UMPS Human

Uridine Monophosphate Synthetase Human Recombinant

Recombinant human UMPS, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 500 amino acids, with residues 1 to 480 representing the UMPS sequence. The protein has a molecular weight of 54.3 kDa. For purification and detection purposes, a 20 amino acid His-tag is attached to the N-terminus. The purification process utilizes proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT27938
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized through filtration.

UMPS Human, Sf9

Uridine Monophosphate Synthetase Human Recombinant, Sf9

Recombinant human UMPS protein, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It comprises 486 amino acids (with amino acids 1-480 representing the UMPS sequence) and has a molecular weight of 53 kDa. Note that the molecular size observed on SDS-PAGE may range from 50-70 kDa. This UMPS protein is engineered with a 6-amino acid His tag at the C-terminus to facilitate purification, which is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28027
Source

Sf9, Baculovirus cells.

Appearance
Clear, sterile-filtered solution.

WARS Human

Tryptophanyl-tRNA Synthetase Human Recombinant

Recombinant Human WARS, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 491 amino acids, with amino acids 1-471 representing the WARS sequence. The protein has a molecular mass of 55.3 kDa. For purification and detection purposes, a 20 amino acid His-Tag is fused to the N-terminus of WARS. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28112
Source
Escherichia Coli.
Appearance
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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