CRIM1 (Cysteine-Rich Motor Neuron 1) is a transmembrane protein implicated in regulating cellular processes such as development, differentiation, and signaling. Initially identified for its role in motor neuron development, CRIM1 contains multiple cysteine-rich repeats and epidermal growth factor (EGF)-like domains, enabling interactions with growth factors like bone morphogenetic proteins (BMPs) and vascular endothelial growth factor (VEGF). These interactions modulate signaling pathways critical for organogenesis, angiogenesis, and tissue homeostasis. Dysregulation of CRIM1 has been linked to diseases, including cancers and kidney disorders, highlighting its biological significance.
CRIM1 antibodies are essential tools for studying its expression, localization, and function. They enable detection of CRIM1 in tissues (e.g., kidney, brain) and cell lines via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Specific antibodies targeting distinct epitopes (e.g., extracellular or intracellular domains) help elucidate CRIM1’s dual roles in membrane-bound and secreted forms. Research using CRIM1 antibodies has revealed its involvement in BMP signaling modulation, cell adhesion, and extracellular matrix remodeling. Recent studies also explore its potential as a biomarker or therapeutic target, particularly in cancers where CRIM1 overexpression correlates with metastasis or poor prognosis. Validation of antibody specificity via knockout controls or siRNA knockdown remains critical to ensure reliability in experimental models.