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AntibodySystem
Recombinant Proteins
Recombinant Human ELAC2 Protein, also known as Endoribonuclease ZC3H12A, is a protein that plays a crucial role in RNA processing and degradation. This protein is encoded by the ELAC2 gene and is highly conserved among different species, indicating its importance in cellular functions.
The primary structure of Recombinant Human ELAC2 Protein consists of 583 amino acids, with a predicted molecular weight of approximately 65 kDa. It contains a highly conserved zinc finger domain at its N-terminus, which is essential for its RNA binding and endoribonuclease activity. The C-terminus of the protein contains a putative nuclease domain, which is responsible for its catalytic activity.
The protein also has several functional domains, including a nuclear localization signal, a nuclear export signal, and a leucine-rich nuclear export signal, which facilitate its transport between the nucleus and cytoplasm. These domains play a crucial role in regulating the activity and localization of the protein within the cell.
Recombinant Human ELAC2 Protein is a multifunctional protein that is involved in various cellular processes. Its main function is to catalyze the endonucleolytic cleavage of single-stranded RNA, leading to its degradation. This activity is essential for maintaining the quality and quantity of RNA within the cell, as well as for regulating gene expression.
In addition to its role in RNA processing, Recombinant Human ELAC2 Protein has been shown to have endoribonuclease activity on double-stranded RNA, indicating its potential role in antiviral defense. It has also been implicated in DNA repair, cell cycle regulation, and apoptosis, highlighting its diverse functions within the cell.
The unique structure and activity of Recombinant Human ELAC2 Protein make it a valuable tool for various applications in the fields of molecular biology and biotechnology. One of its main applications is in the production of recombinant proteins. The protein’s endoribonuclease activity can be used to cleave off unwanted RNA sequences from recombinant mRNA, resulting in a more pure and functional protein product.
Recombinant Human ELAC2 Protein has also been used in RNA interference (RNAi) experiments to study gene function. Its ability to specifically target and degrade RNA makes it an ideal tool for silencing specific genes and studying their role in cellular processes.
Furthermore, Recombinant Human ELAC2 Protein has potential therapeutic applications. Mutations in the ELAC2 gene have been linked to the development of prostate cancer, and studies have shown that the protein’s overexpression can inhibit tumor growth. This suggests that Recombinant Human ELAC2 Protein could be used as a potential target for cancer therapy.
In summary, Recombinant Human ELAC2 Protein is a multifunctional protein with a unique structure and activity. Its role in RNA processing and degradation, as well as its potential involvement in other cellular processes, make it a valuable tool for various applications in the fields of molecular biology and biotechnology. With further research, this protein could also have therapeutic implications for diseases such as cancer.
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