GSTM2 Human

Glutathione S-Transferase MU 2 Human Recombinant

Recombinant human GSTM2, expressed in E. coli, is a purified protein with a His tag. This non-glycosylated polypeptide chain comprises 238 amino acids (with the His tag at the N-terminus) and has a molecular weight of 27.9kDa. The purification process employs proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7228
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

HAT1 Human

Histone Acetyltransferase 1 Human Recombinant

Recombinant human HAT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 343 amino acids (residues 20-341). With a molecular weight of 40.1 kDa, this protein is fused to a 21 amino acid His tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8474
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HNMT Human

Histamine N-Methyltransferase Human Recombinant

Recombinant human HNMT, with a 36-amino acid His-tag at its N-terminus, is produced in E. coli. This purified protein is a single, non-glycosylated polypeptide chain containing 328 amino acids (residues 1-292) with a molecular weight of 37 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8541
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

MAT2A Human

Methionine Adenosyltransferase II Alpha Human Recombinant

Recombinant human MAT2A, fused with a His tag (20 a.a.) at the N-terminus, is produced in E. coli. This results in a single, non-glycosylated polypeptide chain containing 415 amino acids with a molecular mass of 45.8 kDa. The purification of MAT2A is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9879
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

MAT2B Human

Methionine Adenosyltransferase II Beta Human Recombinant

Recombinant Human MAT2B, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 323 amino acids (1-323 a.a) with a molecular weight of 36.4 kDa. The protein is purified using standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9968
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

METTL1 Human

Methyltransferase Like 1 Human Recombinant

Recombinant Human METTL1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 296 amino acids (1-276a.a.) with a molecular weight of 33.6kDa. It features a 20 amino acid His-tag fused at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10096
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

METTL21A Human

Methyltransferase Like 21A Human Recombinant

Recombinant METTL21A Human, produced in E. coli, is a single polypeptide chain consisting of 149 amino acids (93-218) with a molecular weight of 17 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10158
Source
E.coli.
Appearance
A sterile, colorless solution.

MGAT2 Human

Mannoside Acetylglucosaminyltransferase 2 Human Recombinant

Recombinant human MGAT2 protein produced in E. coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (30-447a.a) with a molecular mass of 50 kDa. It is fused to a 21 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10221
Source
Escherichia Coli.
Appearance
Clear, sterile filtered solution.

NMNAT2 Human

Nicotinamide Nucleotide Adenylyltransferase 2 Human Recombinant

Recombinant human NMNAT2, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 327 amino acids (specifically, amino acids 1 to 307) and has a molecular weight of 36.6 kDa. A 20 amino acid His-tag is fused to the N-terminus of NMNAT2. The protein is then purified using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11421
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

NMT1 Human

N-Myristoyltransferase 1 Human Recombinant

NMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 59.2kDa. NMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11507
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
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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