Rabbit Polyclonal DRP1(Phospho-Ser637) Antibody

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     Western blot analysis of extracts from JK cells and K562 cells using DRP1 (Phospho-Ser637) Antibody P40541.The lane on the right is treated with the antigen-specific peptide.    

The DRP1 (Phospho-Ser637) antibody detects dynamin-related protein 1 (DRP1) when phosphorylated at serine residue 637. a post-translational modification critical for regulating mitochondrial dynamics. DRP1 is a GTPase responsible for mitochondrial fission, typically residing in the cytosol until recruited to mitochondrial membranes, where it oligomerizes to constrict and divide mitochondria. Its activity is tightly controlled by phosphorylation: phosphorylation at Ser637 (by protein kinase A, PKA, or Ca²⁺/calmodulin-dependent kinase II, CaMKII) inhibits DRP1’s GTPase activity, reducing mitochondrial fission and promoting fusion. Conversely, dephosphorylation by calcium-dependent phosphatases like calcineurin activates DRP1. This phosphorylation site is implicated in cellular responses to stress, metabolic changes, and apoptotic signals.

The DRP1 (Phospho-Ser637) antibody is widely used in research to study mitochondrial morphology, energy metabolism, and cell death pathways. It helps assess DRP1 activation status in diseases such as neurodegeneration (e.g., Alzheimer’s, Parkinson’s), cardiovascular disorders, and cancer. Applications include Western blotting, immunofluorescence, and immunoprecipitation to evaluate phosphorylation changes under experimental conditions (e.g., drug treatments, genetic manipulations). Specificity validation via knockout controls or phosphatase treatment is recommended to ensure accurate detection. Understanding DRP1 phosphorylation dynamics aids in exploring therapeutic strategies targeting mitochondrial dysfunction.