Anti-ABHD5 Antibody

Product Details

Anti-ABHD5 antibody recognizes ABHD5, a lysophosphatidic acid acyltransferase that is involved in the production of phosphatidic acid, and thereby is also implicated in fatty acid synthesis, triacylglycerol storage, and cell signaling. Mutations in this gene are associated with Chanarin-Dorfman syndrome, a triglyceride storage disease.

ABHD5 binds to the lipid droplet protein Anti-ABHD5 antibody and is recruited to lipid droplets upon Mldp accumulation. Using BiFC to visualize interactions, we observed that ECFP-Abhd5 binding was proportional to Mldp concentration and supported FRET between the ECFP-Abhd5 donor and Mldp-EYFP acceptor in permeabilized cells (supplemental Fig. 1).

Anti-ABHD5 Antibody: Key Features and Uses

Furthermore, immunofluorescence of individual lipid droplets in cardiac myocytes showed that Abhd5 was enriched in a subset of lipid droplets. In addition, a human proteome microarray identified 271 proteins that interact with biotin-tagged ABHD5 (supplemental Fig. 6l). Among them, a lipid droplet scaffold protein called DPY30 was a strong candidate for interacting with ABHD5 (supplemental Fig. 7).

To determine if the Mldp-Abhd5 interaction is functionally important, 3T3-L1 cells were transfected with Mldp-EYFP and ECFP-Abhd5 singly and in combination, lipids were loaded overnight, and confocal microscopy was performed. Lipid droplets were identified by counterstaining with nile red, and Mldp-EYFP was highly targeted to clusters of lipid droplets whereas ECFP-Abhd5 accumulated in the perinuclear region (Fig. 8A and B). The Mldp-Abhd5 binding was abolished by expressing an Abhd5 mutant that lacks the E262K site required for Mldp interaction (E262K-Abhd5), and coexpression of wild type but not mutant Abhd5 significantly reduced neutral lipid accumulation in cellular assays (Fig. 8C and D).