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AntibodySystem
Recombinant Proteins
Recombinant Human ATF6 Protein is a highly specialized protein that plays a crucial role in the cellular stress response. This protein is a key regulator of the unfolded protein response (UPR), a cellular mechanism that is activated in response to the accumulation of misfolded proteins in the endoplasmic reticulum (ER). In this article, we will explore the structure, activity, and applications of this important protein.
The ATF6 protein is a transcription factor that belongs to the basic leucine zipper (bZIP) family. It is composed of 670 amino acids and has a molecular weight of approximately 78 kDa. The protein is composed of several functional domains, including a DNA-binding domain, a transmembrane domain, and a cytoplasmic domain.
The DNA-binding domain is responsible for binding to specific DNA sequences in the promoter regions of target genes. The transmembrane domain anchors the protein to the ER membrane, while the cytoplasmic domain is responsible for regulating the activity of the protein.
Under normal conditions, ATF6 is present in an inactive form in the ER membrane. However, when the ER is under stress, ATF6 is cleaved by specific enzymes, releasing the cytoplasmic domain into the cytoplasm. This activated form of ATF6 then translocates to the nucleus where it binds to specific DNA sequences and activates the transcription of genes involved in the UPR.
The main function of ATF6 is to upregulate the expression of chaperone proteins, which help in the proper folding of misfolded proteins in the ER. It also promotes the degradation of irreversibly misfolded proteins, preventing them from accumulating and causing cellular damage.
The unique structure and activity of Recombinant Human ATF6 Protein make it a valuable tool in various scientific applications. Some of the key applications of this protein include:
In conclusion, Recombinant Human ATF6 Protein is a crucial player in the cellular stress response. Its unique structure and activity make it a valuable tool for studying the UPR pathway and its applications in various fields of research. With further studies and advancements in technology, this protein has the potential to be a key target for therapeutic interventions in diseases associated with ER stress.
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