Anti-Phospholamban/PLN Antibody Picoband® Fluoro647 Conjugated

Phospholamban is a 52 amino acid integral membrane protein that regulates the Ca2+ pump in cardiac muscle and skeletal muscle cells. The subsequent activation of the Ca (2+) pump leads to enhanced muscle relaxation rates, thereby contributing to the inotropic response elicited in heart by beta-agonists. Phospholamban is also expressed in slow-twitch skeletal muscle and some smooth muscle cells. McTiernan et al. (1999) observed that human ventricle and quadriceps displayed high levels of phospholamban transcripts and proteins, with markedly lower expression observed in smooth muscles, while the right atrium also expressed low levels of phospholamban. The structure of the human phospholamban gene closely resembles that reported for chicken, rabbit, rat, and mouse. Comparison of the human to other mammalian phospholamban genes indicated a marked conservation of sequence for at least 217 bp upstream of the transcription start site.

ATPases, Calcium Channels, Calcium Signaling, Cancer, Cardiovascular, Cell Type Markers, Channels, Contractility, Metabolism, Plasma Membrane, Signal Transduction, Signaling Pathway, Vasculature

Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca (2+) . Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. .

1. Rodriguez P, Kranias EG (December 2005) . Phospholamban: a key determinant of cardiac function and dysfunction. Arch Mal Coeur Vaiss 98 (12) : 1239–43. 2. McTiernan, C. F.; Frye, C. S.; Lemster, B. H.; Kinder, E. A.; Ogletree-Hughes, M. L.; Moravec, C. S.; Feldman, A. M. : The human phospholamban gene: structure and expression. J. Molec. Cell Cardiol. 31: 679-692, 1999.

Sarcoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane ; Single- pass membrane protein . Endoplasmic reticulum membrane; Single-pass membrane protein.