Phosphorylation-status of phospholamban and calsequestrin modifies their affinity towards commonly used antibodies.

@article{Huke2004PhosphorylationstatusOP,
  title={Phosphorylation-status of phospholamban and calsequestrin modifies their affinity towards commonly used antibodies.},
  author={Sabine Huke and Muthu Periasamy},
  journal={Journal of molecular and cellular cardiology},
  year={2004},
  volume={37 3},
  pages={795-9}
}
Phospholamban (PLB) and calsequestrin (CSQ) play important roles in sarcoplasmic reticulum Ca(2+) transport and storage in cardiac muscle. Specific antibodies have been frequently used to quantitate CSQ and PLB protein levels. Here we demonstrate that two of the commonly available anti-PLB antibodies, anti-PLB-2D12 and anti-PLB-A1, show lower reactivity to phosphorylated than dephosphorylated PLB. A custom anti-PLB antibody, generated using a peptide corresponding to amino acids 2-14, is not… CONTINUE READING