BPGM Human

2,3-Bisphosphoglycerate Mutase Human Recombinant

BPGM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa. The BPGM is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12320
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

PGAM1 Human

Phosphoglycerate Mutase 1 Human Recombinant

PGAM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-254 a.a.) and having a molecular mass of 30.9 kDa. The PGAM1 is fused to a 20 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12422
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

PGAM1 Human, Active

Phosphoglycerate Mutase 1 Human Recombinant, Active

PGAM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids (1-254 a.a.) and having a molecular mass of 30.9 kDa. The PGAM1 is fused to a 20 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12588
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

PGAM1 Mouse

Phosphoglycerate Mutase 1 Mouse Recombinant

PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.
PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12669
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

PGAM1 Mouse, Active

Phosphoglycerate Mutase 1 Mouse Recombinant, Active

PGAM1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 278 amino acids (1-254) and having a molecular mass of 31.4kDa.
PGAM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12729
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

PGAM2 Human

Phosphoglycerate Mutase 2 Human Recombinant

PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.
PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12810
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PGAM2 Human, Active

Phosphoglycerate Mutase 2 Human Recombinant, Active

PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.
PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12899
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PGM1 Human

Phosphoglucomutase 1 Human Recombinant

PGM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 585 amino acids (1-562 a.a) and having a molecular mass of 63.8kDa.
PGM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12943
Source
Escherichia Coli.
Appearance
Sterile Filtered clear colorless solution.

PGM2 Human

Phosphoglucomutase 2 Human Recombinant

PGM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 635 amino acids (1-612 a.a) and having a molecular mass of 70.7kDa. PGM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13009
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PMM1 Human

Phosphomannomutase 1 Human Recombinant

PMM1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 282 amino acids (1-262 a.a.) and having a molecular mass of 31.9kDa. The PMM1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13095
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
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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