NMNAT1 Human

Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant

Recombinant Human NMNAT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 315 amino acids (1-279 a.a.) with a molecular weight of 36 kDa. A 36 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.
BT11163
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GNPNAT1 Human

Glucosamine-Phosphate N-Acetyltransferase 1 Human Recombinant

Produced in E.Coli, GNPNAT1 is expressed as a single, non-glycosylated polypeptide chain comprising 207 amino acids (residues 1-184). With a molecular weight of 23.1 kDa, the protein includes a 23 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5402
Source
Escherichia Coli.
Appearance
The product appears as a clear, sterile solution following filtration.

GST, 218 a.a.

Glutathione S-Transferase, 218 a.a. Recombinant

Recombinantly produced in E.Coli, this GST is a single, non-glycosylated polypeptide chain encompassing 218 amino acids (1-218 a.a) with a molecular weight of 25.4kDa.
Shipped with Ice Packs
Cat. No.
BT6305
Source

Escherichia Coli.

Appearance
Clear solution, sterile-filtered.

GSTM3 Human

Glutathione S-Transferase MU 3 Human Recombinant

Recombinant GSTM3, expressed in E. coli, is a single polypeptide chain with a molecular weight of 29.1 kDa. It consists of 249 amino acids, including a 24 amino acid His-tag at the N-terminus (amino acids 1-225). Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7319
Source
E.coli.
Appearance
A clear and colorless solution, sterilized by filtration.

N6AMT1 Human

N-6 Adenine-Specific DNA Methyltransferase 1 Human Recombinant

Recombinant human N6AMT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 237 amino acids (1-214 a.a.) with a molecular weight of 25.3 kDa. This protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10679
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

NAA10 Human

N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant

Recombinant human NAA10, a 28.6 kDa (SDS-PAGE may show higher) non-glycosylated polypeptide, is produced in E. coli. It contains amino acids 1-235 of NAA10 with an N-terminal 20 amino acid His-tag. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10762
Source
Escherichia Coli.
Appearance
Colorless, sterile filtered solution.

NAA30 Human

N Alpha-Acetyltransferase 30, NatC Catalytic Subunit Human Recombinant

This product consists of recombinant human NAA30, produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 385 amino acids (amino acids 1-362), with a molecular weight of 41.7 kDa. A 23 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10820
Source
Escherichia Coli.
Appearance
A clear solution, sterile filtered.

NAA50 Human

N Alpha-Acetyltransferase 50, NatE Catalytic Subunit Human Recombinant

Recombinant human NAA50, produced in E. coli, is a single, non-glycosylated polypeptide chain. This protein comprises 193 amino acids (residues 1-169) and possesses a molecular weight of 21.9 kDa. It features a 24 amino acid His-tag fused to the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10883
Source
Escherichia Coli.
Appearance
A clear, sterile solution.

NAT1 Human

N-Acetyltransferase 1 Human Recombinant

Recombinant human NAT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 310 amino acids (residues 1-290) with a molecular weight of 36.1 kDa. This protein is engineered with a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT10948
Source
Escherichia Coli.
Appearance
NAT1 is provided as a clear, sterile solution after filtration.

PNPT1 Human

Polyribonucleotide Nucleotidyltransferase 1 Human Recombinant

Recombinant human PNPT1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 761 amino acids (46-783 a.a.). It has a molecular mass of 83.3 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT12082
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.
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.