Anti-CD10 / Membrane metalloendopeptidase / MME, clone MME/12800R

0.2 mg/ml in 1X PBS with 0.05% BSA, 0.05% sodium azide. MME Antibody recognizes Membrane metalloendopeptidase, also known as CD10, Neprilysin, Neutral endopeptidase, and Common acute lymphoblastic leukemia antigen. Membrane metalloendopeptidase is a zinc-dependent cell surface metalloprotease encoded by the MME gene and is widely expressed in epithelial tissues, certain lymphoid populations, and specialized stromal cells. MME antibody targets a type II transmembrane glycoprotein localized primarily to the plasma membrane, where it functions in the proteolytic processing of bioactive peptides.Membrane metalloendopeptidase plays a critical role in degrading a broad range of regulatory peptides including enkephalins, substance P, atrial natriuretic peptide, bradykinin, and endothelin. Through this enzymatic activity, CD10 antibody is frequently used in studies of neuropeptide signaling, cardiovascular regulation, and inflammatory pathways. In the kidney, Membrane metalloendopeptidase is strongly expressed in proximal tubular epithelial cells, while in the intestine it localizes to the brush border of enterocytes. Expression is also observed in certain hematopoietic precursors and germinal center B cells.MME antibody is widely applied in diagnostic pathology because CD10 expression serves as an important marker in hematologic and solid malignancies. In lymphoid neoplasms, CD10 antibody staining helps identify follicular lymphoma and subsets of diffuse large B-cell lymphoma. In solid tumors, Membrane metalloendopeptidase expression assists in the characterization of renal cell carcinoma, endometrial stromal tumors, and selected carcinomas of breast and prostate origin. The membranous staining pattern typically reflects its role as a cell surface enzyme.At the molecular level, Membrane metalloendopeptidase contains an extracellular catalytic domain with zinc-binding motifs characteristic of the M13 family of metalloproteases. Dysregulation of MME expression has been associated with tumor progression, altered peptide signaling, and changes in the tumor microenvironment. Because of its defined membrane localization and established clinical relevance, MME antibody provides a reliable tool for assessing CD10 expression in normal tissues and neoplastic lesions. Clone MME/12800R is designed to detect Membrane metalloendopeptidase expression in research applications, supporting investigations in oncology, renal biology, immunology, and peptide metabolism.