ST3GAL5 Human

ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5 Human Recombinant

Recombinant human ST3GAL5, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 359 amino acids (83-418a.a). This protein has a molecular weight of 41 kDa and is fused to a 23 amino acid His-tag at its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13763
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

SULT1E1 Human

Estrogen Sulfotransferase Human Recombinant

Recombinant Human SULT1E1 is a protein engineered and produced in E. coli bacteria. This specific SULT1E1 variant is a single polypeptide chain that lacks glycosylation modifications. It encompasses 302 amino acids, with amino acids 1 to 294 representing the core SULT1E1 sequence. A 6-amino acid His Tag is attached to the C-terminus of the protein to facilitate purification. The molecular weight of this recombinant SULT1E1 is 36.1 kDa. It has been purified from E. coli cultures using standard chromatography methods.
Shipped with Ice Packs
Cat. No.
BT14368
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

SULT2A1 Human

Sulfotransferase Family, Cytosolic, 2A, Member 1 Human Recombinant

Recombinant human SULT2A1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 305 amino acids (1-285a.a), with a molecular weight of 35.9kDa. The protein includes a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14442
Source
Escherichia Coli.
Appearance
Clear, sterile filtered solution.

UGT8 Human

UDP Glycosyltransferase 8 Human Recombinant

This product consists of the recombinant human UGT8 protein, produced in E. coli bacteria. It is a single, non-glycosylated polypeptide chain composed of 544 amino acids (with amino acids 21 to 541 representing the UGT8 sequence) and has a molecular weight of 61.6kDa. The N-terminus of the protein is fused with a 23 amino acid His-tag.
Shipped with Ice Packs
Cat. No.
BT15503
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

UPRT Human

Uracil Phosphoribosyltransferase Human Recombinant

Recombinant human UPRT, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 332 amino acids (with residues 1-309 present) and possessing a molecular weight of 36.2 kDa. This protein is fused to a 23-amino acid His-tag at its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15580
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

XYLT2 Human

Xylosyltransferase 2 Human Recombinant

Recombinant Human XYLT2 is a single, glycosylated polypeptide chain. It consists of 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and has a molecular weight of 94.0kDa. This protein includes a N-terminal linker (2 additional amino acids), a C-terminal linker (2 additional amino acids), and a C-terminal His-tag (6 additional amino acids).

Shipped with Ice Packs
Cat. No.
BT15640
Source

HEK293 Cells.

Appearance
White, lyophilized (freeze-dried) powder that has been filtered.
Definition and Classification

Transferases are a class of enzymes that catalyze the transfer of specific functional groups (e.g., methyl, glycosyl) from one molecule (the donor) to another (the acceptor) . They are involved in numerous biochemical pathways and are integral to many of life’s essential processes. Transferases are classified under the EC 2 category in the Enzyme Commission (EC) numbering system, which includes over 450 unique enzymes . The classification is primarily based on the type of biochemical group transferred, such as acyl, glycosyl, methyl, and amino groups .

Biological Properties

Key Biological Properties: Transferases are ubiquitous in nature and play crucial roles in various cellular processes. They are involved in the metabolism of amino acids, carbohydrates, and lipids .

Expression Patterns: The expression of transferases can vary significantly depending on the tissue type and the physiological state of the organism. For example, certain transferases are highly expressed in the liver, where they participate in detoxification processes .

Tissue Distribution: Transferases are distributed across different tissues, with some being tissue-specific. For instance, glutathione S-transferases (GSTs) are predominantly found in the liver, kidneys, and intestines, where they help in detoxifying harmful compounds .

Biological Functions

Primary Biological Functions: Transferases facilitate the transfer of functional groups, which is essential for the synthesis and degradation of biomolecules. They play a pivotal role in metabolic pathways, including glycolysis, the citric acid cycle, and amino acid metabolism .

Role in Immune Responses and Pathogen Recognition: Some transferases, such as glycosyltransferases, are involved in the modification of glycoproteins and glycolipids, which are crucial for cell-cell recognition and immune responses . These modifications can help in the recognition and neutralization of pathogens .

Modes of Action

Mechanisms with Other Molecules and Cells: Transferases typically function by binding to both the donor and acceptor molecules, facilitating the transfer of the functional group. This process often involves the formation of a transient enzyme-substrate complex .

Binding Partners and Downstream Signaling Cascades: Transferases can interact with various binding partners, including coenzymes and other proteins. For example, aminotransferases require pyridoxal phosphate (PLP) as a coenzyme for their activity . These interactions can trigger downstream signaling cascades that regulate cellular functions .

Regulatory Mechanisms

Control of Expression and Activity: The expression and activity of transferases are tightly regulated at multiple levels. Transcriptional regulation involves specific transcription factors that bind to the promoter regions of transferase genes .

Post-Translational Modifications: Transferases can undergo various post-translational modifications, such as phosphorylation, acetylation, and glycosylation, which can modulate their activity and stability .

Applications

Biomedical Research: Transferases are widely used in biomedical research to study metabolic pathways and disease mechanisms. For instance, GSTs are used as biomarkers for oxidative stress and liver function .

Diagnostic Tools: Certain transferases, such as alanine aminotransferase (ALT) and aspartate aminotransferase (AST), are used as diagnostic markers for liver damage .

Therapeutic Strategies: Transferases are being explored as therapeutic targets for various diseases, including cancer and metabolic disorders. Inhibitors of specific transferases are being developed as potential drugs .

Role in the Life Cycle

Development to Aging and Disease: Transferases play critical roles throughout the life cycle. During development, they are involved in the synthesis of essential biomolecules and the regulation of metabolic pathways . In aging, changes in transferase activity can affect cellular homeostasis and contribute to age-related diseases . For example, decreased activity of certain transferases has been linked to neurodegenerative diseases .

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