LCMT1 Human

Leucine Carboxyl Methyltransferase 1 Human Recombinant

Recombinant human LCMT1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 358 amino acids (residues 1-334) with a molecular weight of 41 kDa. The protein includes a 24-amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9634
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile filtered solution.

LPCAT1 Human

Lysophosphatidylcholine Acyltransferase Human Recombinant

Recombinant human LPCAT1, expressed in E. coli, is a monomeric, non-glycosylated polypeptide chain comprising 479 amino acids (residues 79-534). It has a molecular weight of 53.4 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9680
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

EOGT Mouse

EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase Mouse Recombinant

EOGT, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 516 amino acids (amino acids 20-527) and has a molecular mass of 60.4 kDa. On SDS-PAGE under reducing conditions, it migrates at a molecular weight of 50-70 kDa. The protein is expressed with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3835
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HS3ST1 Human

Heparan Sulfate 3-O-Sulfotransferase 1 Human Recombinant

This product consists of the human form of HS3ST1, a protein produced in E. coli bacteria. It is a single chain of 310 amino acids (specifically amino acids 21 to 307), without any sugar modifications, and has a molecular weight of 36.2 kilodaltons. For purification and detection purposes, a 23 amino acid tag called His-tag is attached to the protein's beginning. The purification process involves specialized chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT9179
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized through filtration.

KAT2A Human

K (lysine) Acetyltransferase 2A Human Recombinant

Recombinant human KAT2A, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 447 amino acids (specifically, amino acids 411-837) and has a molecular weight of 51.1 kDa. This KAT2A protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9273
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that is colorless.

KMT5A Human

Lysine Methyltransferase 5A Human Recombinant

This product consists of the recombinant human KMT5A protein, specifically amino acids 195 to 352, produced in Sf9 insect cells using baculovirus expression system. It is a single polypeptide chain with a 7 amino acid Histidine tag at the C-terminus to facilitate purification. The protein has a molecular weight of 18.9 kDa and appears as a band between 18-28 kDa on SDS-PAGE under reducing conditions due to glycosylation. The protein has been purified using proprietary chromatographic techniques to ensure high purity.

Shipped with Ice Packs
Cat. No.
BT9358
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

LCAT Human

Lecithin-Cholesterol Acyltransferase Human Recombinant

Recombinant human LCAT, produced in E. coli, is a single polypeptide chain without any glycosylation. It consists of 441 amino acids, including a 25 amino acid His Tag attached to the N-terminus (amino acids 25-440), resulting in a molecular weight of 49.8 kDa. The purification process involves specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9440
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

M2 Human

DLAT/DLST/BCOADC Recombinant Human

This recombinant antigen is designed for use in both solid-phase (ELISA) and fluid-phase diagnostic assays. It consists of a mixture of E2/dihydrolipamide acyltransferase subunits derived from three distinct mitochondrial protein complexes: pyruvate dehydrogenase complex (PDC-E2) with a molecular mass of 60,630 Daltons and an isoelectric point (pI) of 5.8; 2-oxo-glutarate dehydrogenase complex (OGDC-E2) with a molecular mass of 42,301 Daltons and a pI of 6.3; and branched-chain 2-oxo-acid dehydrogenase complex (BCOADCE2) with a molecular mass of 47,321 Daltons and a pI of 6.5. The mixture contains an equal mass of each protein component. The cDNAs encoding the mature forms of human PDC-E2, OGDC-E2, and BCOADC-E2 were individually fused to a hexa-histidine purification tag.
Shipped with Ice Packs
Cat. No.
BT9742
Source
Sf9 insect cells.

MAT1A Human

Methionine Adenosyltransferase I Alpha Human Recombinant

Recombinant human MAT1A, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 414 amino acids (with amino acids 1 to 395). It has a molecular weight of 45.6 kDa. A 20 amino acid histidine tag is fused to the N-terminus of MAT1A. The protein is purified using standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT9811
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

NAT6 Human

N-Acetyltransferase 6 Human Recombinant

Recombinant Human NAT6, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 328 amino acids (specifically, amino acids 1 to 308). With a molecular weight of 35.9 kDa, this recombinant protein is characterized by a 20 amino acid His tag fused to its N-terminus. Its purification is achieved using standard chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT11066
Source
Escherichia Coli.
Appearance
A clear, 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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