NMT2 Human

N-Myristoyltransferase 2 Human Recombinant

Recombinant human NMT2, with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This non-glycosylated polypeptide chain consists of 518 amino acids (1-498 a.a.), resulting in a molecular mass of 59.1 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11594
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

NNMT Human

Nicotinamide N-Methyltransferase Human Recombinant

Recombinant human NNMT, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a His-tag of 20 amino acids fused at its N-terminus. It consists of 284 amino acids in total (1-264 a.a.), resulting in a molecular mass of 31.7 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11656
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

NTMT1 Human

N-Terminal Xaa-Pro-Lys N-Methyltransferase 1 Human Recombinant

Recombinant human NTMT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 248 amino acids (with a sequence spanning from amino acid positions 1 to 223) and possesses a molecular weight of 28.1 kDa. For purification purposes, a 25 amino acid His-tag is fused to the N-terminus of the NTMT1 protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT11698
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

QPRT Human

Quinolinate Phosphoribosyltransferase Human Recombinant

This product consists of the human recombinant QPRT enzyme, produced in E. coli. It is a single, non-glycosylated polypeptide chain with 317 amino acids, including a 20 amino acid His-Tag attached to the N-terminus. The molecular weight of the protein is 32.9 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12876
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

QTRT1 Human

Queuine TRNA-Ribosyltransferase 1 Human Recombinant

Recombinant human QTRT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein comprises 428 amino acids (specifically, amino acids 1 through 403), resulting in a molecular weight of 46.7 kDa. The recombinant QTRT1 protein is engineered with a 25 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12975
Source
Escherichia Coli.
Appearance
The product is a clear, sterile-filtered solution.

QTRTD1 Human

Queuine TRNA-Ribosyltransferase Domain Containing 1 Human Recombinant

Recombinant human QTRTD1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 438 amino acids (with amino acids 1 to 415 included) and has a molecular weight of 49.1 kDa. A 23 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13056
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

Rhodanese Human

Thiosulfate Sulfurtransferase Human Recombinant

Recombinant Human Rhodanese, expressed in E. coli, is a single, non-glycosylated polypeptide chain with 317 amino acids (1-297 a.a) and a molecular weight of 35.6 kDa. A 20 amino acid His-Tag is fused to the N-terminus to facilitate purification via standard chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13133
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SETD7 Human

Set7/9 Histone Methyltransferase Human Recombinant

Recombinant Human SETD7, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 40.7 kDa, comprising 366 amino acids. The purification of SETD7 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13567
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

ST6GALNAC5 Human

ST6GALNAC5 Human Recombinant

Produced using Sf9 insect cells, ST6GALNAC5 is a single, glycosylated polypeptide chain with a molecular weight of 36.4 kDa. It encompasses amino acids 30 to 336 and includes a 6-amino acid His tag located at the C-terminus. Purification is achieved through proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT13989
Source

Sf9, Baculovirus cells.

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

SULT1A2 Human

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

Recombinant human SULT1A2, expressed in E. coli, is a non-glycosylated polypeptide chain with a single chain. It comprises 315 amino acids (1-295 a.a.) and possesses a molecular weight of 36.4 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.
BT14112
Source
Escherichia 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 .

© Copyright 2024 Thebiotek. All Rights Reserved.