GSTM5 Human, Active

Glutathione S-Transferase MU 5 Human Recombinant, Active

Recombinant human GSTM5, produced in E. coli, is a single polypeptide chain with a molecular weight of 28.2 kDa. It consists of 242 amino acids, including a 24 amino acid His-tag at the N-terminus (amino acids 1-218). Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7639
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NMNAT1 Human, Active

Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant , Active

Recombinant Human NMNAT1, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 315 amino acids (specifically amino acids 1-279) and has a molecular weight of 36 kDa. This protein is fused to a 36 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11291
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NMNAT1 Mouse

Nicotinamide Nucleotide Adenylyltransferase 1 Mouse Recombinant

Recombinant NMNAT1 from Mouse, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 308 amino acids (1-285 a.a), resulting in a molecular weight of 34.7 kDa. The N-terminus of NMNAT1 is fused with a 23 amino acid His-tag. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11358
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PRMT1 Mouse

Protein Arginine Methyltransferase 1 Mouse Recombinant

Recombinant PRMT1 protein from mouse has been expressed in E. coli and purified to greater than 90% purity. This protein is fused to a His-MBP tag at the N-terminus and has a molecular weight of 84 kDa. It is supplied as a sterile, colorless solution in 40mM Tris-HCl pH 8.0, 100mM NaCl, 4mM MgCl2, 2mM DTT, and 40% glycerol.
Shipped with Ice Packs
Cat. No.
BT12472
Source
Escherichia Coli.
Appearance
Clear and colorless liquid

PRMT3 Human

Protein Arginine Methyltransferase 3 Human Recombinant

Recombinant human PRMT3 protein was expressed in E. coli as a non-glycosylated polypeptide chain with a molecular mass of 62.3 kDa. The protein contains 554 amino acids (1-531 a.a) and is fused to a 23 amino acid His-tag at the N-terminus. The protein was purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12538
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PRTFDC1 Human

Phosphoribosyl Transferase Domain Containing 1 Human Recombinant

Produced in E. coli, PRTFDC1 is a single, non-glycosylated polypeptide chain comprising 248 amino acids (1-225 a.a.) with a molecular weight of 28.1 kDa. The protein features a 23 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12663
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PSAT1 Human

Phosphoserine Aminotransferase 1 Human Recombinant

This product consists of the recombinant human PSAT1 protein, expressed in E. coli and purified to a high degree. The protein is a single, non-glycosylated polypeptide chain comprising 394 amino acids (residues 1-370) with a molecular weight of 42.9 kDa. A 24 amino acid His-tag is fused to the N-terminus to facilitate purification by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12733
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

QPCT Human

Glutaminyl-Peptide Cyclotransferase Human Recombinant

QPCT, produced using Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular weight of 38.7kDa. This protein consists of 339 amino acids, spanning from residue 29 to 361. The recombinant QPCT is engineered with a 6-amino acid His tag at its C-terminus. Purification is achieved through proprietary chromatographic techniques. On SDS-PAGE analysis, the molecular size of QPCT is expected to appear between 28-40kDa.
Shipped with Ice Packs
Cat. No.
BT12793
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ST6GAL1 Human

ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1 Human Recombinant

Recombinantly produced in E. coli, ST6GAL1 Human is a single, non-glycosylated polypeptide chain comprising 403 amino acids (27-406 a.a). With a molecular mass of 46kDa, it features a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13843
Source
Escherichia Coli.
Appearance
A sterile, colorless solution.

ST6GAL1 Human, sf9

ST6 Beta-Galactosamide Alpha-2,6-Sialyltranferase 1, sf9 Human Recombinant

ST6GAL1, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular weight of 44.6 kDa. It consists of 389 amino acids (27-406 a.a.). This protein is expressed with a 6-amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13923
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution that has been sterilized by filtration.
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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