Anti-LRRC1 / Leucine-rich repeat-containing protein 1

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. LRRC1 antibody detects Leucine-rich repeat-containing protein 1, a scaffolding protein that plays a crucial role in cell polarity, cytoskeletal organization, and signal transduction. LRRC1 is associated with tight junctions and regulates spatial organization of signaling complexes at the plasma membrane. The LRRC1 antibody is used in cell biology and epithelial research to study junctional assembly, polarity establishment, and cell adhesion.LRRC1 is encoded by the LRRC1 gene located on human chromosome 6p12.2. The protein is approximately 836 amino acids long and contains multiple leucine-rich repeats and coiled-coil regions that facilitate protein-protein interactions. LRRC1 localizes to cell-cell junctions, where it interacts with polarity regulators such as PAR6 and PARD3, forming complexes that define apical and basolateral membrane domains.The LRRC1 antibody detects a 95 kilodalton band by western blot and reveals junctional and cortical membrane staining under immunofluorescence. Through its interactions, LRRC1 maintains epithelial barrier integrity and contributes to asymmetric signaling required for tissue organization. In neurons, LRRC1 participates in axon guidance and synapse formation by coordinating polarity-related signaling.Dysregulation of LRRC1 expression has been associated with tumor progression, particularly in epithelial cancers, where loss of polarity contributes to invasiveness and metastasis. LRRC1 also influences cell migration by regulating cytoskeletal rearrangement and adhesion complex turnover. Studies indicate LRRC1 interacts with small GTPases, linking it to actin dynamics and vesicle trafficking.Because LRRC1 anchors polarity proteins and signaling regulators, it serves as a critical structural determinant of epithelial and neuronal architecture. NSJ Bioreagents provides a validated LRRC1 antibody optimized for its applications, supporting research into cell polarity, adhesion, and cancer biology.