GLUL Human, His Active

Glutamine Synthetase Human Recombinant, His Active

Recombinant human GLUL, expressed in E. coli, is a purified protein with a His-tag. This non-glycosylated polypeptide consists of 393 amino acids, with a molecular weight of 44.2 kDa. The protein sequence spans residues 1-373 of the GLUL protein, with an additional 20 amino acid His-Tag fused at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26235
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

GMPS Human

GMPS Human Recombinant

Recombinant human GMPS, expressed in E. coli, is a non-glycosylated polypeptide chain with 717 amino acids (including a 24 amino acid His-tag at the N-terminus). This protein, with a molecular weight of 79.2 kDa, is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26346
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

PRPS2 Human

Phosphoribosyl Pyrophosphate Synthetase 2 Human Recombinant

Recombinant human PRPS2 protein has been expressed in E. coli and purified to a single, non-glycosylated polypeptide chain. This protein consists of 344 amino acids, with a molecular weight of 37.4 kDa. It encompasses amino acids 1-321 and includes a 23 amino acid His-tag fused to the N-terminus to facilitate purification. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27475
Source
E.coli.
Appearance
The product is provided as a clear, sterile-filtered solution.

SARS Human

Seryl-tRNA Synthetase Human Recombinant

Recombinant human SARS, produced in E.coli, is a single polypeptide chain that lacks glycosylation. It consists of 537 amino acids, with amino acids 1-514 comprising the protein sequence, resulting in a molecular weight of 61.2kDa. The protein includes a 23 amino acid His-tag fused to its N-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27588
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

TARS Human

Threonyl-tRNA Synthetase Human Recombinant

This product consists of the human TARS enzyme, recombinantly produced in E. coli. It is a single polypeptide chain that is not glycosylated, meaning it lacks attached sugar molecules. The protein contains 743 amino acids, with the first 723 representing the TARS sequence. A 20 amino acid His-tag is attached to the N-terminus to facilitate purification. The molecular weight of the recombinant TARS is 85.6 kDa, and it undergoes purification using proprietary chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT27668
Source
Escherichia Coli.
Appearance
Clear and colorless solution, sterilized by filtration.

TARS Human, Sf9

Threonyl-tRNA Synthetase Human Recombinant, Sf9

Recombinant human PL-7, produced in SF9 cells, is a glycosylated polypeptide with a molecular weight of 85 kDa. It is expressed with a -6xHis tag and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27751
Source
Sf9 insect cells.
Appearance
A clear, sterile-filtered solution.

GLUL Human

Glutamine Synthetase Human Recombinant

Recombinant human GLUL, produced in E. coli bacteria, is a single polypeptide chain that lacks glycosylation modifications. It comprises 393 amino acids, with a sequence spanning from position 1 to 373, and has a molecular weight of 44.2 kDa. A 20-amino acid His-Tag is attached to the N-terminus of the protein to facilitate purification using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT26065
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

GLUL Human, Active

Glutamine Synthetase Human Recombinant, Active

Recombinant Human GLUL, produced in E. coli, is a monomeric protein with a molecular weight of approximately 42 kDa. This non-glycosylated polypeptide chain comprises 373 amino acids, representing the full-length protein sequence (residues 1-373).
Shipped with Ice Packs
Cat. No.
BT26145
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

NARS Human, Sf9

Asparaginyl-TRNA Synthetase Human Recombinant, Sf9

Recombinant Human NARS, produced in Sf9 insect cells, is a glycosylated polypeptide with a molecular weight of 63,853 Daltons. It is expressed with a 6xHis tag on its N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT27096
Source
Sf9 Insect Cells.
Appearance
A clear, sterile-filtered solution.

OAS1 Human

2’-5’ Oligoadenylate Synthetase 1 Human Recombinant

Recombinant human OAS1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein, with a molecular weight of 43.9 kDa, consists of 384 amino acids, including a 20 amino acid His tag at the N-terminus (1-364 a.a. of the OAS1 sequence). Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27173
Source
Escherichia Coli.
Appearance
A clear and colorless solution, sterile-filtered.
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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