NNMT Human, Active

Nicotinamide N-Methyltransferase Human Recombinant, Active

Recombinant human NNMT, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 284 amino acids (specifically, residues 1-264) and possessing a molecular weight of 37.7 kDa. This protein is engineered with a 20-amino acid His-tag at its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT1950
Source

Escherichia Coli.

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

AASDHPPT Human

Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase Human Recombinant

Recombinant human AASDHPPT, fused with a 21 amino acid His tag at its N-terminus, is produced in E. coli. This purified protein is a single, non-glycosylated polypeptide chain comprising 316 amino acids (14-309 a.a.) with a molecular weight of 36.4kDa. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT2013
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ABO Human

ABO Blood Group Human Recombinant

Recombinant Human ABO, synthesized in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 322 amino acids (54-354 a.a), resulting in a molecular weight of 37.4kDa. The ABO protein is engineered with a 21 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2045
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

ACAA1 Human

Acetyl-COA Acyltransferase Human Recombinant

Recombinant Human ACAA1, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 419 amino acids (27-424 a.a.). With a molecular mass of 43.8 kDa, it features a 21 amino acid His-Tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT2126
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

ACAA2 Human

Acetyl-COA Acyltransferase 2 Human Recombinant

Recombinant human ACAA2 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 42.6 kDa. The protein sequence contains amino acids 17-397 of ACAA2 and a 23 amino acid His-tag at the N-terminus. It is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2185
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

C1GALT1 Human

Core 1 Beta3-Gal-T1 Human Recombinant

Recombinant human C1GALT1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 357 amino acids (30-363 a.a) with a molecular weight of 41.4 kDa. The protein is expressed with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT3230
Source
Escherichia Coli.
Appearance
The product is a clear, sterile-filtered solution.

CHST10 Human

Carbohydrate Sulfotransferase 10 Human Recombinant

Recombinant human CHST10 protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) with a molecular weight of 41.2 kDa. A 21 amino acid His-tag is fused to the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3275
Source
Escherichia Coli.
Appearance
A clear, sterile solution.

CHST3 Human

Carbohydrate Sulfotransferase 3 Human Recombinant

Produced in Sf9 Baculovirus cells, CHST3 is a single, glycosylated polypeptide chain. It consists of 450 amino acids (39-479.a.a) and has a molecular weight of 51.3kDa. The protein is expressed with a 6 amino acid His tag at the C-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT3391
Source

Sf9, Baculovirus cells.

Appearance

Sterile filtered, colorless solution.

CHST5 Human

Carbohydrate Sulfotransferase 5 Human Recombinant

This recombinant CHST5 protein, of human origin, is produced using Sf9 Baculovirus cells. It exists as a single polypeptide chain that has undergone glycosylation and comprises 380 amino acids (specifically, amino acids 27 to 395). This corresponds to a molecular weight of 42.9 kDa. For purification purposes, the protein is engineered with a 6-amino acid His tag at its C-terminus and subsequently purified through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT3448
Source

Sf9, Baculovirus cells.

Appearance

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

COMT Human

Catechol-O-Methyltransferase Human Recombinant

Recombinant human COMT, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 221 amino acids (residues 51-271). This protein variant corresponds to the mature form of COMT and has a molecular weight of 24.4 kDa. It is purified to high homogeneity using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3482
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.
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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