Human HSP110wt Recombinant Protein

Description of Human HSP110wt Recombinant Protein

The Structure of Human HSP110wt Recombinant Protein

Human HSP110wt recombinant protein is a member of the heat shock protein (HSP) family, which plays a crucial role in cellular stress response and protein homeostasis. This protein is encoded by the HSPH1 gene and is also known as heat shock 105kDa/110kDa protein 1 (HSP105/110) or heat shock protein 105 (HSP105). The protein has a molecular weight of approximately 105kDa and is composed of 938 amino acids.

The primary structure of human HSP110wt recombinant protein consists of three major domains: the N-terminal domain, the central domain, and the C-terminal domain. The N-terminal domain is responsible for the ATPase activity of the protein, which is essential for its chaperone function. The central domain contains the highly conserved HSP70-binding domain, which is responsible for the interaction with HSP70, a key player in protein folding and quality control. The C-terminal domain is involved in the oligomerization of HSP110wt and is essential for its chaperone activity.

The Activity of this protein

Human HSP110wt recombinant protein is a molecular chaperone that belongs to the HSP70 family. As a chaperone, it plays a crucial role in the folding, stabilization, and degradation of other proteins. This activity is essential for maintaining protein homeostasis and preventing the accumulation of misfolded or damaged proteins, which can lead to various diseases.

The main function of HSP110wt is to assist in the folding of newly synthesized proteins and to prevent the aggregation of misfolded proteins. It does this by binding to exposed hydrophobic regions of unfolded or misfolded proteins, preventing their aggregation and promoting their refolding. Additionally, HSP110wt can also interact with other chaperones, such as HSP70 and HSP40, to facilitate the folding of client proteins.

In addition to its chaperone activity, HSP110wt also has ATPase activity, which is essential for its chaperone function. This activity is responsible for the energy-dependent conformational changes that occur during the folding process and helps to stabilize the client protein in its native state.

The Application of Human HSP110wt Recombinant Protein

The unique structure and activity of human HSP110wt recombinant protein make it a promising drug target for various diseases. As a molecular chaperone, it has been shown to play a critical role in the development and progression of neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. Studies have also shown that HSP110wt is involved in the development of cancer, making it a potential target for cancer therapy.

In addition to its potential as a drug target, human HSP110wt recombinant protein also has various applications in research and biotechnology. Its chaperone activity makes it a valuable tool for protein folding studies and for the production of recombinant proteins with correct folding. It can also be used in the development of therapeutics for protein misfolding diseases.

In conclusion, human HSP110wt recombinant protein is a crucial member of the HSP family with a unique structure and activity. Its chaperone function and ATPase activity make it a promising drug target for various diseases, and its applications in research and biotechnology make it a valuable tool in the scientific community. Further research on this protein could lead to the development of novel therapeutics for a range of diseases and advance our understanding of protein folding and quality control mechanisms.