PRPS1 Human

Phosphoribosyl Pyrophosphate Synthetase 1 Human Recombinant

This product consists of the recombinant human PRPS1 protein, expressed in E. coli and purified to a high degree. The protein is a single, non-glycosylated polypeptide chain with 338 amino acids (residues 1-318), exhibiting a molecular weight of 36.9 kDa. For purification purposes, a 20 amino acid His-Tag is fused to the N-terminus of the protein.
Shipped with Ice Packs
Cat. No.
BT27377
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

YARS Human

Tyrosyl-tRNA Synthetase Human Recombinant

Produced in E. coli, YARS is a single, non-glycosylated polypeptide chain composed of 548 amino acids (specifically, amino acids 1 to 528). It possesses a molecular mass of 61.3kDa. For purification, a 20 amino acid His-tag is fused to the N-terminus of YARS, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT28192
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized through filtration.

YARS2 Human

Tyrosyl-tRNA Synthetase 2 Human Recombinant

Recombinant Human YARS2, expressed in E. coli, is a non-glycosylated polypeptide chain. It consists of 482 amino acids (specifically, residues 17-477), resulting in a molecular weight of 53.7kDa. For purification, a 21 amino acid His-tag is fused to the N-terminus, and proprietary chromatographic techniques are employed.
Shipped with Ice Packs
Cat. No.
BT28261
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

AARS Human

Alanyl-tRNA Synthetase Human Recombinant

Recombinant Human Alanyl-tRNA synthetase, produced in SF9 cells, is a glycosylated polypeptide with a molecular weight of 110 kDa. This protein, tagged with -6xHis, undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT25476
Source
Sf9 insect cells.
Appearance
Clear, sterile-filtered solution.

ACSF2 Human

Acyl-CoA Synthetase Family Member 2 Human Recombinant

Recombinant Human ACSF2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 597 amino acids (42-615 a.a), with a molecular weight of 66.1 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT25575
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

AsnRS

Asparagine tRNA Synthetase Brugia Malayi Recombinant

Recombinant AsnRS from Brugia Malayi, expressed in E.Coli, is a monomeric polypeptide chain with a molecular weight of 64.5kDa. It comprises 568 amino acids, including an N-terminal 6xHis Tag for purification purposes. The AsnRS protein has undergone purification using proprietary chromatographic techniques and lacks glycosylation.
Shipped with Ice Packs
Cat. No.
BT25645
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GSS Human

Glutathione Synthetase Human Recombinant

This product consists of recombinant human GSS, expressed in E. coli and fused with a 20 amino acid His tag at its N-terminus. This results in a single, non-glycosylated polypeptide chain containing 494 amino acids (including the His tag, residues 1-474 represent the GSS sequence). The molecular weight of the fusion protein is 54.5kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26450
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

HARS Human

Histidyl-tRNA Synthetase Human Recombinant

Recombinant Human Histidyl-tRNA Synthetase, produced in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 55 kDa.
Shipped with Ice Packs
Cat. No.
BT26532
Source
Escherichia Coli.
Appearance
Clear, sterile, filtered solution.

HARS Human, His

Histidyl-tRNA Synthetase Human Recombinant, His Tag

This product consists of the recombinant human HARS protein, expressed in E. coli and purified to a high degree. A 23-amino acid His tag is fused to the N-terminus to facilitate purification. The protein is a single, non-glycosylated polypeptide chain with a molecular weight of 59.4 kDa. It encompasses amino acids 1-509 of the full HARS sequence. Purification is achieved using proprietary chromatographic methods, resulting in a highly pure protein.
Shipped with Ice Packs
Cat. No.
BT26591
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

TYMS Human

Thymidylate Synthetase Human Recombinant

Recombinant Human Thymidylate synthase, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 333 amino acids (with a sequence spanning from amino acid 1 to 313) and possesses a molecular weight of 37.8 kDa. This Thymidylate synthase variant includes a 20 amino acid His-Tag fused at its N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27850
Source
Escherichia Coli.
Appearance
Clear, colorless solution, 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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