Recombinant Phospholamban antibody (pSer16)

Catalog No. ABIN7879712

This Rabbit Monoclonal antibody specifically detects Phospholamban in WB. It exhibits reactivity toward Human and Mouse.

Quick Overview for Recombinant Phospholamban antibody (pSer16) (ABIN7879712)

Target: Phospholamban (PLN)

Antibody Type: Recombinant Antibody

Reactivity: Human, Mouse

Host: Rabbit

Clonality: Monoclonal

Conjugate: This Phospholamban antibody is un-conjugated

Application: Western Blotting (WB)

Clone: 32P55

Product Details anti-Phospholamban Antibody

Binding Specificity: pSer16

Purpose: Phospho-Phospholamban (S16) Antibody / PLN

Purification: Affinity-chromatography

Immunogen: A synthesized peptide derived from human Phospho-Phospholamban (S16) was used as the immunogen for the Phospho-Phospholamban (S16) antibody.

Isotype: IgG

Application Details

Application Notes: Optimal dilution of the Phospho-Phospholamban (S16) antibody should be determined by the researcher.

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Rabbit IgG in phosphate buffered saline, pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol, 0.4-0.5 mg/mL BSA

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: Store the Phospho-Phospholamban (S16) antibody at -20oC.

Target Details for Phospholamban

Target: Phospholamban (PLN)

Alternative Name: Phospholamban

Background: Phospho-Phospholamban (S16) antibody detects PHOSPHOLAMBAN, encoded by the PLN gene, when phosphorylated at serine 16. Alternate names include cardiac phospholamban, PLB, and phospholamban phosphoprotein. PHOSPHOLAMBAN is a small transmembrane protein in the sarcoplasmic reticulum of cardiac and skeletal muscle. It regulates SERCA2a, the sarcoplasmic reticulum Ca2+ ATPase responsible for calcium uptake during muscle relaxation. In its unphosphorylated state, PHOSPHOLAMBAN inhibits SERCA2a. Phosphorylation at serine 16 by PKA relieves this inhibition, enhancing calcium uptake, promoting relaxation, and increasing cardiac contractility.

Phospho-Phospholamban (S16) antibody is widely applied in cardiovascular biology, muscle physiology, and signaling research. By detecting phosphorylation at serine 16, researchers can study how beta adrenergic signaling enhances cardiac output through PKA mediated regulation of calcium cycling. This site specific antibody allows distinction between active and inhibited PHOSPHOLAMBAN, providing insights into heart function under physiological and pathological conditions.

Applications include western blotting, immunohistochemistry, immunofluorescence, and ELISA. Western blot assays detect phosphorylated PHOSPHOLAMBAN in heart lysates, immunohistochemistry maps phosphorylation in cardiac tissue sections, and immunofluorescence highlights localization in sarcoplasmic reticulum. ELISA assays allow quantification of phosphorylation status in experimental models. These techniques provide direct evidence of cardiac signaling events.

Dysregulation of PHOSPHOLAMBAN phosphorylation contributes to heart failure, arrhythmias, and cardiomyopathies. Mutations in PLN cause inherited dilated cardiomyopathy and arrhythmogenic right ventricular cardiomyopathy. Monitoring serine 16 phosphorylation provides biomarkers for disease progression and therapy efficacy. By applying Phospho-Phospholamban (S16) antibody, scientists can investigate how altered signaling leads to impaired cardiac relaxation and contractility.

Phosphorylation of PHOSPHOLAMBAN is also studied in exercise physiology, where beta adrenergic stimulation enhances contractility. The antibody supports research into how training, drugs, and genetic variants influence calcium cycling. Translational applications include evaluation of therapeutic interventions targeting SERCA2a regulation, such as gene therapy or pharmacologic modulators. NSJ Bioreagents offers Phospho-Phospholamban (S16) antibody with validated specificity, supporting robust research into cardiac physiology and disease.

UniProt: P26678

Pathways: Negative Regulation of Transporter Activity