|Detection of Human PKA C by Western Blot. Western blot shows lysates of A549 human lung carcinoma cell line, HepG2 human hepatocellular carcinoma cell line, SW480 human colorectal adenocarcinoma cell line, MCF‑7 human breast cancer cell line, and MDA‑MB‑468 human breast cancer cell lines. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat PKA C Pan Specific Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4175) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for PKA C Pan Specific at approximately 42 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
The cAMP-dependent protein kinase (PKA) holoenzyme is composed of two regulatory and two catalytic subunits, designated PKA R and PKA C, respectively. Three catalytic subunit isoforms, C alpha, C beta, and C gamma, have been identified. Upon PKA R subunit binding to the second messenger cAMP, active PKA C subunits are released, initiating a phosphorylation cascade that regulates such cellular functions as metabolism, ion transport, and gene transcription.
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