The ABHD5 Picoband? antibody is a high-affinity, rabbit polyclonal antibody directed against human ABHD5. This antibody detects a 180 kDa protein, also known as ABHD5 (ADP-glucose dehydrogenase) or GAPDH, which is involved in the oxidative breakdown of polyunsaturated fatty acids. ABHD5 is expressed predominantly in the testis and adipose tissue, but is also found at low levels in liver, skin, kidney, and heart. ABHD5-dependent lipolysis is essential in both adipose tissue and other tissues, such as skeletal muscle. ABHD5-independent functions involve the interaction with other proteins and enzymes that affect lipid and energy homeostasis in different tissues of the body.

The carboxyl terminus of ABHD5 Picoband™ antibody contains the conserved HxxxxD sequence typical of acyltransferases and is therefore predicted to have enzymatic activity. Gosh et al. [25] initially reported that recombinant ABHD5 has acyl-CoA dependent lysophosphatidic acid acyltransferase (LPAAT) activity in the presence of cobalt chloride and adenyl phosphate.

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However, subsequent experiments using a recombinant mutant of ABHD5 that has a substitution of R299 for lysine showed no LPAAT activity, suggesting that the residue is not required for this function. Interestingly, a structural study found that arginine has a higher capacity for creating perturbations in phospholipid membranes than lysine due to its high pKa and five potential H-bond donors.

Studies of the lipolytic effect of ABHD5 have shown that it is essential for normal blood glucose and insulin homeostasis in mice and humans. Additionally, it is a key regulator of fatty acid metabolism and atherosclerosis in adipose tissue, liver, and heart muscle. Loss of ABHD5 leads to impaired lipolysis and TAG accumulation in adipose tissue, as well as to reduced TAG hydrolysis and release in heart and oxidatively challenged skeletal muscle.

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