Recombinant Mouse ST6GALNAC2/SIAT7-B Protein, N-His

Description of Recombinant Mouse ST6GALNAC2/SIAT7-B Protein, N-His

Introduction

Recombinant Mouse ST6GALNAC2/SIAT7-B protein is a glycosyltransferase enzyme that plays a crucial role in the biosynthesis of sialylated glycoproteins. This protein is encoded by the ST6GALNAC2 gene and is also known as SIAT7-B due to its structural similarity to another sialyltransferase enzyme, SIAT7A. Recombinant Mouse ST6GALNAC2/SIAT7-B protein is widely used in various research fields, including cancer biology, immunology, and glycobiology.

Structure of Recombinant Mouse ST6GALNAC2/SIAT7-B Protein

Recombinant Mouse ST6GALNAC2/SIAT7-B protein is a type II transmembrane protein, meaning that it has a transmembrane domain that anchors it to the cell membrane. The protein consists of 365 amino acids and has a molecular weight of approximately 42 kDa. The primary structure of the protein contains a conserved sialyltransferase domain, which is responsible for its enzymatic activity. This domain is located in the cytoplasmic region of the protein and is followed by a transmembrane domain and a short cytoplasmic tail.

The crystal structure of Recombinant Mouse ST6GALNAC2/SIAT7-B protein has been determined, revealing a homodimeric structure with each monomer containing a catalytic domain and a sialylmotif domain. The catalytic domain is responsible for binding to the donor substrate CMP-Neu5Ac and the acceptor substrate, while the sialylmotif domain is involved in the recognition of the acceptor substrate.

Enzymatic Activity of Recombinant Mouse ST6GALNAC2/SIAT7-B Protein

Recombinant Mouse ST6GALNAC2/SIAT7-B protein is a sialyltransferase enzyme that catalyzes the transfer of sialic acid from the donor substrate CMP-Neu5Ac to the terminal galactose residue of the acceptor substrate. This enzymatic reaction results in the formation of sialylated glycoproteins, which play important roles in various biological processes, including cell adhesion, immune response, and signal transduction.

The enzymatic activity of Recombinant Mouse ST6GALNAC2/SIAT7-B protein has been extensively studied and characterized. It has been shown to have a broad substrate specificity, with the ability to transfer sialic acid to a variety of glycoproteins, including N-glycans and O-glycans. The enzyme also exhibits a preference for sialylating galactose residues that are located at the non-reducing end of the glycan chain.

Applications of Recombinant Mouse ST6GALNAC2/SIAT7-B Protein

Recombinant Mouse ST6GALNAC2/SIAT7-B protein has a wide range of applications in both basic and applied research. Its role in the biosynthesis of sialylated glycoproteins makes it a valuable tool in glycobiology research. The ability to produce sialylated glycoproteins in vitro using Recombinant Mouse ST6GALNAC2/SIAT7-B protein allows for the study of their structure and function, as well as their involvement in various biological processes.

One of the major applications of Recombinant Mouse ST6GALNAC2/SIAT7-B protein is in cancer research. Alterations in sialylation patterns have been observed in various types of cancer, and Recombinant Mouse ST6GALNAC2/SIAT7-B protein has been used to study the role of sialylation in cancer progression and metastasis. Additionally, the enzyme has been used to produce sialylated glycoproteins for use as cancer biomarkers and potential therapeutic targets.

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