Anti-TPD52 / Tumor protein D52

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. TPD52 antibody detects Tumor protein D52, a small coiled-coil protein that regulates vesicle trafficking, calcium-dependent exocytosis, and cell proliferation. Originally identified as an overexpressed antigen in breast carcinoma, TPD52 has since been linked to cancer progression, membrane trafficking, and secretory granule dynamics. The TPD52 antibody is widely used to study tumor biology, exocytosis, and intracellular vesicle regulation.TPD52 is encoded by the TPD52 gene located on human chromosome 8q21.13. The protein is approximately 25 kilodaltons and characterized by a central coiled-coil domain that mediates homo- and hetero-oligomerization with other D52-like proteins (TPD52L1 and TPD52L2). This interaction facilitates vesicle docking and fusion processes within the Golgi network and secretory pathway. Expression is highest in epithelial tissues, immune cells, and tumors with high metabolic activity.A TPD52 antibody detects a 25 kilodalton band in western blot analysis and reveals diffuse cytoplasmic and perinuclear staining in immunofluorescence assays. TPD52 associates with synaptotagmin-like proteins and small GTPases that control vesicle exocytosis, contributing to regulated secretion in endocrine and immune systems. Its upregulation enhances secretory granule release and cell motility, promoting oncogenic transformation and metastasis.In cancer biology, TPD52 is implicated in cell-cycle progression, lipid storage, and energy metabolism. Overexpression increases tumorigenicity by stimulating AKT signaling and inhibiting apoptosis. Conversely, TPD52 depletion suppresses proliferation and sensitizes cells to chemotherapeutic stress. Clinical studies have identified elevated TPD52 expression in breast, ovarian, lung, and prostate cancers, often correlating with poor prognosis and high metastatic potential.Beyond oncology, TPD52 participates in vesicle fusion during immune cell degranulation and insulin granule exocytosis, highlighting its role in both secretory and metabolic regulation. Phosphorylation by casein kinase 2 modulates its subcellular localization and protein-binding properties, linking signaling cues to vesicular transport efficiency. NSJ Bioreagents provides a validated TPD52 antibody validated for its applications, supporting research into vesicle dynamics, tumor progression, and secretory pathway regulation.