TSTD1 Human

Thiosulfate Sulfurtransferase Like Domain Containing 1 Human Recombinant

TSTD1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids (1-115 a.a.) and having a molecular mass of 14.6kDa.
TSTD1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT15268
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

TSTD3 Human

Thiosulfate Sulfurtransferase Like Domain Containing 3 Human Recombinant

TSTD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97 a.a) and having a molecular mass of 13.7kDa.
TSTD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15352
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

UGT1A1 Human

UDP Glucuronosyltransferase 1 Family Polypeptide A1 Human Recombinant

UGT1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 488 amino acids (26-490 a.a) and having a molecular mass of 54.7kDa.
UGT1A1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15438
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

UGT8 Human

UDP Glycosyltransferase 8 Human Recombinant

UGT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 544 amino acids (21-541 a.a) and having a molecular mass of 61.6kDa.
UGT8 is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT15503
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

UPRT Human

Uracil Phosphoribosyltransferase Human Recombinant

UPRT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.2kDa.
UPRT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15580
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

XYLT2 Human

Xylosyltransferase 2 Human Recombinant

XYLT2 Human Recombinant is a single, glycosylated polypeptide chain containing 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and having a molecular mass of 94.0kDa. XYLT2 is fused to an N-terminal linker (2 extra a.a), C-terminal linker (2 extra a.a) and C-terminal His-tag (6 extra a.a).

Shipped with Ice Packs
Cat. No.
BT15640
Source

HEK293 Cells.

Appearance
Filtered White lyophilized (freeze-dried) powder.
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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