PAICS Human

Phosphoribosylaminoimidazole Carboxylase Human Recombinant

Recombinant human PAICS, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 448 amino acids (1-425) with a molecular weight of 49.5kDa. This protein features a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27251
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PPCS Human

Phosphopantothenoylcysteine Synthetase Human Recombinant

Produced in E. coli, our PPCS is a single, non-glycosylated polypeptide chain consisting of 331 amino acids (specifically, amino acids 1 to 311). It has a molecular weight of 36.1 kDa. Our PPCS is engineered with a 20 amino acid His-tag at the N-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27308
Source
Escherichia Coli.
Appearance
Our PPCS is supplied as a sterile, colorless solution.

DARS Human

Aspartyl-tRNA Synthetase Human Recombinant

Recombinant DARS, produced in E. coli, is a single polypeptide chain with a molecular weight of 59.3 kDa. It consists of 521 amino acids, with the first 501 amino acids corresponding to the DARS protein. A 20 amino acid His-tag is fused to the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25722
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

FARSB Human

Phenylalanyl-TRNA Synthetase Beta Human Recombinant

Recombinant FARSB protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 612 amino acids (specifically, residues 1-589) and exhibits a molecular weight of 68.5kDa. This protein includes a 23 amino acid His-tag fused at the N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25845
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered.

GARS Human

Glycyl-TRNA Synthetase Human Recombinant

Recombinant human GARS protein, expressed in E. coli, is available as a single, non-glycosylated polypeptide chain. This protein consists of 270 amino acids, spanning from residues 43 to 289, and has a molecular weight of 30 kDa. The N-terminus of GARS is fused to a 23 amino acid His-tag to facilitate purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25924
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

GARS Human, sf9

Glycyl-TRNA Synthetase Human Recombinant, sf9

Recombinant human GARS, produced in SF9 insect cells, is a glycosylated polypeptide with a molecular weight of 78.9 kDa. It features a 10xHis tag at the N-terminus to facilitate purification. The protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25994
Source
Sf9 Insect Cells.
Appearance
Clear, sterile-filtered solution.

HARS Human, Sf9

Histidyl-tRNA Synthetase Human Recombinant, Sf9

Baculovirus-produced Histidyl-tRNA Synthetase Human Recombinant is a single glycosylated polypeptide chain with a molecular weight of 58.3 kDa. Histidyl-tRNA Synthetase is fused with a 6x His Tag and purified using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT26683
Source
Sf9 Insect Cells.
Appearance
Clear, sterile filtered solution.

KARS Human

Lysyl-tRNA Synthetase Human Recombinant

This product consists of the recombinant human KARS protein, produced in E. coli. It is a single, non-glycosylated polypeptide chain that contains 558 amino acids (residues 63-597) and has a molecular weight of 63.7 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus to facilitate purification, which is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26752
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterilized by filtration.

MTHFS Human

5,10-Methenyltetrahydrofolate Synthetase Human Recombinant

Recombinant MTHFS protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 223 amino acids (residues 1-203) with a molecular weight of 25.4 kDa. The protein is expressed with an N-terminal 20-amino acid His-tag and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26930
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

NARS Human

Asparaginyl-TRNA Synthetase Human Recombinant

Recombinant human NARS, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 571 amino acids (with amino acids 1 to 548 being part of the NARS sequence) and has a molecular weight of 65.3 kDa. This protein is engineered with a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26994
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Synthetases are a class of enzymes that catalyze the synthesis of complex molecules from simpler ones, typically using energy derived from ATP. They are also known as ligases. Synthetases are classified based on the type of reaction they catalyze and the substrates they act upon. Major classes include aminoacyl-tRNA synthetases, which play a crucial role in protein synthesis, and fatty acid synthetases, involved in lipid metabolism.

Biological Properties

Key Biological Properties: Synthetases are essential for various biosynthetic pathways. They exhibit high substrate specificity and catalytic efficiency. Expression Patterns: The expression of synthetases is tightly regulated and varies across different tissues and developmental stages. Tissue Distribution: Synthetases are ubiquitously expressed but are particularly abundant in tissues with high metabolic activity, such as the liver, muscle, and brain.

Biological Functions

Primary Biological Functions: Synthetases are involved in the synthesis of proteins, nucleic acids, lipids, and other macromolecules. They are critical for cellular growth, division, and maintenance. Role in Immune Responses: Certain synthetases, like aminoacyl-tRNA synthetases, have been implicated in immune responses by modulating the production of cytokines and other immune mediators. Pathogen Recognition: Some synthetases can recognize and respond to pathogen-associated molecular patterns (PAMPs), contributing to the innate immune response.

Modes of Action

Mechanisms with Other Molecules and Cells: Synthetases interact with various substrates and cofactors to catalyze the formation of complex molecules. For example, aminoacyl-tRNA synthetases bind to tRNA and amino acids to form aminoacyl-tRNA. Binding Partners: Synthetases often form complexes with other proteins to enhance their catalytic activity and ensure substrate specificity. Downstream Signaling Cascades: The products of synthetase-catalyzed reactions can act as signaling molecules, influencing various cellular pathways and processes.

Regulatory Mechanisms

Expression and Activity Control: The expression of synthetases is regulated at the transcriptional level by various transcription factors and signaling pathways. Transcriptional Regulation: Specific promoter regions and enhancers control the transcription of synthetase genes in response to cellular and environmental cues. Post-Translational Modifications: Synthetases undergo various post-translational modifications, such as phosphorylation and ubiquitination, which modulate their activity, stability, and interactions with other proteins.

Applications

Biomedical Research: Synthetases are used as tools to study protein synthesis, metabolic pathways, and enzyme kinetics. Diagnostic Tools: Abnormal levels of certain synthetases can serve as biomarkers for diseases, such as cancer and metabolic disorders. Therapeutic Strategies: Targeting synthetases with specific inhibitors or activators holds potential for treating various diseases, including infections, cancer, and genetic disorders.

Role in the Life Cycle

Development: Synthetases are essential for embryonic development, as they provide the necessary building blocks for cell growth and differentiation. Aging: The activity of synthetases can decline with age, leading to reduced cellular function and increased susceptibility to diseases. Disease: Dysregulation of synthetase activity is associated with various diseases, including neurodegenerative disorders, metabolic syndromes, and cancer.

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