MPST Human

Mercaptopyruvate Sulfurtransferase Human Recombinant

Recombinant human MPST, produced in E. coli, is available as a single, non-glycosylated polypeptide chain. This protein consists of 321 amino acids (residues 1-297) and has a molecular mass of 35 kDa. The recombinant MPST is fused to a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10563
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

Ornithine Aminotransferase Human

Ornithine Aminotransferase Human Recombinant

Recombinant Human Ornithine Aminotransferase, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 408 amino acids (residues 33-439). With a molecular weight of 45.2 kDa, the protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11763
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

OTC Human

Ornithine Carbamoyltransferase Human Recombinant

Recombinant OTC, expressed in E. coli, is a single polypeptide chain consisting of 347 amino acids (residues 33-354) with a molecular weight of 38.9 kDa. This OTC protein is modified with a 25 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11821
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PCMT1 Human

Protein-L-Isoaspartate O-Methyltransferase Human Recombinant

Recombinant Human PCMT1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 263 amino acids (with a sequence spanning from amino acid 1 to 227) and possessing a molecular mass of 28.8 kDa. A 36 amino acid His-Tag is fused to the N-terminus of PCMT1. The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11878
Source
Escherichia Coli.
Appearance
A clear and sterile solution.

PCYT2 Human

Phosphate Cytidylyltransferase 2 Human Recombinant

Recombinant PCYT2, derived from humans and produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 409 amino acids (specifically, amino acids 1 to 389) and exhibits a molecular weight of 45.9 kDa. The protein includes a 20-amino acid His-tag fused to its N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11941
Source
Escherichia Coli.
Appearance
The product appears as a sterile, colorless solution after filtration.

PNMT Human

Phenylethanolamine-N-Methyltransferase Human Recombinant

Recombinant Human PNMT, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 282 amino acids (amino acids 1-282) and has a molecular weight of 30.8 kDa. The purification of PNMT is carried out using standard chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT12007
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

RNMT Human

RNA (guanine-7-) Methyltransferase Human Recombinant

Produced in E. coli, recombinant human RNMT is a single, non-glycosylated polypeptide chain consisting of 496 amino acids (specifically, amino acids 1 to 476). It has a molecular mass of 57 kDa. The protein is fused to a 20 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13245
Source
Escherichia Coli.
Appearance
The product is a clear, sterile-filtered solution without any color.

RNMTL1 Human

RNA Methyltransferase Like 1 Human Recombinant

Recombinant human RNMTL1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 443 amino acids (with amino acids 1 to 420 included). It has a molecular weight of 49.4 kDa. A 23-amino acid His-tag is fused to the N-terminus of the RNMTL1 protein. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13328
Source
Escherichia Coli.
Appearance
A sterile, colorless solution that has been filtered.

SAT1 Human

Spermidine/Spermine N1-Acetyltransferase 1 Human Recombinant

Recombinant human SAT1, engineered with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This non-glycosylated polypeptide chain comprises 191 amino acids (1-171 a.a.) and exhibits a molecular weight of 22.1kDa. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13409
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SAT2 Human

Spermidine/Spermine N1-Acetyltransferase 2 Human Recombinant

Recombinant human SAT2, expressed in E. coli, is a single polypeptide chain with a molecular weight of 21.0 kDa. It consists of 190 amino acids, with residues 1-170 representing the SAT2 protein. A 20 amino acid His-tag is fused to the N-terminus to aid in purification, which is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13486
Source
E.coli.
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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