PGAM2 Human, Active

Phosphoglycerate Mutase 2 Human Recombinant, Active

Recombinant human PGAM2, expressed in E.coli, is a non-glycosylated polypeptide chain with a molecular weight of 30.9kDa. The protein comprises 273 amino acids, including a 20 amino acid His-tag at the N-terminus (amino acids 1-253). Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12899
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

PGM1 Human

Phosphoglucomutase 1 Human Recombinant

Recombinant human PGM1, expressed in E. coli, is a non-glycosylated polypeptide chain. It consists of 585 amino acids, with the first 562 amino acids forming the PGM1 protein. A 23 amino acid His-tag is fused to the N-terminus. The protein has a molecular mass of 63.8 kDa and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12943
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PGM2 Human

Phosphoglucomutase 2 Human Recombinant

Recombinant human PGM2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 635 amino acids (residues 1-612) and has a molecular weight of 70.7 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13009
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PMM1 Human

Phosphomannomutase 1 Human Recombinant

Recombinant human PMM1, with a 20-amino acid His tag at the N-terminus, is produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 282 amino acids (residues 1-262), resulting in a molecular weight of 31.9 kDa. The purification of PMM1 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13095
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PMM2 Human

Phosphomannomutase 2 Human Recombinant

Recombinant human PMM2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein variant includes a 20 amino acid His tag at the N-terminus and consists of 266 amino acids (residues 1-246), resulting in a molecular weight of 30.2 kDa. Purification of PMM2 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13202
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

BPGM Human

2,3-Bisphosphoglycerate Mutase Human Recombinant

Recombinant human BPGM, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 267 amino acids (specifically, amino acids 1 to 259). With a molecular weight of 31 kDa, it features an 8-amino acid His tag at the C-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT12320
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PGAM1 Human

Phosphoglycerate Mutase 1 Human Recombinant

Recombinant PGAM1 is a human protein produced in E. coli. This non-glycosylated protein consists of a single polypeptide chain of 274 amino acids (residues 1-254), resulting in a molecular weight of 30.9 kDa. For purification purposes, a 20-amino acid His Tag is fused to the N-terminus of the protein. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12422
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

PGAM1 Human, Active

Phosphoglycerate Mutase 1 Human Recombinant, Active

Recombinant human PGAM1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 274 amino acids (residues 1-254) with a molecular weight of 30.9 kDa. This protein is fused to a 20 amino acid His Tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12588
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

PGAM1 Mouse

Phosphoglycerate Mutase 1 Mouse Recombinant

Recombinant PGAM1 Mouse, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 278 amino acids (1-254) with a molecular mass of 31.4kDa. This protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12669
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

PGAM1 Mouse, Active

Phosphoglycerate Mutase 1 Mouse Recombinant, Active

Recombinant Mouse PGAM1, expressed in E.coli, is a non-glycosylated polypeptide chain. This monomeric protein consists of 278 amino acids (residues 1-254), with a molecular weight of 31.4kDa. It features a 24 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12729
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Mutases are a subclass of isomerase enzymes that catalyze the transfer of functional groups within a molecule, resulting in the isomerization of the molecule. They play a crucial role in various metabolic pathways by facilitating the rearrangement of atoms within a substrate. Mutases are classified based on the type of functional group they transfer, such as phosphomutases, which transfer phosphate groups, and carbon mutases, which transfer carbon groups.

Biological Properties

Key Biological Properties: Mutases exhibit high substrate specificity and catalytic efficiency. They often require cofactors such as metal ions or coenzymes to function effectively.

Expression Patterns: The expression of mutases varies across different tissues and developmental stages. Some mutases are ubiquitously expressed, while others are tissue-specific.

Tissue Distribution: Mutases are found in various tissues, including the liver, muscle, and brain. Their distribution is closely linked to the metabolic needs of the tissue.

Biological Functions

Primary Biological Functions: Mutases play a pivotal role in metabolic pathways, including glycolysis, gluconeogenesis, and the citric acid cycle. They facilitate the conversion of substrates into intermediates that are essential for energy production and biosynthesis.

Role in Immune Responses: Some mutases are involved in the immune response by modulating the activity of immune cells and influencing the production of signaling molecules.

Pathogen Recognition: Certain mutases participate in the recognition and response to pathogens by altering the structure of molecules involved in pathogen detection.

Modes of Action

Mechanisms with Other Molecules and Cells: Mutases interact with various molecules, including substrates, cofactors, and regulatory proteins. These interactions are essential for their catalytic activity and regulation.

Binding Partners: Mutases often form complexes with other enzymes or structural proteins, which can enhance their stability and activity.

Downstream Signaling Cascades: The activity of mutases can trigger downstream signaling pathways that regulate cellular processes such as metabolism, growth, and differentiation.

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of mutases are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms.

Transcriptional Regulation: The transcription of mutase genes is controlled by various transcription factors and signaling pathways that respond to cellular and environmental cues.

Post-Translational Modifications: Mutases undergo post-translational modifications such as phosphorylation, acetylation, and ubiquitination, which can modulate their activity, stability, and interactions with other proteins.

Applications

Biomedical Research: Mutases are valuable tools in biomedical research for studying metabolic pathways and disease mechanisms. They are used in assays to measure enzyme activity and substrate concentrations.

Diagnostic Tools: Mutase activity can serve as a biomarker for certain diseases, and assays measuring their activity are used in clinical diagnostics.

Therapeutic Strategies: Mutases are potential targets for drug development, and modulating their activity can have therapeutic benefits in metabolic disorders, cancer, and infectious diseases.

Role in the Life Cycle

Development: Mutases are essential for proper development, as they regulate metabolic pathways that provide energy and biosynthetic precursors for growing tissues.

Aging: The activity of mutases can decline with age, leading to metabolic imbalances and contributing to age-related diseases.

Disease: Mutase dysfunction is associated with various diseases, including metabolic disorders, cancer, and neurodegenerative conditions. Understanding their role in disease can inform the development of therapeutic interventions.

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