Recombinant Human DNAJB2 Protein, N-GST & C-His

Description of Recombinant Human DNAJB2 Protein, N-GST & C-His

Introduction to Recombinant Human DNAJB2 Protein

Recombinant Human DNAJB2 Protein, also known as DnaJ homolog subfamily B member 2, is a heat shock protein that plays an important role in protein folding and quality control. This protein is encoded by the DNAJB2 gene and is found in various tissues and cell types, including the brain, heart, and skeletal muscle.

Structure of Recombinant Human DNAJB2 Protein

Recombinant Human DNAJB2 Protein is composed of 378 amino acids and has a molecular weight of approximately 42 kDa. It contains a J domain, which is responsible for its chaperone activity, and a C-terminal domain that is involved in protein-protein interactions.

The J domain of DNAJB2 is highly conserved among different species and is essential for its function as a co-chaperone. It binds to the ATPase domain of Hsp70, a major chaperone protein, and stimulates its ATPase activity, leading to efficient protein folding.

Activity of Recombinant Human DNAJB2 Protein

Recombinant Human DNAJB2 Protein has been shown to have chaperone activity, which is crucial for maintaining protein homeostasis in cells. It assists in the proper folding of newly synthesized proteins and prevents the aggregation of misfolded proteins.

In addition to its chaperone activity, DNAJB2 also plays a role in regulating the activity of other chaperone proteins. It has been shown to interact with Hsp70 and Hsp90, two major chaperones involved in protein folding, and modulate their activity.

Furthermore, DNAJB2 has been found to be involved in the degradation of misfolded proteins through the ubiquitin-proteasome pathway. It interacts with the E3 ubiquitin ligase CHIP and promotes the ubiquitination and subsequent degradation of misfolded proteins.

Application of Recombinant Human DNAJB2 Protein

Recombinant Human DNAJB2 Protein has a wide range of applications in both research and therapeutic settings. Its chaperone activity and involvement in protein quality control make it a valuable tool for studying protein folding and its role in diseases.

One of the main applications of DNAJB2 is in the production of recombinant proteins. It can be used as a co-chaperone to enhance the folding and solubility of recombinant proteins, leading to higher yields of functional proteins.

Moreover, DNAJB2 has been implicated in various diseases, including neurodegenerative disorders and cancer. Its role in protein quality control makes it a potential therapeutic target for these diseases. Recombinant Human DNAJB2 Protein can be used to study its function in disease models and to develop targeted therapies.

In addition, DNAJB2 has been found to be a potential biomarker for certain diseases. Its expression has been shown to be altered in various cancers and neurodegenerative disorders, making it a potential diagnostic and prognostic marker.

Conclusion

In summary, Recombinant Human DNAJB2 Protein is a crucial chaperone protein involved in protein folding and quality control. Its structure, activity, and various applications make it a valuable tool for studying protein folding and its role in diseases. Further research on this protein may lead to new insights into its function and potential therapeutic applications.