ART4 Human

ADP-Ribosyltransferase 4 Human Recombinant

ART4, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain comprising 248 amino acids (residues 47-285) with a molecular weight of 28.8 kDa. It should be noted that on SDS-PAGE, the apparent molecular weight might range from 28 to 40 kDa. The protein is expressed with a 9-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2603
Source

Sf9, Insect cells.

Appearance
A clear, sterile-filtered solution.

AS3MT Human

Arsenic Methyltransferase Human Recombinant

Recombinant human AS3MT, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 399 amino acids, with amino acids 1 to 375 representing the AS3MT sequence, and has a molecular weight of 44.3 kDa. The protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2709
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

FUT7 Human

Fucosyltransferase 7 Human Recombinant

Recombinant human FUT7, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 329 amino acids (residues 37-342) and possessing a molecular weight of 37.9 kDa. This protein is tagged at the N-terminus with a 23 amino acid His-tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT3985
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

GALNT1 Human

Polypeptide N-Acetylgalactosaminyltransferase 1 Human Recombinant

Produced in Sf9 Insect cells, GALNT1 is a single, glycosylated polypeptide chain that consists of 528 amino acids (41-559a.a.) and has a molecular weight of 60.4kDa. A 9 amino acid His tag is present at the C-Terminus of GALNT1, which is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT4075
Source

Sf9, Insect cells.

Appearance

A clear, colorless solution that has been sterilized by filtration.

GALNT1 Mouse

Polypeptide N-Acetylgalactosaminyltransferase 1 Mouse Recombinant

Recombinant Mouse GALNT1 is produced in Sf9 insect cells. It is a single-chain polypeptide containing 528 amino acids (residues 41-559), with a predicted molecular weight of 60.5 kDa. The protein migrates at approximately 50-70 kDa on SDS-PAGE due to glycosylation. The recombinant protein includes a C-terminal 9-amino acid His-tag. It is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT4138
Source

Sf9, Insect cells.

Appearance

Clear, colorless, and sterile-filtered solution.

GALT Human

Galactose-1-Phosphate Uridylyltransferase Human Recombinant

GALT Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 403 amino acids (1-379) and having a molecular mass of 45.9 kDa. GALT is fused to a 24 amino acid His-tag at the N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4215
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

FDFT1 Human

Farnesyl-Diphosphate Farnesyltransferase 1 Human Recombinant

Recombinant human FDFT1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 306 amino acids (with amino acids 1-283 being the primary sequence) and has a molecular weight of 35.4 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3904
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

GAMT Human

Guanidinoacetate N-Methyltransferase Human Recombinant

Recombinant Human GAMT is a laboratory-produced protein based on the human GAMT enzyme. It is manufactured using E. coli bacteria and consists of a single polypeptide chain containing 256 amino acids. This non-glycosylated protein has a molecular weight of 28.4 kDa. For purification and detection purposes, a 20 amino acid His-Tag is attached to the N-terminus of the protein.
Shipped with Ice Packs
Cat. No.
BT4292
Source
Escherichia Coli.
Appearance
Clear and colorless solution that has been sterilized by filtration.

GATC Human

Glutamyl-TRNA Amidotransferase, Subunit C Human Recombinant

This product is a recombinant human GATC protein produced in E. coli. It is a single, non-glycosylated polypeptide chain that consists of 159 amino acids, with amino acids 1-136 representing the GATC sequence. The protein has a molecular mass of 17.5 kDa. However, its apparent size on SDS-PAGE may be higher due to the presence of a 23 amino acid His-tag at the N-terminus. The protein has been purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT4374
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized by filtration.

GATM Human

Glycine Amidinotransferase Human Recombinant

Recombinant human GATM, produced in E. coli, is a monomeric, non-glycosylated polypeptide chain comprising 410 amino acids (38-423). It has a molecular weight of 46.9 kDa. However, its apparent size on SDS-PAGE may be larger. The N-terminus of GATM is fused to a 24-amino acid His-tag. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4471
Source
E.coli.
Appearance
A clear, sterile-filtered 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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