Recombinant Human SSR1 Protein, N-His

Description of Recombinant Human SSR1 Protein, N-His

Introduction to Recombinant Human SSR1 Protein

Recombinant Human SSR1 Protein, also known as Signal Sequence Receptor 1, is a type I transmembrane glycoprotein that plays a crucial role in protein translocation and secretion in eukaryotic cells. It is a member of the signal recognition particle (SRP) receptor family and is encoded by the SSR1 gene located on chromosome 6 in humans.

Structure of Recombinant Human SSR1 Protein

The recombinant human SSR1 protein is composed of 3 domains: the N-terminal cytoplasmic domain, the transmembrane domain, and the C-terminal luminal domain. The N-terminal domain is responsible for binding to the SRP and the ribosome, while the transmembrane domain anchors the protein to the endoplasmic reticulum (ER) membrane. The C-terminal domain contains the signal peptidase cleavage site, which is essential for the release of the signal peptide from the nascent polypeptide chain during protein translocation.

The crystal structure of recombinant human SSR1 protein has been determined and consists of a compact globular structure with a central cavity. This cavity is believed to be the binding site for the signal peptide during protein translocation. The protein also contains several glycosylation sites, which are important for its stability and proper functioning.

Activity of Recombinant Human SSR1 Protein

Recombinant Human SSR1 Protein is primarily involved in the targeting and translocation of secretory proteins to the ER. It functions as a receptor for the SRP, a ribonucleoprotein complex that recognizes and binds to the signal peptide of nascent polypeptide chains. This interaction between SSR1 and SRP leads to the localization of the ribosome to the ER membrane, where the polypeptide chain is translocated across the membrane into the ER lumen.

In addition to its role in protein translocation, recombinant human SSR1 protein has also been shown to play a role in regulating the unfolded protein response (UPR). The UPR is a cellular stress response that is activated when there is an accumulation of misfolded proteins in the ER. SSR1 has been found to interact with the UPR regulator, GRP78, and may play a role in modulating the UPR signaling pathway.

Application of Recombinant Human SSR1 Protein

Recombinant Human SSR1 Protein has a wide range of applications in both research and therapeutic settings. One of the main applications is in the production of recombinant proteins for various biotechnological and pharmaceutical purposes. SSR1 is essential for the correct targeting and translocation of recombinant proteins into the ER, making it an important component in protein production systems.

Furthermore, SSR1 has been implicated in various diseases, including cancer and neurodegenerative disorders. Its involvement in the UPR pathway makes it a potential target for the development of new therapies for these diseases. In fact, there is ongoing research on the use of SSR1 inhibitors as a potential treatment for certain types of cancer.

Additionally, recombinant human SSR1 protein has also been used in diagnostic assays for various diseases. Antibodies against SSR1 can be used as biomarkers to detect aberrant protein secretion and ER stress in diseases such as diabetes and Alzheimer’s.

Conclusion

In conclusion, Recombinant Human SSR1 Protein is a crucial component in the protein translocation and secretion pathway. Its structure and activity make it an essential protein in various cellular processes, and its potential applications in research and therapeutics make it a valuable tool in the scientific community. Further studies on the role of SSR1 in disease pathogenesis may lead to the development of novel treatments for various disorders.