Recombinant Human C1GALT1C1 Protein, N-His

Description of Recombinant Human C1GALT1C1 Protein, N-His

Recombinant Human C1GALT1C1 Protein, also known as Core 1 Beta 3-Galactosyltransferase 1, is a type II transmembrane glycoprotein that is encoded by the C1GALT1C1 gene. This protein plays a crucial role in the biosynthesis of O-glycans, which are essential for the proper functioning of many glycoproteins. The structure of Recombinant Human C1GALT1C1 Protein has been extensively studied and is composed of 362 amino acids, with a predicted molecular weight of approximately 41 kDa.

The protein consists of three distinct domains: an N-terminal cytoplasmic domain, a transmembrane domain, and a C-terminal catalytic domain. The cytoplasmic domain contains a conserved motif that is responsible for the transfer of the sugar group from the donor molecule to the acceptor molecule. The transmembrane domain anchors the protein to the cell membrane, while the catalytic domain is responsible for the enzymatic activity of the protein.

Recombinant Human C1GALT1C1 Protein is a glycosyltransferase enzyme that catalyzes the transfer of a galactose sugar from a donor molecule to the core 1 structure of O-glycans. This activity is crucial for the proper glycosylation of many proteins, including mucins, which are important for cell adhesion, signaling, and immune response. The activity of Recombinant Human C1GALT1C1 Protein has been shown to be essential for the development and function of various tissues and organs, including the gastrointestinal tract, immune system, and reproductive system.

In addition to its role in O-glycan biosynthesis, Recombinant Human C1GALT1C1 Protein has also been shown to have a regulatory function in the immune response. Studies have demonstrated that this protein can modulate the activity of immune cells, such as T-cells and natural killer cells, by altering the glycosylation patterns of their surface receptors. This activity has been linked to the regulation of immune cell activation, differentiation, and function.

The unique structure and activity of Recombinant Human C1GALT1C1 Protein make it a valuable tool in various research and biotechnology applications. One of the most significant applications of this protein is in the production of recombinant glycoproteins with enhanced functionality. By modifying the glycosylation patterns of these proteins, researchers can improve their stability, solubility, and biological activity, making them more suitable for therapeutic use.

Another potential application of Recombinant Human C1GALT1C1 Protein is in the development of vaccines. The protein has been shown to be an important antigen in the immune response against various pathogens, including bacteria and viruses. By using this protein as a vaccine antigen, researchers can potentially enhance the immune response and improve the efficacy of vaccines.

Furthermore, Recombinant Human C1GALT1C1 Protein has also been studied for its potential role in cancer research. Alterations in O-glycosylation patterns have been observed in various types of cancer, and studies have shown that this protein may play a role in these changes. By understanding the role of Recombinant Human C1GALT1C1 Protein in cancer, researchers can potentially develop new diagnostic and therapeutic strategies for this disease.

In conclusion, Recombinant Human C1GALT1C1 Protein is a crucial enzyme involved in the biosynthesis of O-glycans, with a unique structure and activity. Its diverse functions in various biological processes make it a valuable tool in research and biotechnology. Further studies on this protein may lead to new insights into its role in health and disease, as well as potential applications in medicine.