DIMT1 Human

DIM1 Dimethyladenosine Transferase 1 Human Recombinant

Recombinant human DIMT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 334 amino acids (residues 1-313). It has a molecular weight of 37.5 kDa. The protein includes a 21 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3524
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

DLAT Human

Dihydrolipoamide S-Acetyltransferase Human Recombinant

This product consists of a full-length cDNA sequence that codes for the mature human PDC-E2 protein. This protein, with a molecular weight of 60,630 Daltons at a pH of 5.8, has been engineered to include a hexa-histidine tag for purification purposes.
Shipped with Ice Packs
Cat. No.
BT3569
Source
Sf9 insect cells.
Appearance
The product is a clear, sterile-filtered solution.

glpE E.Coli

Thiosulfate sulfurtransferase E.Coli Recombinant

Recombinant glpE, produced in E. coli, is a single polypeptide chain consisting of 131 amino acids (amino acids 1 to 108) and possesses a molecular weight of 14.5 kDa. A 23 amino acid His-tag is fused to the N-terminus of glpE, and the protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4758
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that is colorless.

GLYAT Human

Glycine-N-Acyltransferase Human Recombinant

Recombinant human GLYAT, produced in E.coli, is a single, non-glycosylated polypeptide chain. It consists of 316 amino acids (amino acids 1-296) and has a molecular weight of 36.0 kDa. A 20 amino acid His-Tag is fused to the N-terminus of GLYAT, and the protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4820
Source
Escherichia Coli.
Appearance
GLYAT is provided as a clear solution that has been sterilized by filtration.

GLYATL2 Human

Glycine-N-Acyltransferase-Like 2 Human Recombinant

Recombinant human GLYATL2, expressed in E. coli, is a monomeric, non-glycosylated polypeptide chain. It consists of 317 amino acids (residues 1-294a.a), with a molecular weight of 36.7 kDa. The protein includes an N-terminal 23-amino acid His-tag and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4885
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GNMT Human

Glycine N-methyltransferase Human Recombinant

Recombinant human GNMT, with a 20-amino acid Histidine tag attached to its N-terminus, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 315 amino acids (with amino acids 1-295 originating from the GNMT sequence) and has a molecular weight of 34.9 kDa. The purification of GNMT is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4964
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GNMT Human, Active

Glycine N-Methyltransferase Human Recombinant , Active

Recombinant human GNMT, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 315 amino acids, with the first 295 amino acids representing the native protein sequence. It has a molecular weight of 34.9 kDa. The protein is engineered with a 20-amino acid His-tag at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5023
Source

Escherichia Coli.

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

GSTM1 Human, Sf9

Glutathione S-Transferase M1 Human Recombinant, Sf9

Recombinant GSTM1 protein, expressed in Sf9 insect cells, is a single polypeptide chain with a molecular weight of 26.8 kDa. It comprises 227 amino acids, including the 1-218 amino acid sequence of GSTM1 and a 9 amino acid Histidine tag fused at the C-terminus. The protein is glycosylated, meaning it has sugar molecules attached. On SDS-PAGE analysis under reducing conditions, GSTM1 appears as multiple bands between 28-40 kDa. The protein has been purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT6982
Source

Sf9, Insect cells.

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

GSTM1 Mouse

Glutathione S-Transferase M1 Mouse Recombinant

GSTM1 Mouse Recombinant is a single, non-glycosylated polypeptide chain with a molecular weight of 25.9 kDa that contains 218 amino acids. It is produced in E. coli. Proprietary chromatographic methods are used to purify the GTM1.
Shipped with Ice Packs
Cat. No.
BT7073
Source
Escherichia Coli.
Appearance
Colorless solution that has been sterile filtered.

GSTM1 Mouse, His

Glutathione S-Transferase M1 Mouse Recombinant, His Tag

Recombinant GSTM1 from mouse, expressed in E. coli, is a purified protein. It is a single, non-glycosylated polypeptide chain with 238 amino acids (amino acids 1-218) and a molecular weight of 28.1 kDa. A 20 amino acid His-tag is present at the N-terminus of the protein. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7152
Source
Escherichia 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 .

© Copyright 2024 Thebiotek. All Rights Reserved.