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Recombinant Proteins
Recombinant Human HSPA1B/HSP70-2 Protein, also known as heat shock protein 70-2 (HSP70-2), is a highly conserved molecular chaperone protein that is found in all living organisms. It is encoded by the HSPA1B gene in humans and is a member of the heat shock protein 70 family. This protein plays a crucial role in cellular protection and stress response by facilitating the folding, assembly, and transportation of other proteins.
The recombinant form of HSPA1B/HSP70-2 protein is produced through genetic engineering techniques, where the gene for this protein is inserted into a suitable expression system, such as bacteria or yeast. The resulting protein is identical to the native human HSP70-2 protein in terms of structure and function.
The structure of HSP70-2 protein consists of three major domains: the N-terminal ATPase domain, the substrate-binding domain, and the C-terminal domain. The ATPase domain is responsible for the ATPase activity of the protein, which is essential for its chaperone function. The substrate-binding domain is responsible for binding to unfolded or misfolded proteins, while the C-terminal domain is involved in protein-protein interactions and regulation of the chaperone activity.
The main activity of HSP70-2 protein is its role as a molecular chaperone. It assists in the folding and unfolding of proteins, prevents aggregation of misfolded proteins, and helps in the degradation of damaged proteins. HSP70-2 protein also plays a crucial role in cellular stress response, as it is induced in response to various stressors, such as heat, oxidative stress, and exposure to toxins.
One of the key functions of HSP70-2 protein is its ability to bind to hydrophobic regions of proteins, preventing their aggregation and promoting their correct folding. This activity is essential for maintaining protein homeostasis and preventing the accumulation of misfolded or damaged proteins, which can lead to cellular dysfunction and disease.
The recombinant form of HSPA1B/HSP70-2 protein has various applications in both research and therapeutic settings. In research, this protein is widely used as a tool for studying protein folding, chaperone activity, and stress response. It is also used in protein purification and as a molecular tag for protein expression and detection.
In therapeutic settings, HSP70-2 protein has shown potential as a therapeutic target for various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Its chaperone activity can be harnessed to prevent protein misfolding and aggregation, which are common features of these diseases. Additionally, the induction of HSP70-2 expression has been shown to have protective effects against cellular stressors, making it a potential therapeutic strategy for various conditions.
Furthermore, HSP70-2 protein has been used in vaccine development as an antigen carrier. Its ability to bind to a wide range of proteins makes it an ideal carrier for delivering antigens to immune cells, thereby enhancing the immune response. This has been demonstrated in pre-clinical studies for vaccines against infectious diseases and cancer.
In summary, Recombinant Human HSPA1B/HSP70-2 Protein is a highly conserved molecular chaperone with diverse functions in cellular protection and stress response. Its recombinant form has various applications in research and therapeutics, making it a valuable tool in the field of biotechnology. Further studies on the structure and function of this protein may lead to new insights and potential therapeutic
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