POFUT1 Human

Protein O-Fucosyltransferase 1 Human Recombinant

Recombinant human POFUT1, expressed in E. coli, is a single polypeptide chain with a molecular weight of 43.7 kDa. This protein consists of 385 amino acids (residues 27-388) and includes a 23 amino acid His-tag fused to the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12159
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

POGLUT1 Human

Protein O-Glucosyltransferase 1 Human Recombinant

Recombinant human POGLUT1, expressed in Sf9 Baculovirus cells, is a non-glycosylated polypeptide chain. This single chain protein consists of 377 amino acids (24-392a.a) and exhibits a molecular weight of 44.5kDa. Under reducing conditions on SDS-PAGE, it migrates between 40-57kDa. The protein is fused with an 8 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12278
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

PRMT1 Human

Protein Arginine Methyltransferase 1 Human Recombinant

PRMT1 Human Recombinant, spanning amino acids 1 to 353, is expressed in E.Coli with an N-terminal His-MBP tag. This non-glycosylated polypeptide chain consists of 750 amino acids, resulting in a molecular weight of 84 kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12388
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

SHMT1 Human

Serine Hydroxymethyltransferase 1 Human Recombinant

Recombinant human SHMT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 503 amino acids (with amino acids 1-483 present) and has a molecular weight of 55.2 kDa. The protein includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13685
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

SULT2B1 Human

Sulfotransferase Family, Cytosolic, 2B, Member 1 Human Recombinant

SULT2B1 Human Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 365 amino acids (1-365 a.a.) with a molecular weight of 41.3 kDa. The protein undergoes purification using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT14776
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

THG1L Human

tRNA-Histidine Guanylyltransferase 1-Like Human Recombinant

Recombinant human THG1L, produced in E. coli, is a single polypeptide chain containing 292 amino acids (residues 30-298) with a molecular weight of 34.0 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.
BT14820
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TPST1 Human

Tyrosylprotein Sulfotransferase 1 Human Recombinant

Recombinant human TPST1, expressed in E. coli, is a non-glycosylated polypeptide chain. It consists of 369 amino acids (26-370 a.a), with a molecular weight of 42kDa. The protein includes a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14855
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TPST1 Human, sf9

Tyrosylprotein Sulfotransferase 1, sf9 Human Recombinant

Produced in Sf9 insect cells using a baculovirus expression system, TPST1 is a single, glycosylated polypeptide chain. It consists of 354 amino acids, with the mature protein sequence spanning from amino acid 26 to 370. TPST1 has a molecular weight of 40.6 kDa and migrates between 40-57 kDa on SDS-PAGE under reducing conditions due to glycosylation.
For purification purposes, TPST1 is expressed with a six-amino acid His tag at the C-terminus. The protein is then purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14917
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GSTM4 Human

Glutathione S-Transferase MU 4 Human Recombinant

Recombinant Human GSTM4, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 238 amino acids (1-218 a.a.). With a molecular weight of 27.7 kDa, it features a 20 amino acid His-Tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7389
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

GSTM5 Human

Glutathione S-Transferase MU 5 Human Recombinant

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 (1-218) and is fused to a 24 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7533
Source
E.coli.
Appearance
A 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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