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"Name": "Intended Use",
"Value": "Anti-PRAME (EPR20330) Rabbit Monoclonal Primary Antibody (anti-PRAME (EPR20330) antibody) is intended for laboratory use in the qualitative immunohistochemical detection of PRAME by light microscopy in sections of formalin-fixed, paraffin-embedded tissue stained on a BenchMark IHC/ISH instrument.
This product should be interpreted by a qualified pathologist in conjunction with histological examination, relevant clinical information, and proper controls.
This antibody is intended for in vitro diagnostic (IVD) use.",
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"Value": "Preferentially expressed antigen in melanoma (PRAME) is a 58 kDa cancer testis antigen and is located on chromosome 22 (22q11.22).1 First characterized in 1997, the PRAME gene encodes the human leucocyte antigen HLA-A24.2,3 PRAME is typically not expressed in normal human tissues, with the exception of testes, though limited expression in ovary, placenta, adrenal gland, and endometrium has been observed.2,4 Cellular expression of PRAME has been detected in the nuclear and cytoplasmic compartments as well as on the cell membrane.5-8 The variance in cellular distribution is not understood; however, different epitopes of the PRAME gene may be disparately expressed depending on cell type and physiological condition.8 Under normal physiological conditions, PRAME is a transcriptional regulator involved in germline development and gametogenesis.9 Beyond embryogenesis, the function of PRAME in normal human tissues is not yet well understood. When overexpressed, PRAME is a dominant repressor of retinoic acid receptor signaling and inhibits retinoic acid-induced differentiation, growth arrest, and apoptosis; contributing to tumorigenesis.5
Melanocytic neoplasms are a heterogeneous group of lesions that include benign and malignant tumors, which are categorized and subtyped according to the World Health Organization guidelines.10,11 PRAME is generally overexpressed in melanomas (i.e., malignant melanocytic tumors). When immunoreactivity is considered diffuse (i.e., nuclear staining in > 75% of tumor cells), PRAME expression has been observed in 50-100% of malignant melanomas, excluding desmoplastic subtypes.4,13-17,20,22-25 Additional studies have reported 92% and 94% of malignant melanoma cases expressed PRAME, although the threshold for positivity was lower (i.e., nuclear staining in 50% and 60% of tumor cells).18,19
Benign nevi are clonal proliferations of melanocytic cells with mutated oncogenes that are often considered simulators of melanoma with low malignant potential.10,11 The majority of benign nevi lack nuclear PRAME staining; although, some of these melanocytic lesions exhibit what is described as focal immunoreactivity (i.e., ≤ 75% nuclear staining in tumor cells). When > 75% is used as the threshold for positivity, 90-100% of benign nevi specimens are either negative or focally positive for PRAME.4,13,14,16,18,20,21,24,25,27-30
Therefore, the detection of PRAME by IHC with anti-PRAME (EPR20330) antibody may be used as an aid to differentiate between benign and malignant melanocytic neoplasms. This antibody may complement findings from routinely used H&E and ancillary IHC panels.
1. Hermes N, Kewitz S, Staege MS. Preferentially Expressed Antigen in Melanoma (PRAME) and the PRAME Family of Leucine-Rich Repeat Proteins. Curr Cancer Drug Targets. 2016;16(5):400-414.
2. Ikeda H, Lethé B, Lehmann F, et al. Characterization of an Antigen That Is Recognized on a Melanoma Showing Partial HLA Loss by CTL Expressing an NK Inhibitory Receptor. Immunity. 1997;6(2):199-208.
3. Xu Y, Zou R, Wang J, et al. The Role of the Cancer Testis Antigen PRAME in Tumorigenesis and Immunotherapy in Human Cancer. Cell Prolif. 2020;53(3).
4. Lezcano C, Jungbluth AA, Nehal KS, et al. PRAME Expression in Melanocytic Tumors. Am J Surg Pathol. 2018;42(11):1456-1465.
5. Epping MT, Wang L, Edel MJ, et al. The Human Tumor Antigen PRAME Is a Dominant Repressor of Retinoic Acid Receptor Signaling. Cell. 2005;122(6):835-847.
6. Proto-Siqueira R, Figueiredo-Pontes LL, Panepucci RA, et al. PRAME Is a Membrane and Cytoplasmic Protein Aberrantly Expressed in Chronic Lymphocytic Leukemia and Mantle Cell Lymphoma. Leuk Res. 2006;30(11):1333-1339.
7. Wadelin FR, Fulton J, Collins HM, et al. PRAME Is a Golgi-Targeted Protein That Associates with the Elongin BC Complex and Is Upregulated by Interferon-Gamma and Bacterial PAMPs. PLoS One. 2013;8(2):e58052-e58052.
8. Pankov D, Sjöström L, Kalidindi T, et al. In Vivo Immuno-Targeting of an Extracellular Epitope of Membrane Bound Preferentially Expressed Antigen in Melanoma (PRAME). Oncotarget. 2017;8(39):65917-65931.
9. Kern CH, Yang M, Liu WS. The PRAME Family of Cancer Testis Antigens Is Essential for Germline clinics Development and Gametogenesis†. Biol Reprod. 2021;105(2):290-304.
10. Elder D, Massi D, Scolyer R, et al. WHO (2018) Classification of Skin Tumors. Vol 11. 4 ed. Lyon France: LWW; 2018.
11. Ferrara G, Argenziano G. The WHO 2018 Classification of Cutaneous Melanocytic Neoplasms: Suggestions from Routine Practice. Front Oncol. 2021;11.
12. Lezcano C, Jungbluth AA, Busam KJ. PRAME Immunohistochemistry as an Ancillary Test for the Assessment of Melanocytic Lesions. Surg Pathol Clin. 2021;14(2):165-175.
13. Googe PB, Flanigan KL, Miedema JR. Preferentially Expressed Antigen in Melanoma Immunostaining in a Series of Melanocytic Neoplasms. Am J Dermatopathol. 2021;43(11):794-800.
14. Alomari AK, Tharp AW, Umphress B, et al. The Utility of PRAME Immunohistochemistry in the Evaluation of Challenging Melanocytic Tumors. J Cutan Pathol. 2021.
15. Lezcano C, Jungbluth AA, Busam KJ. Comparison of Immunohistochemistry for PRAME with Cytogenetic Test Results in the Evaluation of Challenging Melanocytic Tumors. Am J Surg Pathol. 2020;44(7):893-900.
16. Gassenmaier M, Hahn M, Metzler G, et al. Diffuse PRAME Expression Is Highly Specific for Thin Melanomas in the Distinction from Severely Dysplastic Nevi but Does Not Distinguish Metastasizing from Non-Metastasizing Thin Melanomas. Cancers. 2021;13(15).
17. Tio D, Willemsen M, Krebbers G, et al. Differential Expression of Cancer Testis Antigens on Lentigo Maligna and Lentigo Maligna Melanoma. Am J Dermatopathol. 2020;42(8):625-627.
18. Raghavan SS, Wang JY, Kwok S, et al. PRAME Expression in Melanocytic Proliferations with Intermediate Histopathologic or Spitzoid Features. J Cutan Pathol. 2020;47(12):1123-1131.
19. Gradecki SE, Valdes-Rodriguez R, Wick MR, et al. PRAME Immunohistochemistry as an Adjunct for Diagnosis and Histological Margin Assessment in Lentigo Maligna. Histopathology. 2021;78(7):1000-1008.
20. Šekoranja D, Hawlina G, Pižem J. PRAME Expression in Melanocytic Lesions of the Conjunctiva. Histopathology. 2021.
21. LeBlanc RE, Miller DM, Zegans ME. PRAME Immunohistochemistry Is Useful in the Evaluation of Conjunctival Melanomas, Nevi, and Primary Acquired Melanosis. J Cutan Pathol. 2021.
22. Toyama A, Siegel L, Nelson AC, et al. Analyses of Molecular and Histopathologic Features and Expression of PRAME by Immunohistochemistry in Mucosal Melanomas. Mod Pathol. 2019;32(12):1727-1733.
23. Lezcano C, Müller AM, Frosina D, et al. Immunohistochemical Detection of Cancer-Testis Antigen PRAME. Int J Surg Pathol. 2021.
24. See SHC, Finkelman BS, Yeldandi AV. The Diagnostic Utility of PRAME and p16 in Distinguishing Nodal Nevi from Nodal Metastatic Melanoma. Pathol Res Pract. 2020;216(9).
25. Lezcano C, Pulitzer M, Moy AP, et al. Immunohistochemistry for PRAME in the Distinction of Nodal Nevi from Metastatic Melanoma. Am J Surg Pathol. 2020;44(4):503-508.
26. Gradecki SE, Slingluff CL, Jr., Gru AA. PRAME Expression in 155 Cases of Metastatic Melanoma. J Cutan Pathol. 2021;48(4):479-485.
27. Lohman ME, Steen AJ, Grekin RC, et al. The Utility of PRAME Staining in Identifying Malignant Transformation of Melanocytic Nevi. J Cutan Pathol. 2021;48(7):856-862.
28. Parra O, Lefferts JA, Tafe LJ, et al. Cross-Reactivity of NRASQ61R Antibody in a Subset of Spitz Nevi with 11p Gain: A Potential Confounding Factor in the Era of Pathway-Based Diagnostic Approach. Hum Pathol. 2021;112:35-47.
29. Umano GR, Errico ME, D’Onofrio V, et al. The Challenge of Melanocytic Lesions in Pediatric Patients: Clinical-Pathological Findings and the Diagnostic Value of PRAME. Front Oncol. 2021;11.
30. Ruby KN, Li Z, Yan S. Aberrant Expression of HMB45 and Negative PRAME Expression in Halo Nevi. J Cutan Pathol. 2021;48(4):519-525.",
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"Value": "Anti-PRAME (EPR20330) antibody binds to the PRAME antigen in formalin-fixed, paraffin-embedded (FFPE) tissue sections. This antibody can be visualized using OptiView DAB IHC Detection Kit (Cat. No. 760-700 / 06396500001), ultraView Universal Alkaline Phosphatase Red Detection Kit (Cat. No. 760-501/ 05269814001) or ultraView Universal DAB Detection Kit (Cat. No. 760-500 / 05269806001). Refer to the respective method sheet for further information.",
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"Value": "Mat. No. 09592237001
Anti-PRAME (EPR20330) antibody contains sufficient reagent for 50 tests.
One 5 mL dispenser of anti-PRAME (EPR20330) antibody contains approximately 58.5 μg of a rabbit monoclonal antibody.
Mat. No. 09592245001
Anti-PRAME (EPR20330) antibody contains sufficient reagent for 250 tests.
One 25 mL dispenser of anti-PRAME (EPR20330) antibody contains approximately 292.5 μg of a rabbit monoclonal antibody.
The antibody is diluted in 0.05 M Tris buffered saline, 0.01 M EDTA, 0.05% Brij-35 with 0.3% carrier protein and 0.05% sodium azide, a preservative.
Specific antibody concentration is approximately 11.7 μg/mL. There is no known non-specific antibody reactivity observed in this product.
Anti-PRAME (EPR20330) antibody is a recombinant species monoclonal antibody produced as purified cell culture supernatant.
Refer to the appropriate VENTANA detection kit method sheet for detailed descriptions of: Principle of the Procedure, Material and Methods, Specimen Collection and Preparation for Analysis, Quality Control Procedures, Troubleshooting, Interpretation of Results, and Limitations.",
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