Recombinant Human HSPB7, N-His

Description of Recombinant Human HSPB7, N-His

Introduction to Recombinant Human HSPB7

Recombinant Human HSPB7, also known as Heat Shock Protein Beta-7, is a protein that belongs to the family of small heat shock proteins. It is encoded by the HSPB7 gene and is highly conserved across different species. This protein is involved in various cellular processes, including stress response, protein folding, and cytoskeletal organization. Recombinant Human HSPB7 is produced through recombinant DNA technology and has shown promising potential in various applications.

Structure of Recombinant Human HSPB7

Recombinant Human HSPB7 is a small protein with a molecular weight of approximately 20 kDa. It consists of 175 amino acids and has a highly conserved alpha-crystallin domain, which is characteristic of small heat shock proteins. This domain is responsible for the chaperone activity of HSPB7, which helps in the proper folding and stabilization of other proteins.

In addition to the alpha-crystallin domain, Recombinant Human HSPB7 also has a C-terminal extension, which is unique to this protein. This extension is believed to play a role in the interaction of HSPB7 with other proteins and in regulating its activity. The three-dimensional structure of Recombinant Human HSPB7 has been determined through X-ray crystallography, revealing a dimeric structure with two alpha-crystallin domains in each monomer.

Activity of Recombinant Human HSPB7

The main activity of Recombinant Human HSPB7 is its chaperone function, which helps in maintaining protein homeostasis in the cell. This protein is induced in response to cellular stress, such as heat shock, oxidative stress, and exposure to toxic substances. It acts as a molecular chaperone by binding to misfolded or denatured proteins and preventing their aggregation. This not only helps in the proper folding of these proteins but also protects them from degradation.

In addition to its chaperone activity, Recombinant Human HSPB7 has also been shown to have a role in cytoskeletal organization. It interacts with actin and tubulin, two important components of the cytoskeleton, and has been found to regulate their assembly and disassembly. This suggests that Recombinant Human HSPB7 may play a role in maintaining the structural integrity of the cell.

Applications of Recombinant Human HSPB7

Recombinant Human HSPB7 has shown potential in various applications, particularly in the field of medicine. Its chaperone activity makes it a promising candidate for the treatment of protein misfolding diseases, such as Alzheimer’s and Parkinson’s. By preventing the aggregation of misfolded proteins, Recombinant Human HSPB7 may help in slowing down the progression of these diseases.

Moreover, Recombinant Human HSPB7 has also been studied for its potential in cardioprotection. It has been shown to protect cardiac cells from stress-induced damage, making it a potential therapeutic target for heart diseases. In addition, studies have also suggested a role for Recombinant Human HSPB7 in cancer, as it has been found to regulate the activity of certain proteins involved in cell proliferation and survival.

Conclusion

In summary, Recombinant Human HSPB7 is a small heat shock protein with a highly conserved alpha-crystallin domain and a unique C-terminal extension. It acts as a chaperone and is involved in maintaining protein homeostasis and cytoskeletal organization. This protein has shown potential in various applications, including the treatment of protein misfolding diseases and heart diseases. Further research on Recombinant Human HSPB7 may uncover its full potential and lead to the development of novel therapies for various diseases.