A fully validated, highly specific affinity purified rabbit antibody to threonine-17 phosphorylated forms of phospholamban

Phospholamban (PLB/PLN) is a small transmembrane protein which plays an important role in controlling the activity of the sarcoplasmic reticulum ATPase (SERCA2a) of cardiac muscle during calcium sequestration.

Phospholamban is phosphorylated on separate amino acid residues by cAMP-dependent, and cGMP-dependent (Ser-16) and Ca²⁺/CaM-dependent (threonine-17) protein kinases in response to β-adrenergic stimulation. Akt has also been shown to phosphorylate threonine-17. The result is an increased calcium pump activity which reduces the time course of the calcium transient, increases the calcium load in the sarcoplasmic reticulum, and consequently, produces a larger calcium transient at the next action potential. However, alteration in this homeostatic interaction has been shown to result in heart failure.

Tested applications: Western blot (1:5000 dilution), IHC microscopy (1:200 dilution).