GSTO1 Human

Glutathione S-Transferase Omega 1 Human Recombinant

Recombinant human GSTO1, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 241 amino acids (fragment 1-241). This protein, with a molecular weight of 32.1 kDa, is fused with an amino-terminal hexahistidine tag, resulting in a total molecular weight of 36 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7701
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

GSTO1 Human Mutant

Glutathione S-Transferase Omega 1 Mutant Human Recombinant

Human GSTO1 exhibits several polymorphisms within its coding regions. One notable polymorphism results in an alanine-to-aspartate (A140D) substitution at amino acid position 140. This variant demonstrates reduced enzymatic activity in arsenic biotransformation.
Recombinant human GSTO1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 241 amino acids (fragment 1-241). It has a molecular mass of 36 kDa and includes a 4.5 kDa amino-terminal hexahistidine tag.
Purification of GSTO1 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7784
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

GSTO2 Human

Glutathione S-Transferase Omega 2 Human Recombinant

Recombinant human GSTO2, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 266 amino acids (residues 1-243) with a molecular weight of 30.6 kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7866
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

GSTP1 Human

Glutathione S-Transferase pi 1 Human Recombinant

GSTP1 Human Recombinant protein is produced in E. coli and fused with a 36 amino acid His tag at its N-terminus. This results in a single, non-glycosylated polypeptide chain containing 246 amino acids (1-210 a.a.) with a molecular mass of 27.4 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7949
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

GSTP1 Mouse

Glutathione S-Transferase pi 1 Mouse Recombinant

Recombinant Mouse GSTP1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 233 amino acids, comprising amino acids 1 to 210, and has a molecular weight of 26 kDa. This GSTP1 protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8038
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

HPRT1 Human, Active

Hypoxanthine-Guanine Phosphoribosyltransferase, Human Recombinant, Active

Recombinant Human HPRT1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 238 amino acids (1-218 a.a), resulting in a molecular weight of 26.7kDa. The protein is engineered with a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9128
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

GSTT1 Human

Glutathione S-Transferase Theta-1 Human Recombinant

Recombinant human GSTT1, expressed in E. coli and fused with a 37 amino acid His tag at the N-terminus, is available as a non-glycosylated polypeptide chain. This single-chain protein comprises 277 amino acids (1-240 a.a.) and exhibits a molecular weight of 31.5kDa. Purification of GSTT1 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8225
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GSTT2 Human

Glutathione S-Transferase Theta-2 Human Recombinant

Recombinant GSTT2, produced in E. coli, is a single polypeptide chain consisting of 264 amino acids (residues 1-244) with a molecular weight of 29.6 kDa. A 20 amino acid His-tag is fused to the N-terminus of GSTT2. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8302
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GSTZ1 Human

Glutathione Transferase Zeta 1 Human Recombinant

Recombinant human GSTZ1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 236 amino acids (1-216 a.a.) with a molecular weight of 26.2 kDa. The protein is engineered with a 20 amino acid His-Tag at the N-terminus and purified using conventional chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT8385
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

LCAT Human, HEK

Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK

Recombinant human LCAT, expressed in HEK cells, is a glycosylated polypeptide chain consisting of 429 amino acids (25-440). It includes a 13 amino acid Flag Tag at the N-terminus, resulting in a total molecular mass of 48.5 kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9556
Source
Human Embryonic Kidney 293 cells
Appearance
White powder, lyophilized and 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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