HNMT Human, Active

Histamine N-Methyltransferase Human Recombinant, Active

Recombinant human HNMT, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 328 amino acids (with the mature protein encompassing residues 1-292) and has a molecular weight of 37.4 kDa. The protein includes a 36 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT8961
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

HPRT1 Human

Hypoxanthine-Guanine Phosphoribosyltransferase Human Recombinant

Recombinant Human HPRT1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 238 amino acids (with positions 1 through 218 being the active amino acids) and has a molecular weight of 26.7 kDa. A 20 amino acid His-Tag is fused to the N-terminus of the HPRT1. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9048
Source
Escherichia Coli.
Appearance
A clear and colorless solution that has been sterilized by filtration.

TPST2 Human

Tyrosylprotein Sulfotransferase 2 Human Recombinant

Recombinant human TPST2 protein was expressed in E. coli and purified to a single, non-glycosylated polypeptide chain. The protein contains 375 amino acids (residues 26-377) with a molecular weight of 41 kDa. It includes a 23 amino acid His-tag fused at the N-terminus to facilitate purification.
Shipped with Ice Packs
Cat. No.
BT14965
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

TPST2 Human, sf9

Tyrosylprotein Sulfotransferase 2, sf9 Human Recombinant

TPST2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 361 amino acids (26-377 a.a.) with a molecular mass of 40.4kDa. It migrates at 40-57kDa on SDS-PAGE under reducing conditions. TPST2 is expressed with a 6 amino acid His tag at the C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15044
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

TRDMT1 Human

tRNA Aspartic Acid Methyltransferase 1 Human Recombinant

Recombinant Human TRDMT1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 415 amino acids (1-391). It has a molecular weight of 47.2 kDa. 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.
BT15123
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TRPT1 Human

tRNA Phosphotransferase 1 Human Recombinant

Recombinant human TRPT1, expressed in E. coli, is available as a single, non-glycosylated polypeptide chain. It consists of 277 amino acids (residues 1-253) and has a molecular weight of 30.3 kDa. The protein includes a 24-amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15183
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

TSTD1 Human

Thiosulfate Sulfurtransferase Like Domain Containing 1 Human Recombinant

Recombinant human TSTD1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 135 amino acids (1-115 a.a.) and having a molecular mass of 14.6kDa. The TSTD1 protein is fused to a 20 amino acid His tag at the N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15268
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution

MGAT2 Human, Sf9

Mannoside Acetylglucosaminyltransferase 2 Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, MGAT2 is a single, glycosylated polypeptide chain that contains 427 amino acids (specifically, amino acids 30 to 447) and has a molecular mass of 49.3 kDa. It's important to note that on SDS-PAGE, the molecular size will appear to be between 40 kDa and 57 kDa. MGAT2 is engineered with a 6 amino acid His tag at its C-Terminus and undergoes purification using specialized chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10317
Source

Sf9, Baculovirus cells.

Appearance

The product is a colorless solution that has been sterilized by filtration.

MGMT Human

O-6-Methylguanine-DNA Methyltransferase Human Recombinant

This product consists of recombinant human MGMT, with an N-terminal 20 amino acid His Tag, produced in E. coli. It exists as a single, non-glycosylated polypeptide chain comprising 227 amino acids (residues 1-207) and possesses a molecular weight of 23.8 kDa. The purification of MGMT is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10458
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.

MMAB Human

Methylmalonic Aciduria Type B Human Recombinant

Recombinant Human MMAB, synthesized in E. coli, is a single, non-glycosylated polypeptide chain consisting of 239 amino acids (specifically, residues 33-250). With a molecular weight of 26.3 kDa, the MMAB protein is fused to a 21 amino acid His-Tag at its N-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10510
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized through 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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