Phospho-PLN-S16 Rabbit pAb for WB and ELISA - P26678

Core Product Specifications and Parameters

Biological Background: Phospholamban Function and Localization

• Phospholamban (PLN) is a 6.1 kDa transmembrane phosphoprotein that reversibly inhibits SERCA2 Ca2+-ATPase in cardiac sarcoplasmic reticulum by reducing the pump's apparent Ca2+ affinity, thereby regulating cardiac contractility and relaxation (PubMed:28890335). Related references: PMID:28890335
• PLN preferentially binds the ATP-bound E1 conformation of SERCA2, which predominates at low diastolic Ca2+ concentrations, and disrupts allosteric activation by ATP to slow Ca2+ re-uptake during diastole.
• Beyond SERCA2, PLN also inhibits SERCA3 and has been implicated in calcium homeostasis in elongated spermatids and the thalamic reticular nucleus, potentially affecting germ cell differentiation and sleep/wake behaviors.
• PLN phosphorylation at Ser16 (and Thr17) by protein kinases such as PKA and CaMKII reverses SERCA2 inhibition, serving as a critical regulatory node in β-adrenergic signaling and cardiac contractility.
• Subcellularly, PLN resides in the sarcoplasmic/endoplasmic reticulum membrane and the mitochondrial membrane, anchoring its regulatory functions in calcium-handling organelles.
• PLN is expressed predominantly in heart muscle; mutations in PLN cause inherited cardiomyopathies including dilated cardiomyopathy (CMD1P) and hypertrophic cardiomyopathy (CMH18).
• The protein undergoes multiple covalent modifications—palmitoylation, acetylation, and phosphorylation—that influence its oligomeric state, membrane anchoring, and regulatory activity.

Experimental Guidance and Technical Tips

• The immunogen is a synthetic phosphopeptide corresponding to residues around Ser16 of human PLN; this design enriches for antibodies recognizing the phosphorylated epitope. For ELISA and Western blot, consider using non-phosphorylated peptide or phosphatase-treated lysates as negative controls to confirm phosphorylation specificity.
• Due to the low molecular weight of PLN (~6 kDa), standard SDS-PAGE conditions may not resolve the protein efficiently; high-percentage gels (e.g., 15–20%) or Tricine-SDS-PAGE are recommended for Western blot detection.
• The antibody cross-reacts with mouse and rat PLN as indicated; validate detection of endogenous phosphorylated PLN in cardiac tissue lysates from these species, as PLN is highly expressed in heart.
• For ELISA, the rabbit polyclonal nature may provide sensitive capture/detection; however, lot-to-lot consistency should be verified for quantitative assays.
• Since PLN phosphorylation is dynamically regulated, appropriate sample preparation with phosphatase inhibitors is essential to preserve the phospho-S16 signal.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers and researchers with streamlined access to high-quality IVD raw materials, including phosphorylation-specific antibodies like this anti-phospho-PLN-S16 pAb. Our comprehensive portfolio supports cardiovascular biomarker development with validated antibody pairs, bulk ancillary reagents, and custom sourcing for rare targets, helping you accelerate assay development from concept to clinic.