PARVA Human

Parvin Alpha contains two calponin-homology (CH) domains, which are crucial for its function. These domains allow Parvin Alpha to bind to actin filaments, a key component of the cell’s cytoskeleton . The protein also interacts with integrin-linked protein kinase (ILK) and paxillin, which are involved in cell signaling and adhesion .

The N-terminus of Parvin Alpha has two nuclear localization signals and three potential SH3-binding sites, which are important for its localization and function within the cell . The protein’s structure allows it to play a significant role in the regulation of cell adhesion and cytoskeleton organization .

The PARVA gene is located on chromosome 11p15.3 and contains 13 exons . The gene produces multiple transcripts through the use of different polyadenylation signals. These transcripts encode a protein with a molecular mass of approximately 42.3 kDa .

Parvin Alpha is expressed in most tissues, with the highest expression levels observed in the kidney and heart . It is also expressed throughout mouse embryonic development, indicating its importance in early development .

Recombinant human Parvin Alpha is produced using various expression systems, including E. coli . The recombinant protein is often tagged with GST (Glutathione S-transferase) or His (Histidine) tags to facilitate purification and detection . The recombinant protein is typically lyophilized and can be stored at -20°C to -80°C for long-term stability .

Recombinant Parvin Alpha is used in various research applications, including studies on cell adhesion, cytoskeleton organization, and signal transduction. Its ability to bind actin and interact with other proteins makes it a valuable tool for understanding the molecular mechanisms underlying these processes .