Enzymes
Product List
GSTM5 Human, Active
Glutathione S-Transferase MU 5 Human Recombinant, Active
GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GSTO1 Human
Glutathione S-Transferase Omega 1 Human Recombinant
GSTO1 is fused with an amino-terminal hexahistidine tag having a total Mw of 36kDa and purified by proprietary chromatographic techniques.
GSTO1 Human Mutant
Glutathione S-Transferase Omega 1 Mutant Human Recombinant
GSTO1 Variant Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 241 amino acids fragment (1-241) having a total molecular mass of 36kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The GSTO1 is purified by proprietary chromatographic techniques.
GSTO2 Human
Glutathione S-Transferase Omega 2 Human Recombinant
GSTO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GSTP1 Human
Glutathione S-Transferase pi 1 Human Recombinant
GSTP1 Human Recombinant fused with 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids
(1-210 a.a.) And having a molecular mass of 27.4kDa.
The GSTP1 is purified by proprietary chromatographic techniques.
GSTP1 Mouse
Glutathione S-Transferase pi 1 Mouse Recombinant
GSTP2 Mouse
Glutathione S-Transferase pi 2 Mouse Recombinant
The GSTP2 is purified by proprietary chromatographic techniques.
GSTP2 Mouse, His
Glutathione S-Transferase pi 2 Mouse Recombinant, His Tag
GSTT1 Human
Glutathione S-Transferase Theta-1 Human Recombinant
The GSTT1 is purified by proprietary chromatographic techniques.
GSTT2 Human
Glutathione S-Transferase Theta-2 Human Recombinant
GSTT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
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 .
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 .
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 .
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 .
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 .
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 .
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 .
