regulators of early developmental processes. Dysregulation of PAX gene expression has been implicated in oncogenic transformation. PAX5, also referred to as B-cell?specific activator protein (BSAP), is selectively expressed during the early stages of B-cell differentiation, but its expression is downregulated in later stages of B-cell maturation. In addition to its hematopoietic role, PAX5 expression has been identified in the developing central nervous system and testis, suggesting its involvement in neural development and spermatogenesis. Pathogenic variants or aberrations of the PAX5 gene are associated with hematologic malignancies, most notably B-cell acute lymphoblastic leukemia (B-ALL).
The PAX-8 antibody is expressed in the thyroid (and associated carcinomas), non-ciliated mucosal cells of the fallopian tubes and simple ovarian inclusion cysts, but not normal ovarian surface epithelial cells. The PAX-8 antibody is also expressed in a high percentage of ovarian serous, endometrioid, and clear cell carcinomas, but only rarely in primary ovarian mucinous adenocarcinomas. Studies have also found PAX-8 antibody expression in renal tubules as well as renal carcinoma, nephroblastoma and seminoma. Normal lung and lung carcinomas do not express PAX-8. Similarly, the absence of expression of PAX-8 in breast and other non-GYN carcinomas other than those primary to the thyroid indicates that the PAX-8 antibody is an important new marker of ovarian cancer and a useful marker for the differential diagnoses in lung and neck tumors, or tumors at distant sites where primary lung carcinoma or thyroid carcinoma are possibilities.
Proliferating Cell Nuclear Antigen (PCNA), also known as the polymerase ? auxiliary protein, is a pivotal component of DNA replication and DNA repair processes, including nucleotide excision repair and mismatch repair. PCNA functions as a nuclear protein and serves as a processivity factor for DNA polymerase ?, assembling as a homotrimeric sliding clamp that enhances the efficiency of leading-strand DNA synthesis. Beyond its role in replication, PCNA interacts with several regulatory and repair proteins, including the CDK inhibitor p21, structure-specific endonucleases such as Fen1 and XPG, and DNA cytosine-5-methyltransferase (MCMT), thereby integrating cell cycle regulation with DNA repair and epigenetic maintenance. PCNA expression is closely associated with proliferative activity, rendering it a valuable biomarker for assessing cell proliferation and the prognostic evaluation of neoplastic tissues. It is predominantly expressed during the early G1 and S phases of the cell cycle. In response to DNA damage, PCNA undergoes ubiquitination, participating in RAD6-dependent DNA damage tolerance pathways. Two transcript variants encoding the identical protein have been identified, and pseudogenes of PCNA have been described on chromosome 4 and the X chromosome.
PD-L1 is a checkpoint regulator in immune cells, it is expressed on immune or non-hematopoietic cells. Expression of the protein is seen during pregnancy where it has a role in suppressing the immune system. PD-L1 induces an inhibitory signal in activated T-cells and promotes T-cell apoptosis. It is overexpressed in a number of different cancers where it is believed to play a significant role in the cancer s ability to evade the immune system.
Programmed death receptor ligand 1 (PD-L1, also called B7-H1) is a recently described B7 family member. To date, one specific receptor has been identified that can be ligated by PD-L1. This receptor, programmed death receptor 1 (PD-1), has been shown to negatively regulate T-cell receptor (TCR) signaling. Upon ligating its receptor, PD-L1 has been reported to decrease TCR-mediated proliferation and cytokine production. PD-L1 expression was found to be abundant on many murine and human cancers and could be further up-regulated upon IFN-gamma stimulation. Thus, PD-L1 might play an important role in tumor immune evasion.
Programmed Death-Ligand 1 (PD-L1), also known as CD274 or B7 Homolog 1 (B7-H1), is a transmembrane protein that plays a critical role in immune suppression and in enabling tumor cells to evade immune destruction by binding to the Programmed Death-1 (PD-1) receptor. Overexpression of PD-L1 can help cancer cells evade detection and destruction by the host's immune system. In renal cell carcinoma, elevated PD-L1 levels have been associated with increased tumor aggressiveness and a higher risk of mortality. When evaluated in conjunction with the density of CD8+ tumor-infiltrating lymphocytes, PD-L1 expression levels can serve as a valuable predictor for various cancer types, including stage III non-small-cell lung cancer, hormone receptor-negative breast cancer, and sentinel lymph node melanoma
Perforin is a key cytolytic effector protein localized within the cytoplasmic granules of cytotoxic lymphocytes. It plays a critical role in immune surveillance and host defense by mediating the lysis of virus-infected and neoplastic cells. Perforin is a 555-amino acid protein that includes a 21-amino acid N-terminal signal peptide and has an estimated molecular mass ranging from 70 to 75 kDa. Functionally, perforin operates as a pore-forming protein, facilitating transmembrane channel formation via a mechanism analogous to that of complement component C9, with which it shares significant structural homology.
Expression of perforin is restricted to cytotoxic effector cell subsets, such as CD8? T lymphocytes and natural killer (NK) cells, and is absent in CD4? helper T cells and various tumor cell lines. Perforin serves as a crucial mediator of granule exocytosis-induced cytotoxicity, enabling the delivery of pro-apoptotic granzymes into target cells. Genetic mutations in the PRF1 gene encoding perforin are causative of familial hemophagocytic lymphohistiocytosis type 2 (FHL2 or HPLH2), a severe autosomal recessive immunoregulatory disorder manifesting in early childhood. Additionally, alternative splicing of PRF1 results in the generation of multiple transcript variants, potentially contributing to functional diversity.
Protein gene product 9.5 (PGP9.5), also known as ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1, PARK5), is a neuron-specific protein that is structurally and immunologically distinct from neuron-specific enolase. With a molecular mass of approximately 27 kDa, PGP9.5 was originally identified by high-resolution two-dimensional PAGE. It belongs to the ubiquitin carboxyl-terminal hydrolase family 1 (peptidase family C12) and contains an ubiquitin hydrolase domain. Functionally, PGP9.5 exhibits both ubiquitin hydrolase and ligase activities, mediating the hydrolysis of small C-terminal ubiquitin adducts to generate free ubiquitin monomers.
PGP9.5 is abundantly expressed in neurons and nerve fibers throughout the central and peripheral nervous systems, as well as in neuroendocrine cells, renal tubular epithelium, spermatogonia and Leydig cells of the testis, oocytes, and luteal cells in both pregnant and non-pregnant ovaries. Aberrant expression of PGP9.5 has pathological relevance: overexpression is associated with non-small cell lung carcinoma, while reduced expression has been implicated in neurodegenerative diseases such as Huntington?s disease and Alzheimer?s disease. Given its presence in neuronal inclusions, PGP9.5 serves as a reliable neuronal marker and is widely utilized in studies of neurodegenerative disorders, including Parkinson?s disease
This gene represents a phospholipase A2 receptor. The encoded protein likely exists as both a transmembrane form and a soluble form. The transmembrane receptor may play a role in clearance of phospholipase A2, thereby inhibiting its action. Polymorphisms at this locus have been associated with susceptibility to idiopathic membranous nephropathy. Alternatively spliced transcript variants encoding different isoforms have been identified.
Alkaline phosphatases (ALPs) are dimeric enzymes anchored to the cell membrane via glycosylphosphatidylinositol (GPI) linkages. There are four major isoforms: placental alkaline phosphatase (PLAP), germ cell alkaline phosphatase (GCAP or PLAP-like), intestinal alkaline phosphatase (IAP), and tissue non-specific alkaline phosphatase (TNAP). These isoenzymes are implicated in various physiological functions, including guidance of migratory cells, transmembrane transport of molecules such as lipids and immunoglobulins, and detoxification of lipopolysaccharides to protect against microbial invasion of the gastrointestinal mucosa. This antibody exhibits specificity for PLAP and GCAP. PLAP is physiologically expressed in the human placenta starting in the late first trimester of gestation. GCAP is present in normal tissues such as the endocervix and fallopian tube. Aberrant expression of GCAP is characteristic of several germ cell tumors, including intratubular germ cell neoplasia, unclassified (IGCNU), seminoma, embryonal carcinoma, and choriocarcinoma. PLAP serves as a diagnostic marker for germ cell tumors and is particularly useful in identifying primary intracranial germinomas.
This antibody targets a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental alkaline phosphatase (PLAP), which appears in the placenta during the third trimester. It is highly specific to PLAP and does not cross-react with other alkaline phosphatase isozymes. Anti-PLAP antibody is reactive with germ cell tumors, helping to differentiate them from other types of neoplasms. Additionally, some somatic tumors, such as breast, gastrointestinal, prostate, and urinary cancers, may also show immunoreactivity with anti-PLAP. Positive staining for anti-PLAP combined with negative anti-keratin staining supports a diagnosis of seminoma rather than carcinoma. While germ cell tumors are generally positive for anti-keratin, they often do not stain with anti-EMA (epithelial membrane antigen), unlike most carcinomas, which are anti-EMA positive. Anti-PLAP is also valuable in diagnosing gestational trophoblastic disease..
PMS2 is a gene that encodes for DNA repair proteins involved in mismatch repair. Carriers of the mismatch repair gene mutations have a high lifetime risk of developing Hereditary Non-Polyposis Colon Cancer (HNPCC) and several other cancers including endometrial cancer due to microsatellite instability (MSI) caused by accumulation of DNA replication errors in proliferating cells. Along with MLH1, MSH2 and MSH6, PMS2 is helpful in diagnosing MSI. Tumors with low-level MSI show unfavorable pathological characteristics compared to tumors with none and tumors with high-level MSI
Podoplanin is a transmembrane mucoprotein (38 kDa) recognized by the D2-40 monoclonal antibody. Podoplanin is specifically expressed in the endothelium of lymphatic capillaries but not in the blood vasculature. In normal skin and kidney, podoplanin is co-localized with VEGFR3/FLT4, another marker for lymphatic endothelial cells. Podoplanin is selectively expressed in lymphatic endothelium as well as Lymphangiomas, Kaposi?s Sarcomas and in subset Angiosarcomas with probable lymphatic differentiation. Podoplanin has also been shown to be expressed in Epithelioid Mesotheliomas, Hemangioblastomas and Seminomas
This gene encodes a protein that functions as a transcriptional repressor, inhibiting retinoic acid (RA) signaling via the nuclear receptors RARA, RARB, and RARG. It suppresses RA-mediated cellular outcomes, including proliferation arrest, differentiation, and apoptosis. The encoded protein is a cancer/testis antigen with restricted expression in malignant melanomas and immunoprivileged testicular tissue, and it is recognized by cytotoxic T lymphocytes. Its repressive activity on RA receptor signaling is thought to promote tumor cell survival and proliferation. Alternative splicing gives rise to multiple transcript variants encoding distinct isoforms
The human progesterone receptor (PR), is a ligand-activated transcription factor and is a member of the steroid receptor family. PR exists in humans as two isoforms; PR-A (94 kDa) which lacks the first 164 amino acids of PR-B and PR-B(114 kDa).
While the two forms of PR have similar DNA and Ligand binding affinities they have opposite transcriptional activities PR-B functions as an activator of progesterone-responsive genes, while PR-A functions as a strong transdominant repressor of PRB. This anti-PR recognizes both PR-A and B. It labels epithelial cells of breast, ovary and endometrium.
The progesterone receptor (PgR) is an estrogen-regulated protein. It has been proposed that expression of PgR determination indicates responsive estrogen receptor (ER) pathway, and therefore, may predict likely response to endocrine therapy in human breast cancer. A number of studies have shown that PgR determination provides supplementary information to ER, both in predicting response to endocrine therapy and estimating survival. PgR has proved superior to ER as a prognostic indicator in some studies.
Prolactin, a growth factor secreted by the anterior pituitary gland, is essential for the proliferation and differentiation of mammary glands. It is valuable in classifying pituitary tumors and studying pituitary diseases.
Additionally, prolactin contributes to the development of mammary cancer, acting both as a mitogen to stimulate cell division and as an agent promoting cellular differentiation
Prolactin, a growth factor secreted by the anterior pituitary gland, is essential for the proliferation and differentiation of mammary glands. It is valuable in classifying pituitary tumors and studying pituitary diseases.
Additionally, prolactin contributes to the development of mammary cancer, acting both as a mitogen to stimulate cell division and as an agent promoting cellular differentiation
Prostate-Specific Antigen (PSA) is a 33 kDa glycoprotein serine protease predominantly secreted by the luminal epithelial cells of the prostate gland and the periurethral glandular epithelium. PSA demonstrates robust cytoplasmic expression in both benign and malignant prostatic tissues. Immunohistochemical detection of PSA using anti-PSA antibodies serves as a valuable diagnostic tool for confirming prostatic origin in metastatic carcinomas involving non-prostatic sites
Prostate-specific antigen (PSA) is a protein produced by the cells of the prostate gland. PSA is present in small quantities in the serum of normal men and is often elevated in the presence of prostate cancer and in other prostate disorders. Higher than normal levels of PSA are associated with both localized and metastatic prostate cancer.
The PSA antibodyrecognizes primary and metastatic prostatic neoplasms but not tumors of nonprostatic origin. The antigen is a 33-34 kDa glycoprotein that is restricted to cells of prostatic origin. An immunohistochemical studyshowed more than 95% of prostatic carcinomas stained with PSA. PSA is demonstrable in the cytoplasm of acinar and ductal cells of normal or malignant prostate tissue
Prostate-specific antigen (PSA) is a single-chain glycoprotein of 237 amino acids containing approximately 8% carbohydrate. It is a serine protease produced almost exclusively by prostatic epithelial cells.Immunohistochemically PSA is expressed in the highly specialized apically-superficial layer of female and male secretory cells of the prostate gland, and is readily demonstrated in adenocarcinomas of the prostate in about 99% of the cases.
There is a correlation between malignancy grade and intensity of staining, high grade carcinomas displaying weaker expression. About 1% of poorly differentiated carcinomas have been negative for PSA.Due to the high specificity of PSA for prostatic glandular epithelium, it is very useful in identifying prostatic carcinoma in the prostate and in the adjacent organs often affected by epithelial malignancies, i.e. rectum and urinary bladder. PSA may be used in a panel together with NKX3.1 and Prostein, which are at least as sensitive and slightly more specific than PSA
Anti-PSAP demonstrates reactivity with prostatic acid phosphatase in the glandular epithelium of normal prostate, benign prostatic hyperplasia, and prostatic adenocarcinoma. It is valuable for establishing prostatic origin in metastatic lesions and serves as a complementary immunohistochemical marker when interpreted within the appropriate clinical and pathological context.
Prostate-specific membrane antigen (PSMA) is a type II transmembrane glycoprotein exhibiting enzymatic activity. It is expressed in both normal prostatic epithelial cells and neoplastic prostate cells. PSMA expression is upregulated in prostate cancer and has been associated with tumor progression. While PSMA demonstrates high sensitivity and specificity for prostatic tissue, its expression is also observed in select non-prostatic tissues, such as the small intestine and kidney. PSMA is a valuable biomarker for the detection of metastatic prostate carcinoma and for differentiating prostate carcinoma from urothelial carcinoma
PTEN (phosphatidylinositol-3, 4, 5-trisphosphate 3-phosphatase) is a tumor suppressor protein that harbors a tensin-like domain and a catalytic domain structurally homologous to dual-specificity protein tyrosine phosphatases. Loss-of-function alterations or mutations in PTEN have been frequently documented across a wide spectrum of human malignancies, including sporadic brain, breast, kidney, and prostate cancers
PTEN (phosphatidylinositol-3, 4, 5-trisphosphate 3-phosphatase) is a tumor suppressor protein that harbors a tensin-like domain and a catalytic domain structurally homologous to dual-specificity protein tyrosine phosphatases. Loss-of-function alterations or mutations in PTEN have been frequently documented across a wide spectrum of human malignancies, including sporadic brain, breast, kidney, and prostate cancers.
This gene encodes a member of the parathyroid hormone (PTH) protein family. The translated preproprotein undergoes proteolytic processing to yield the mature hormone, which interacts with the parathyroid hormone/parathyroid hormone-related peptide receptor (PTH/PTHrP receptor) to regulate systemic calcium and phosphate homeostasis. Pathological overproduction of PTH, as seen in hyperparathyroidism, results in hypercalcemia and may contribute to nephrolithiasis. Conversely, impaired synthesis or processing of PTH underlies hypoparathyroidism, a disorder characterized by hypocalcemia and associated neuromuscular manifestations such as paresthesia and tetany.