It is a regulator of Ca2+-uptake by the sarcoplasmic reticulum, and achieves this by inhibition of the Ca2+-pump, SERCA2. Phosphorylation of particular residues in phospholamban blocks this inhibition of SERCA2, and thereby enhances Ca2+-uptake by the SR. This is critical to fight or flight stress responses. Over inhibition of SERCA function occurs in heart failure, and research to modify phospholamban function is being examined to find new ways to manage heart failure.
The scientific team at Badrilla were the first to produce phospho-specific antibodies to phospholamban (Drago & Colyer (1994) J. Biol. Chem. 269, 25073–25077). These have become the gold-standards for phospholamban research and have been used in >200 papers. Badrilla now offers antibodies to three phosphorylated forms of phospholamban (PLB, PLN): phospho-Serine10 (PKC site), phospho-Ser16 (PKA, PKG site) and phospho-Threonine17 (CamKII, Akt site), and to the total protein (mAb A1).
NEW: Leeds students map scientific progress arising from key phospholamban antibodies. Browse the interactive graphic and discover key papers and contributions in popular areas of research including apoptosis, arrhythmia β-adrenergic stimulation, calcium handling, contractility, diabetes, heart failure, hypertension, hypertrophy, hypoxia, NOS and PLN phosphorylation signalling. Find out more.
Affinity purified rabbit polyclonal antibody specific to threonine-17 phosphorylated forms of phospholamban.
Rabbit polyclonal anti-serum specific to Thr-17 phosphorylated forms of phospholamban.
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