Recombinant Human C1GALT1C1 Protein, N-His

Reference: YHN30701
Product nameRecombinant Human C1GALT1C1 Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight34.24 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeHis41-Asp318
Aliases /SynonymsC1Gal-T2, Core 1 beta1,3-galactosyltransferase 2, Core 1 beta3-galactosyltransferase-specific molecular chaperone, C38H2-L1, C1GALT1C1, COSMC, C38H2-like protein 1, Core 1 beta3-Gal-T2, C1GalT2, C1GALT1-specific chaperone 1
ReferenceYHN30701
NoteFor research use only.

Description of Recombinant Human C1GALT1C1 Protein, N-His

Introduction

Recombinant Human C1GALT1C1 Protein, also known as core 1 synthase, is a glycosyltransferase enzyme that plays a crucial role in the biosynthesis of O-glycans. This protein is encoded by the C1GALT1C1 gene and is involved in the transfer of N-acetylgalactosamine (GalNAc) to the core 1 structure of mucin-type O-glycans. In this article, we will discuss the structure, activity, and applications of Recombinant Human C1GALT1C1 Protein.

Structure of Recombinant Human C1GALT1C1 Protein

The Recombinant Human C1GALT1C1 Protein is a 50 kDa protein consisting of 435 amino acids. It contains a conserved glycosyltransferase domain and shares sequence homology with other members of the glycosyltransferase family. The structure of this protein has been determined by X-ray crystallography, which revealed that it adopts a GT-A fold, a common structural motif found in glycosyltransferases. It also contains a unique C-terminal domain that is essential for its activity.

Activity of Recombinant Human C1GALT1C1 Protein

The main activity of Recombinant Human C1GALT1C1 Protein is the transfer of GalNAc to the Tn antigen, a core 1 precursor structure found on mucin-type O-glycans. This transfer is essential for the biosynthesis of complex O-glycans, which play a critical role in cell signaling, immune response, and cell adhesion. The enzyme catalyzes the addition of GalNAc to the core 1 structure, resulting in the formation of the core 2 structure, a key intermediate in the biosynthesis of complex O-glycans.

Recombinant Human C1GALT1C1 Protein is also involved in the biosynthesis of Sda antigen, a type 2 precursor structure found on O-glycans. This protein catalyzes the addition of GalNAc to the Sd(a) antigen, resulting in the formation of the Sd(a) antigen, which is involved in cell adhesion and immune response. Additionally, this protein has been shown to play a role in the biosynthesis of blood group antigens, such as the ABO and Lewis antigens.

Applications of Recombinant Human C1GALT1C1 Protein

The unique activity of Recombinant Human C1GALT1C1 Protein makes it a valuable tool in various research and industrial applications. One of the main applications of this protein is in the study of O-glycosylation, a critical process that regulates many biological functions. Recombinant Human C1GALT1C1 Protein can be used to study the biosynthesis and structure of O-glycans, as well as their role in various biological processes.

Furthermore, this protein has potential therapeutic applications in the treatment of diseases associated with abnormal O-glycosylation, such as cancer and inflammatory disorders. Recombinant Human C1GALT1C1 Protein can be used to modify the O-glycosylation pattern of cells, which can alter their function and potentially lead to the development of novel therapeutics.

Another application of Recombinant Human C1GALT1C1 Protein is in the production of recombinant glycoproteins with improved glycosylation patterns. By modifying the O-glycosylation of proteins, it is possible to improve their stability, solubility, and biological activity. This can be particularly useful in the production of therapeutic proteins, as well as for the development of glycoengineered antibodies with enhanced effector functions.

Conclusion</h2

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