Recombinant Human MDA5/IFIH1 Protein, N-His

Description of Recombinant Human MDA5/IFIH1 Protein, N-His

Introduction to Recombinant Human MDA5/IFIH1 Protein

Recombinant Human MDA5/IFIH1 Protein, also known as Melanoma Differentiation-Associated Protein 5 or Interferon-Induced Helicase C Domain-Containing Protein 1, is a type of protein that plays a crucial role in the innate immune response against viral infections. This protein is encoded by the IFIH1 gene and is a member of the RIG-I-like receptor (RLR) family. It is involved in the detection of viral RNA and activation of antiviral signaling pathways, making it a vital component of the immune system.

Structure of Recombinant Human MDA5/IFIH1 Protein

The Recombinant Human MDA5/IFIH1 Protein is a 1023 amino acid long protein with a molecular weight of approximately 114 kDa. It contains a helicase domain at the N-terminus, which is responsible for its ability to bind and unwind double-stranded RNA (dsRNA). This is followed by a central DExD/H-box helicase domain and a C-terminal domain that is involved in protein-protein interactions. The protein also has a CARD domain, which is essential for its signaling function. Overall, the structure of Recombinant Human MDA5/IFIH1 Protein is well conserved among species, indicating its importance in the immune system.

Activity of Recombinant Human MDA5/IFIH1 Protein

Recombinant Human MDA5/IFIH1 Protein is a key component of the innate immune response against viral infections. It is primarily expressed in immune cells such as dendritic cells, macrophages, and monocytes. Upon detection of viral RNA, the helicase domain of MDA5 binds to the dsRNA, leading to a conformational change and activation of the protein. This, in turn, triggers the formation of a signaling complex involving other proteins such as MAVS and TRAF3, leading to the production of type I interferons and pro-inflammatory cytokines. These molecules play a crucial role in activating the adaptive immune response and eliminating the viral infection.

Applications of Recombinant Human MDA5/IFIH1 Protein

The unique structure and activity of Recombinant Human MDA5/IFIH1 Protein make it a valuable tool in various research applications. One of the primary applications of this protein is in the study of viral infections and the immune response. Its role in detecting viral RNA and activating antiviral signaling pathways makes it a crucial player in understanding the mechanisms of viral pathogenesis. Additionally, Recombinant Human MDA5/IFIH1 Protein can also be used in drug discovery and development for antiviral therapies. By targeting this protein, researchers can potentially inhibit viral replication and reduce the severity of viral infections.

Moreover, Recombinant Human MDA5/IFIH1 Protein has also been studied in the context of autoimmune diseases. Mutations in the IFIH1 gene have been linked to the development of autoimmune disorders such as type 1 diabetes and systemic lupus erythematosus. By studying the structure and function of this protein, researchers can gain insights into the mechanisms underlying these diseases and potentially develop new treatments.

Conclusion

In summary, Recombinant Human MDA5/IFIH1 Protein is a crucial component of the innate immune response against viral infections. Its unique structure and activity make it a valuable tool in studying viral pathogenesis, drug discovery, and autoimmune diseases. With further research and understanding of this protein, we can potentially develop new therapeutic strategies to combat viral infections and autoimmune disorders.