AKAP7 Human

AKAP7 is known for its ability to bind to the regulatory subunit (RII) of PKA, facilitating the localization of the kinase to discrete locations within the cell. This interaction is mediated through a conserved domain known as the dimerization and docking (D/D) domain . AKAP7 has several isoforms, including AKAP7α, AKAP7β, AKAP7γ, and AKAP7δ, which arise from alternative splicing events .

The AKAP7 gene has undergone significant evolutionary changes. The ancestral AKAP7 splice variant is AKAP7α, while the long form AKAP7γ is also considered ancestral. The formation of AKAP7δ is a more recent event, observed in rodents and early primates . This evolutionary adaptation highlights the importance of AKAP7 in various physiological processes across different species.

AKAP7 is involved in several critical cellular functions:

• Neuronal and Cardiac Function: AKAP7 isoforms are vital components of neuronal and cardiac phosphatase complexes, ion channels, and cardiac Ca²⁺ handling .
• Renal Water Transport: AKAP7 plays a role in the regulation of renal water transport, contributing to the maintenance of water balance in the body .

Recombinant human AKAP7 is produced using E. coli expression systems. The recombinant protein typically includes an N-terminal His-tag and corresponds to the amino acids 1-81 of human AKAP7 . This recombinant form is used in various research applications to study the protein’s function and interactions.

Recombinant AKAP7 is utilized in studies focusing on:

• Protein-Protein Interactions: Understanding how AKAP7 interacts with other proteins, particularly PKA, to regulate cellular processes.
• Signal Transduction: Investigating the role of AKAP7 in cAMP signaling pathways and its impact on cellular functions.
• Disease Mechanisms: Exploring the involvement of AKAP7 in diseases related to its functional roles, such as cardiac disorders and neurological conditions.