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M Nap

Publications and source records attributed to M Nap.

At least 37 records · Page 2Linked to original sources
PubMed1998

Epitope specificity of 30 monoclonal antibodies against cytokeratin antigens: the ISOBM TD5-1 Workshop.

The epitope specificities of 30 monoclonal antibodies (MAbs) against the most common human cytokeratins. i.e., Nos. 8, 18, and 19, in epithelial cells were investigated in the ISOBM TD-5 Workshop. Seven research groups from universities or companies participated independently in the evaluation of the antibody specificities. The complex assembly of cytokeratins in vivo, with obligatory heterologous dimeric combinations of different cytokeratins from each of the two major groups, comprising together more than 20 different individual cytokeratins, made analysis of the antibody reactivity patterns with isolated single cytokeratins necessary. The concordance of the evaluations was striking and independent of the technologies used. As antigens purified individual cytokeratins, chemically degraded purified cytokeratins, recombinant intact and truncated cytokeratins, as well as specific synthesized shorter peptides were used. In order to elucidate the epitope specificity, reactivity patterns in ELISA assays and immunoblots with partial enzymatic degradation of the antigens were performed. Competitive cross-inhibition experiments between antibodies using antigens and antibodies in all possible combinations were performed with radioimmunometric assays, BIAcore, and ELISA technology. All 30 antibodies could convincingly be classified with regard to target cytokeratin. One MAb (192) had to be deleted due to dual specificities in both isotype and epitope specificity against its target. Six antibodies bound selectively to cytokeratin 8, 14 to cytokeratin 18, and 10 to cytokeratin 19, as demonstrated by using native, recombinant, and synthesized antigens. The immunodominant part of the molecule for all three types of cytokeratins was located in the region of amino acid (aa) 270-400. Out of the six MAbs reactive with cytokeratin 8, four MAbs, i.e., 178, 199, 202, and 206, were reactive with a sequence in the interval aa 340-365, and MAb 191 reacted with a closely related epitope. The remaining antibody, 192, presented dual specificities. At least two closely related major immunogenic epitopes could be identified in cytokeratin 8. In cytokeratin 18 four distinct epitopes could be documented, again with the dominating sequence region 270-429 as target for 10 (181, 184, 186, 188, 189, 190, 193, 196, 198, and 200) out of 14 antibodies. Since MAb 193 is known to react with the M3 epitope, aa 322-342 in cytokeratin 18, this entire group is reactive in the region close to the charge shift, in the middle of the rod 2B region, as shown by competitive binding. The remaining four anticytokeratin 18 antibodies (180, 185, 203, and 205) displayed unique, noncompetitive binding to this filament. Cytokeratin 19, reactive with altogether ten antibodies, displayed two major epitopes, all of them also within the large immunodominant region. MAbs 179, 195, 197, and 204 were reactive with the peptides aa 311-335 also known as the KS 19.1 epitope, and MAbs 182, 183, 187, 194, and 201 bound to peptide aa 346-367, known as the BM 19.21 epitope. One antibody, 231, was selectively reactive with aa 356-370 in cytokeratin 19. A complex pattern of binding specificities comprising at least ten different, noncompetitive epitopes, mainly situated in the rod portion, 2A and 2B, situated close to the charge shift in the rod of all three cytokeratins was documented. Out of the 29 classifiable antibodies, altogether 22 were reactive in this very short region, i.e., from aa 311 to 370 in all cytokeratin filaments. The remaining seven antibodies displayed unique binding properties. The implications of the findings are of significance both for immunohistochemistry and for assaying circulating heterodimeric, partially degraded complexes in patients' blood for tumor marker evaluation.

Amino Acid Sequence↗
PubMed1997

Quantification of vascular density and of lumen and vessel morphology in endometrial carcinoma. Evaluation of their relation to serum levels of tissue polypeptide-specific antigen and CA-125.

OBJECTIVE: To determine whether differences in tumor vessel architecture influence the entry of tumor-associated antigens into the circulation. STUDY DESIGN: Using an image analysis system, nine vascular parameters in samples of endometrial carcinomas stained for factor VIII-related antigen were evaluated. These were related to groups with, respectively, normal and elevated serum values for two different serum tumor markers: one with low tissue polypeptide-specific antigen (TPS) and one with high molecular weight (CA-125). RESULTS: Lumen area, lumen perimeter and maximum lumen diameter appeared to differentiate between the normal and elevated TPS group; the higher lumen values occurred in the latter (Mann and Whitney U test: P = .021, .013 and .014, respectively). For CA-125 a higher number of vessels per square millimeter after correction for the epithelium-stroma ratio was found to differentiate between the normal and elevated group (P = .011). The other parameters did not show differentiation between the groups. CONCLUSION: Distension of vessels appears to be related to the TPS serum level; that might be explained by the presence of endothelial gaps, permitting passive passage of the small TPS molecules. Vascular density appears to be related to the CA-125 serum level. However, whether this relation is real remains to be determined.

Antigens, Neoplasm↗
PubMed1996

Specificity and affinity of 26 monoclonal antibodies against the CA 125 antigen: first report from the ISOBM TD-1 workshop. International Society for Oncodevelopmental Biology and Medicine.

The specificity of 26 monoclonal antibodies against the CA 125 antigen was investigated in two phases of the ISOBM TD-1 workshop. The binding specificity was studied using CA 125 immunoextracted by specific antibodies immobilized on various solid phases, or on the surface of human cell lines. Immunometric assays using all possible antibody combinations were used to study the topography of antibody binding sites on the antigen. We conclude that the CA 125 antigen carries only two major antigenic domains, which classifies the antibodies as OC125-like (group A) or M11-like (group B). One antibody, OV 197, showed binding specificity related to some of the OC125-like antibodies, but was classified into a separate group C. The OC125-like group of antibodies has four subgroups with different binding specificities. These are A1 = OC 125 and K 95, A2 = K 93, A3 = B43.13, and A4 = ZS 33, B27.1 and CCD 247. Binding of nonlabelled OC 125 or K 95 to CA 125 caused a marked increase in binding of labelled OV 197 to the complex. This conformational change was not observed with any other antibody combinations. Antibody B43.13 could form immunometric assay combinations particularly with antibodies of subgroup A4, indicating that the B43.13 epitope is in the periphery of the binding area of OC125-like antibodies. The M11-like group of antibodies is more homogenous with strong cross-inhibition between most antibodies. Only one antibody, ZR 38, would form an immunoassay combination with other M11-like antibodies and thus represents a distinct subgroup. The main group of M11-like antibodies are M 11, ZR 45, MA602-6, K 91, OV 185, K 101, K 90, K 96, K 97, K 102, CCD 242, 145-9, and 130-22. Antibody OV 197 binds to a domain designated C and is unique, as stated above. Antibody pairs from any two of the three groups may be used in immunometric assays. Three antibodies were not studied by complete cross-inhibition due to low affinity (OV 198 and K 100) or lack of material (MA602-1). OV 198 and K 100 are most likely OC125-like and MA602-1 is M11-like. Antibody affinity was estimated with labelled antigen in solution or with antigen absorbed on microtiter wells. Western blot analysis showed staining both in the stacking gel and corresponding to a molecule of 200 kDa. There was a marked difference between the antibodies in their ability to bind to CA 125 immobilized on a membrane. Strongest binding was observed with the M11-like antibodies, particularly M 11, K 96, K 97, MA602-6, 145-9. Antibodies belonging to the subgroup A4 were the only OC 125-like antibodies which reacted well with CA 125 in Western analysis. Digestion of CA 125 with proteolytic enzymes showed it to be particularly sensitive to trypsin cleavage. However, no low molecular weight fragments with preserved immunoreactivity were found.

Animals↗
PubMed1996

Immunohistochemical characterization of 22 monoclonal antibodies against the CA125 antigen: 2nd report from the ISOBM TD-1 Workshop.

We evaluated the immunohistological (IH) characteristics of 22 different antibodies that were submitted for study in the frame of the TD-1 ISOBM Workshop on monoclonal antibodies against CA125. Information on relative affinities and epitope similarities was obtained from a parallel immunochemical study. Antibodies were tested at concentrations of 10 and 1 micrograms/ml on frozen and paraffin sections. Paraffin sections were stained according to the streptavidin-biotin complex protocol, and frozen sections according to a two-step immunoperoxidase technique. Aminoethylcarbazole served as the chromogen. The tissues were from normal proliferative endometrium (formalin-fixed paraffin-embedded) material and clear-cell adenocarcinoma of the ovary (formalin-fixed paraffin-embedded and frozen material). Sections were scored for staining in epithelial cells, basal, apical and diffuse cytoplasmic and in stromal components. Intensity was graded as 1, 2 or 3 for epithelial cells and as -1, -2 or -3 for stroma. The cumulative scores for each antibody expressed the discriminative properties of specific epithelial staining against background. M11 and M11-like antibodies, as well as OC125 and OC125-like antibodies, in general showed good staining results. Although there was a trend for high-affinity antibodies to show higher scores, there was no clear relationship between affinity and staining result. For nine antibodies (ZR45, MA602-1, K102, K94, K90, OV185, K97, K96, OV198), the reactions in paraffin and frozen sections were of similar intensity. Most of these were of low affinity with one exception: antibody ZR45, a rat monoclonal antibody (MAb) which had a high relative affinity. For eight antibodies (M11, K101, MA602-6, ZS33, B27.1, B43.13, K93, OC125), a loss of specific staining was observed in frozen sections. All but two of these antibodies (MA602-6 and OC125) were of high relative affinity. With four antibodies (K91, ZR38, K95, K100), the reverse situation was observed. One (K100) was of low affinity, two (K95 and K91) of high affinity and the fourth (ZR38) was a rat MAb of high affinity. Mainly due to the increased cytoplasmic staining in carcinoma, the reactivity in paraffin sections was less extensive in normal endometrium compared to ovarian carcinoma for the majority of antibodies, irrespective of their affinity or epitope group. The IH characterization of these antibodies may be of help in selecting antibodies with specific properties for further comparative studies. The reactivity of normal endometrium with all useful antibodies makes it a good candidate for standard external IH tissue control.

Adenocarcinoma, Clear Cell↗
PubMed1995

Quantification of relative area of pS2 immunohistochemical staining and epithelial percentage in breast carcinomas: the effect of the latter on the interpretation of a cytosolic pS2 assay.

In immunochemical assays of specific cell constituents in cytosols from tumors, the relationship between epithelial and stromal fractions is not taken into account. This may influence the outcome of the measurements and result in incorrect categorization as negative or positive. In a setting addressing pS2 (only detectable in epithelial cells) in breast carcinomas, we investigated three possibilities that may overcome this problem using histologic sections of breast carcinomas of 50 patients: (a) visual estimation of area percentage of immunohistochemical staining of the cell constituent of interest performed by three independent individuals, (b) quantification of area percentage of the immunohistochemical results by true color image analysis, and (c) quantification of the epithelial and stromal compartments of the tumors in Heidenhain's-azan-stained tissue sections, using the true color image analysis system, to assess the epithelial percentage in the tumors. This percentage was used as a correction factor for data on pS2 obtained by cytosolic determinations. Visual estimation appeared to be subject to interobserver variation and, subsequently, becomes less applicable in the absence of strict scoring rules. Based on tests for correlation, image analysis system quantification seemed reproducible in both quantification procedures. However, due to the high magnification necessary to visualize the immunohistochemical staining product, the effect of field selection caused systematic differences between repeat measurements (Friedman test). As a result of the contrasting colors of the azan staining, the calculation of the epithelia percentage could be performed at a low magnification. Consequently, here the effect of field selection was not present. Correction of cytosolic values for epithelial percentage resulted in 8% of the cases changing category.(ABSTRACT TRUNCATED AT 250 WORDS)

Breast Neoplasms↗
PubMed1994

Immunohistochemical localization of insulin-like growth factor 1 receptors in benign and malignant tissues of the female genital tract.

The distribution of insulin-like growth factor I (IGF-1) receptors in the female genital tract was examined by immunohistochemistry. The monoclonal antibody alpha-IR-3, which binds to the alpha-subunits of the IGF-1 receptor, was used for specific binding and the peroxidase-antiperoxidase method was used for staining. IGF-1 receptors were consistently detected in the epithelium of cervix, endometrium and the fallopian tube. Furthermore, high expression of the IGF-1 receptors was found in ovarian cancer tissue, where predominantly the stromal cells around the vessels gave an intense staining. Since the expression of the IGF-1 receptors in tumor epithelium was only weak and inconsistent, it is tempting to speculate that the stromal compartment in ovarian cancer is the target tissue for the effects of IGF-1.

Cell Membrane↗
PubMed1994

Quantification of area percentage of immunohistochemical staining by true color image analysis with application of fixed thresholds.

Most image analysis systems (IAS) use black-and-white cameras. However, true color IASs are considered to be useful for quantification of immunohistologically stained structures. Using a true color IAS, we evaluated two methods of segmentation for quantification of area percentage of staining: one using fixed, preset thresholds and one using thresholds interactively set per image. Furthermore, the effect of shading correction was evaluated, and measurements in both color and black-and-white mode were compared. The results of segmentation with fixed thresholds did not differ significantly from those of control percentages, established by interactive morphometry using a grid, which served as reference. Interactive segmentation was significantly different from the reference (t test, P = .0001). The effect of shading correction was negligible. Measurements with and without this procedure correlated highly (r = .99, P < .001). Comparison of the results obtained in color and black-and-white mode showed a significant difference in the latter from the reference (t test, P = .005). We conclude that it is possible to quantify, in a reliable way, area percentage of positive staining using a true color IAS with application of a segmentation method with fixed thresholds.

Breast Neoplasms↗
PubMed1993

Immunohistochemical detection of P-glycoprotein in normal and malignant tissues: a comparative study of three monoclonal antibodies, JSB-1, C 219 and 265/F4, against different epitopes using frozen and paraffin tissue sections.

In this study, the reactivity of three different monoclonal antibodies (MAbs) against the multiple-drug resistance (MDR)-related P-glycoprotein (P-170) were compared with each other using a collection of frozen and paraffin-embedded tumors, normal tissues and metastatic cells of malignant pleural and peritoneal effusions. The MAbs JSB-1, C 219 and 265/F4 were used in an indirect immunoperoxidase technique on frozen material. In addition, MAb C 219 was used on formalin-fixed, paraffin-embedded material from the same tumors, of which frozen sections were studied, and in a retrospective study C 219 was tested on paraffin blocks of the primary tumors that were responsible for the malignant effusions. The results show different staining patterns for all three MAbs to some extent. Results in frozen and paraffin sections obtained with MAb C 219 were comparable. MAb C 219 performs well both in frozen and formalin-fixed, paraffin-embedded material, making it a useful candidate for application in routine laboratory analysis. The retrospective analysis did not show consistency of P-170 expression in the same patients. This leads to the hypothesis that the actual status of P-170 expression in recurrent disease should be obtained before continuing or modifying chemotherapy. Clinical studies aimed at the correlation of immunohistochemistry with therapy response have to evaluate the relevance of P-170 expression in drug resistance of primary and metastatic tumors.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1993

Image analysis in immunohistochemistry. Factors with a possible influence on the performance of VIDAS version 2.0, a commercially available true color image analysis system.

This paper describes the evaluation of several factors with a possible influence on the performance of a commercially available image analysis system capable of true color image analysis. The software used by this system is VIDAS Version 2.0. The following factors were evaluated: illumination, power supply, warming up, shading correction, averaging of image intake, hue luminance and saturation images and relation of illumination to quantification of area percentage (area %) of positively staining structures. The first six factors were evaluated by using a macro, with which it is possible to obtain information on variations over the image and over time. The last factor was evaluated by repeated measurement of area % of positive staining in a routinely processed tissue section. In our setting, stability of illumination and warmup time of the camera appeared to be the most important factors with influence on the performance of the image analysis system.

Color↗
PubMed1993

Rupture of an aortic aneurysm caused by Haemophilus influenzae type B infection.

A patient was operated for a contained rupture of an aortic aneurysm that appeared to be infected with Haemophilus influenzae type b. Reports on this species as a cause of infection and rupturation of an atherosclerotic aneurysm are extremely rare and we therefore describe this case. Apparently the risk of bacteraemia and the possible effects of it in patients with an aneurysm should be considered in surgical decision-making and management.

Aged↗
PubMed1992

Specificity and affinity of monoclonal antibodies against carcinoembryonic antigen.

The binding specificities of 52 well-characterized monoclonal antibodies (Mabs) against carcinoembryonic antigen (CEA) from 12 different research groups were studied by immunohistochemistry and immuno flow cytometry. In addition, the binding constant for the interaction between Mab and CEA was determined by a solution-phase assay. Cryostat sections of colon carcinoma and normal colon, stomach, liver, pancreas, and spleen were studied by immunohistochemistry. Peripheral blood granulocytes, monocytes, and lymphocytes were assayed by immuno flow cytometry. The Mabs used here have previously been classified into five essentially nonoverlapping epitope groups (GOLD 1-5) (Cancer Res., 49: 4852-4858, 1989). Most Mabs cross-reacted with different normal tissues, ranging from highly cross-reactive Mabs (positive reaction with 8 of 9 discriminating tissues) to relatively specific Mabs (positive reaction with 1 of 9 discriminating tissues). Five Mabs (10%) were specific, reacting only with colon carcinoma, normal colon mucosa, and normal gastric foveola. There was a correlation between epitope group and binding specificity. Mabs with a high degree of CEA specificity almost exclusively belonged to epitope groups 1, 2, and 3, while highly cross-reactive Mabs belonged to epitope groups 4 and 5. There was no correlation between antibody specificity and affinity for CEA. Specific Mabs with high as well as low affinity were found.

Adult↗
PubMed1990

Prediction of relapse and survival in breast cancer patients by pS2 protein status.

Application of systemic adjuvant therapy for primary breast cancer patients requires a more accurate identification of patients at high risk for recurrence. We have quantitatively assessed the cytosolic levels of estrogen-regulated pS2 protein in tumors of 205 breast cancer patients (median follow-up, 47 mo). There were no significant associations between the level of pS2 protein and tumor size, lymph node status, and differentiation grade. Using length of relapse-free survival (RFS) and overall survival (OS) as end points, 11 ng of pS2 protein/mg of cytosol protein were found as the best cutoff level to discriminate between positive (pS2+) and negative (pS2-). Patients with pS2- tumors showed significantly shorter RFS and OS (P less than 0.0001) than patients with pS2+ tumors. Also after adjustment for tumor size, lymph node status, and estrogen receptor (ER) status, pS2 negativity was associated with earlier recurrence and death. Tumors positive for pS2 (55 of 205, 27%) were almost exclusively confined to the subclass of ER+ tumors (53 of 55, 96%). The death rate for patients with pS2+ tumors was one-tenth of the death rate for patients with pS2-/ER- tumors. In the patients with ER+ tumors, the prognostic power of the pS2 status was especially present in patients whose tumors were also positive for the progesterone receptor (5-yr RFS and OS, 85% and 97% for ER+/PgR+/pS2+ tumors compared with 50% and 54% for the patients with ER+/PgR+/pS2- tumors). In patients with axillary lymph node involvement (N+), pS2 status could discriminate strongly between a good and bad prognosis group (5-yr RFS and OS, 65% and 88% for N+/pS2+ compared with 32% and 34% for N+/pS2-). A similar phenomenon was observed in patients without axillary lymph node involvement (5-yr RFS and OS, 89% and 95% for N0/pS2+ compared with 58% and 82% for N0/pS2-). We conclude that the pS2 status of human primary breast tumors is an important variable for the identification of patients at high risk for recurrence and death. Knowledge of the cytosolic pS2 status appeared of particular importance to identify patients at high risk in the ER+/PgR+ subclass of tumors, and in both the N0 and N+ subclasses of patients.

Adult↗
PubMed1990

An immunohistologic study of the feto-acinar pancreatic protein (FAP) in the normal pancreas, chronic pancreatitis, pancreatic adenocarcinoma, and intraabdominal metastases of adenocarcinomas.

The immunohistologic distribution of the feto-acinar pancreatic protein (FAP), detected by the monoclonal antibody (MoAb) J28 using an indirect immunoperoxidase technique, is described. Tests were carried out on normal adult pancreas (n = 10), chronic pancreatitis (n = 14), pancreatic adenocarcinoma (n = 17), intraabdominal metastases of pancreatic and nonpancreatic origin (n = 22), metastatic tumors invading the pancreas (n = 3), nonpancreatic fetal (n = 39) and adult (n = 65) normal organs (n = 104), and nonpancreatic malignancies (n = 145). All sections were formalin fixed and paraffin embedded. In the normal pancreas, only a few positive acinar cells were found around some islets of Langerhans. In pancreatitis there was an increased expression of FAP protein in the acinar tissue in relation to inflammatory changes. In cases of primary pancreatic adenocarcinoma and metastatic tumors in the pancreas, a strong expression of FAP protein in the peritumoral acinar area was found. The tumors themselves were FAP protein negative, as were the nonpancreatic tumors and normal organs. It can be concluded that FAP protein, detected by MoAb J28 in tissue sections, is specific for pancreatic exocrine tissue with reactive changes.

Adenocarcinoma↗
PubMed1988

Carcinoembryonic antigen in primary and metastatic ovarian tumors.

The immunoperoxidase method and an absorbed monospecific commercial rabbit anti-CEA antiserum were used to detect CEA in 105 primary ovarian tumors and 12 metastatic ovarian adenocarcinomas of intestinal origin. Primary ovarian tumors showed CEA in foci of squamous differentiation in 9 out of 10 cases of endometrioid carcinomas and focally in areas of intestinal differentiation in 21 out of 28 mucinous tumors as well as 4 out of 5 Brenner tumors. All of the serous tumors, clear cell carcinomas, and undifferentiated carcinomas as well as 19 of the 22 mucinous tumors without intestinal differentiation lacked CEA. All metastatic ovarian adenocarcinomas showed characteristic diffuse staining of CEA. Differences in CEA staining were found to be useful for histological differentiation between primary ovarian cancers and metastatic ovarian adenocarcinomas of intestinal origin. Furthermore, these data might be helpful in the selection of patients for serial CEA evaluation.

Adenocarcinoma↗
PubMed1988

Immunohistochemistry of CEA in the human pancreas during development, in the adult, chronic pancreatitis, and pancreatic adenocarcinoma.

This study describes the immunohistologic distribution of carcinoembryonic antigen (CEA) in 30 fetal pancreata, 5 normal adult pancreata, 11 cases of chronic pancreatitis without carcinoma, 16 cases of chronic pancreatitis with carcinoma, and 20 cases of primary pancreatic adenocarcinoma. The position of CEA-cross-reacting antigen, especially of nonspecific cross-reacting antigen (NCA), was also studied in the case of chronic pancreatitis and pancreatic adenocarcinoma. For this purpose, both monospecific antibodies to CEA and NCA, as well as cross-reacting antibodies, were used in an indirect immunoperoxidase technique. CEA reactivity could not be detected, neither during pancreatic development nor in chronic pancreatitis with or without associated adenocarcinoma. In 15 of 20 pancreatic adenocarcinomas, CEA positivity was found both with membranous and cytoplasmic localization. With the use of the cross-reacting antibodies, all cases of chronic pancreatitis and pancreatic adenocarcinomas showed positive staining of both ductal and tubular structures. Antibodies to NCA closely mimicked the results obtained with the cross-reacting antibodies both in pancreatitis and adenocarcinoma. From the authors' results it can be concluded that CEA is not a developmental antigen of the pancreas. Furthermore, NCA cross-activity of anti-CEA antibodies is an important reason of false positive reaction in chronic pancreatitis. Moreover, true CEA positivity in the pancreas appears to be restricted to adenocarcinoma of the exocrine pancreas.

Adenocarcinoma↗
PubMed1988

Tumor markers for ovarian cancer. A comparative immunohistochemical and immunocytochemical study of two commercial monoclonal antibodies (OV632 and OC125).

A comparative immunohistologic and immunocytologic study was performed to assess the immunoreactivity of the monoclonal antibodies OC125 and OV632, both directed at antigens present on epithelial ovarian tumors. OC125 reacted with 53 of 59 ovarian carcinomas, 20 of 20 uterine carcinomas, and 25 of 111 nongynecologic tumors (including 20 of 38 breast carcinomas). OV632 was demonstrated in 47 of 59 ovarian carcinomas, 11 of 20 uterine carcinomas, and only 7 of 111 nongynecologic tumors. With OV632 no reactivity was found in carcinomas of the breast or the gastrointestinal tract. Cytologic preparations of malignant effusions of patients with ovarian cancer showed reactivity with OC125 in 32 of 35 cases, and OV632 with positivity in 34 of 35 cases. Mesothelial cells in reactive effusions were OC125 positive in 16 of 20 cases but never showed positivity with OV632. The authors conclude that for histopathology a combination of OC125 and OV632 offers high sensitivity (0.86) and specificity (0.89) for ovarian cancer. For cytology, OV632 is the most specific tumor marker available.

Antibodies, Monoclonal↗