Recombinant Human ALG13 Protein, N-His

Description of Recombinant Human ALG13 Protein, N-His

Introduction

Recombinant Human ALG13 Protein, also known as Alpha-1,3-glucosyltransferase ALG13, is a glycosyltransferase enzyme that plays a crucial role in the biosynthesis of N-linked glycoproteins. It is encoded by the ALG13 gene and is highly conserved among eukaryotic organisms. Recombinant Human ALG13 Protein is widely used in various research fields, such as glycobiology, cell biology, and biotechnology, due to its unique structure and diverse functions.

Structure of Recombinant Human ALG13 Protein

Recombinant Human ALG13 Protein is a type II transmembrane protein that consists of 382 amino acids. It has a molecular weight of approximately 43 kDa and is composed of multiple structural domains. The N-terminus of the protein contains a cytoplasmic domain, followed by a transmembrane domain, and a large luminal domain. The luminal domain of Recombinant Human ALG13 Protein has a conserved catalytic domain, which is responsible for its enzymatic activity.

Enzymatic Activity of Recombinant Human ALG13 Protein

Recombinant Human ALG13 Protein is a glycosyltransferase enzyme that catalyzes the transfer of glucose from UDP-glucose to the growing oligosaccharide chain of N-linked glycoproteins. This enzymatic activity is essential for the proper folding and function of glycoproteins, which are involved in a wide range of biological processes, including cell signaling, immune response, and protein trafficking.

The enzymatic activity of Recombinant Human ALG13 Protein is dependent on its interaction with other proteins, such as ALG14 and ALG2, which form a complex known as the ALG13/ALG14/ALG2 complex. This complex acts as a heterodimeric glycosyltransferase and plays a crucial role in the biosynthesis of N-linked glycoproteins.

Applications of Recombinant Human ALG13 Protein

Recombinant Human ALG13 Protein has a wide range of applications in various research fields. One of its major applications is in the study of glycobiology, where it is used to investigate the biosynthesis and function of N-linked glycoproteins. It is also used in cell biology studies to understand the role of glycosylation in cellular processes, such as protein folding, trafficking, and signaling.

In addition, Recombinant Human ALG13 Protein is used in biotechnology for the production of glycoprotein-based therapeutics. Its enzymatic activity is utilized in the in vitro glycosylation of recombinant proteins, which can improve their stability, solubility, and efficacy. This makes Recombinant Human ALG13 Protein a valuable tool for the development of novel glycoprotein-based drugs.

Furthermore, Recombinant Human ALG13 Protein has potential applications in the diagnosis and treatment of certain diseases. Mutations in the ALG13 gene have been linked to various disorders, such as congenital disorders of glycosylation and intellectual disabilities. Recombinant Human ALG13 Protein can be used to study these diseases and potentially develop targeted therapies.

Conclusion

In summary, Recombinant Human ALG13 Protein is a crucial enzyme that plays a vital role in the biosynthesis of N-linked glycoproteins. Its unique structure and enzymatic activity make it a valuable tool for studying glycobiology, cell biology, and biotechnology. With its potential applications in drug development and disease research, Recombinant Human ALG13 Protein continues to be an important protein in the scientific community.