PPP3CA antibodies are immunoassays designed to detect protein phosphatase 3 catalytic subunit alpha (PPP3CA), also known as calcineurin Aα. This enzyme regulates calcium-dependent signaling cascades, impacting processes such as neuronal development, immune response, and muscle fiber differentiation .
Epilepsy: Truncating PPP3CA variants (e.g., p.Gln442Ter) reduce protein expression and cause constitutive calcineurin activation, linked to developmental and epileptic encephalopathy .
Cell Proliferation: Patient-derived lymphoblasts with PPP3CA frameshift variants show reduced wild-type PPP3CA protein levels and increased apoptosis .
Muscle Fiber Differentiation: PPP3CA regulates skeletal muscle fiber type conversion via NFAT signaling .
Osteoblast/Osteoclast Regulation: Critical for bone formation and resorption through osteoblast differentiation and NFATC1 signaling .
Unfolded Protein Response (UPR): Cells with truncated PPP3CA exhibit UPR activation, leading to apoptosis .
Isoform Imbalance: Splicing variants (e.g., c.1308_1311dupACTT) skew isoform expression ratios, affecting neural and muscular functions .
Antigen Retrieval: TE buffer (pH 9.0) or citrate buffer (pH 6.0) .
Staining: Detects PPP3CA in thyroid cancer and skeletal muscle tissues .
Orthogonal RNAseq: Confirms tissue-specific expression patterns .
qRT-PCR: Validates transcript levels in patient-derived cells .
Patient Studies:
Mechanistic Insights:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform, CAM-PRP catalytic subunit, Calmodulin-dependent calcineurin A subunit alpha isoform, PPP3CA, CALNA, CAN, CALN, CCN1, CNA1, PPP2B, CALNA1.
PPP3CA antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
PAT1E11AT.
Anti-human PPP3CA mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PPP3CA protein 1-511 amino acids purified from E. coli.
Mouse IgG2b heavy chain and k light chain.
Protein Phosphatase 3, also known as Calcineurin, is a calcium and calmodulin-dependent serine/threonine protein phosphatase. The alpha isozyme of the catalytic subunit of this enzyme is encoded by the PPP3CA gene. This enzyme plays a crucial role in various biological processes, including T-cell activation, synaptic vesicle recycling, and other calcium-mediated signaling pathways .
Calcineurin is a heterodimer composed of a catalytic subunit (Calcineurin A) and a regulatory subunit (Calcineurin B). The catalytic subunit, encoded by the PPP3CA gene, contains several functional domains, including a calmodulin-binding domain, an autoinhibitory domain, and a catalytic domain. The enzyme is activated by the binding of calcium ions and calmodulin, which induces a conformational change that relieves autoinhibition and allows substrate access to the catalytic site .
Calcineurin plays a pivotal role in the immune system by activating T-cells through the dephosphorylation of the nuclear factor of activated T-cells (NFAT). This process is essential for the transcription of interleukin-2 and other cytokines, which are critical for T-cell proliferation and differentiation . Additionally, Calcineurin is involved in synaptic plasticity and memory formation in the brain, making it a key player in neurobiology .
The mouse anti-human PPP3CA antibody is a monoclonal antibody that specifically targets the alpha isozyme of the catalytic subunit of Calcineurin. This antibody is commonly used in research to study the expression, localization, and function of Calcineurin in various tissues and cell types. It is particularly useful in techniques such as Western blotting, immunohistochemistry, and immunoprecipitation .