LIN7A Human

LIN7A comprises one L27 domain and one PDZ (DHR) domain . These domains are crucial for its function in cellular processes. The L27 domain is involved in protein-protein interactions, while the PDZ domain plays a role in binding to specific sequences in other proteins, facilitating the formation of protein complexes at the cell membrane .

LIN7A is expressed in various tissues, including the brain, testis, kidney, placenta, and liver . Its expression in these tissues suggests a role in diverse physiological processes. For instance, in the brain, LIN7A is involved in synaptic function and neuronal signaling .

The primary function of LIN7A is to maintain the polarized distribution of membrane proteins. This is essential for the proper functioning of epithelial cells and neurons. By interacting with other proteins, LIN7A helps to anchor channels and receptors at specific locations on the cell membrane, ensuring that they are correctly positioned to carry out their functions .

Recombinant LIN7A is produced in Escherichia coli and is a single, non-glycosylated polypeptide chain containing 256 amino acids, with a molecular mass of 28.4 kDa . It is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification using chromatographic techniques . The recombinant protein is typically used in research to study its function and interactions with other proteins.

Recombinant LIN7A is valuable in various research applications, including:

• Protein-protein interaction studies: Understanding how LIN7A interacts with other proteins can provide insights into its role in cellular processes.
• Functional assays: Investigating the effects of LIN7A on cell polarity and membrane protein distribution.
• Structural studies: Analyzing the structure of LIN7A to understand the mechanisms underlying its function.

Recombinant LIN7A should be stored at 4°C if used within 2-4 weeks. For longer storage, it should be frozen at -20°C, with the addition of a carrier protein (e.g., 0.1% HSA or BSA) to prevent degradation. It is important to avoid multiple freeze-thaw cycles to maintain the protein’s stability .