RMDN3 antibodies are immunological reagents designed to detect and analyze the RMDN3 protein (UniProt ID: Q96TC7), which regulates endoplasmic reticulum (ER)-mitochondria contacts (MERCs), lipid radical transfer, and apoptosis. These antibodies are widely used in techniques such as Western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF) to study RMDN3's interactions, localization, and expression levels in diverse cellular contexts .
RMDN3 antibodies have been pivotal in elucidating how mitochondrial ROS (mtROS) upregulate MERCs via RMDN3-VAPB tethering. Key findings include:
Phosphorylation-Dependent Binding: mtROS induce phosphorylation of RMDN3 at threonine 160 (T160), enhancing its interaction with VAPB to form MERCs. Knockdown experiments using siRNA (validated by RMDN3 antibodies) showed that disrupting this interaction increases mitochondrial lipid radical accumulation and cell death .
Lipid Radical Transfer: The TPR domain of RMDN3 facilitates lipid radical transfer from mitochondria to the ER, as demonstrated by LipiRADICAL assays and liposome experiments .
Prostate and Keratinocyte Carcinomas: RMDN3 antibodies have detected overexpression in prostate cancer (PCa) and keratinocyte carcinomas, linked to CpG island hypomethylation and MAPK pathway dysregulation .
Therapeutic Target Potential: In acute myeloid leukemia, RMDN3 interacts with PTP1B to modulate apoptosis, highlighting its role as a biomarker or drug target .
RMDN3 antibodies reveal its dual role in apoptosis:
Pro-Survival: Under mitochondrial damage, RMDN3-VAPB tethering prevents ferroptosis by transferring lipid radicals to the ER .
Pro-Apoptotic: Overexpression in keratinocytes induces apoptosis, suggesting context-dependent functions .
In MELAS syndrome (mitochondrial encephalopathy), fibroblasts with high mtROS show stronger RMDN3-VAPB binding, implicating MERCs in mitochondrial disease pathology .
Kinase Identification: The kinase responsible for RMDN3 T160 phosphorylation remains unidentified. Antibody-based phosphoproteomics could resolve this .
Mechanistic Specificity: While RMDN3 transfers lipid radicals, its selectivity for oxidized lipids versus phosphatidic acid requires further study .