PGAM1 Human

Phosphoglycerate Mutase 1 Human Recombinant
Cat. No.
BT12422
Source
Escherichia Coli.
Synonyms
Phosphoglycerate mutase isozyme B, PGAM-B, PGAMA.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

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.

Product Specs

Introduction
Phosphoglycerate mutase 1 (PGAM1) is an enzyme that plays a crucial role in glucose metabolism. It catalyzes the reversible conversion of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM1 also participates in the metabolism of 2,3-bisphosphoglycerate (2,3-BPGA). The enzyme exists as a dimer and exhibits tissue-specific isozyme variations, including a slow-migrating muscle isozyme (MM), a fast-migrating brain isozyme (BB), and a hybrid form (MB). Mutations in the PGAM1 gene can lead to muscle phosphoglycerate mutase deficiency, a metabolic disorder also known as glycogen storage disease X.
Description
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.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The PGAM1 protein solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8), 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the protein solution should be stored at 4°C. For long-term storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) to the solution before freezing can enhance stability during long-term storage. Repeated freezing and thawing of the protein solution should be avoided.
Purity
Analysis by SDS-PAGE indicates a purity of greater than 90%.
Synonyms
Phosphoglycerate mutase isozyme B, PGAM-B, PGAMA.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR KAMEAVAAQG KAKK.

Product Science Overview

Structure and Function

PGAM1 belongs to the phosphoglycerate mutase family and is encoded by the PGAM1 gene located on chromosome 10 in humans . The enzyme is composed of 254 amino acids and has a molecular weight of approximately 28.8 kDa . It functions by using 2,3-bisphosphoglycerate as a cofactor to facilitate the interconversion of 3-PGA and 2-PGA .

Biological Significance

PGAM1 is essential for efficient energy production in cells. It is involved in both glycolysis and gluconeogenesis, making it a key player in cellular metabolism . The enzyme is found in various tissues, including the brain, muscle, and liver, highlighting its importance in different physiological processes .

Clinical Relevance

Mutations or dysregulation of the PGAM1 gene have been associated with several diseases. For instance, PGAM1 is upregulated in certain types of cancer, such as leukemia, where it supports the metabolic needs of rapidly proliferating cancer cells . This makes PGAM1 a potential therapeutic target for cancer treatment .

Recombinant PGAM1

Human recombinant PGAM1 is produced using recombinant DNA technology, which involves inserting the human PGAM1 gene into a suitable expression system, such as bacteria or yeast, to produce the enzyme in large quantities. This recombinant enzyme is used in various research applications, including studies on glycolysis, cancer metabolism, and enzyme kinetics.

Research and Applications

PGAM1 is widely studied for its role in metabolism and disease. Researchers use human recombinant PGAM1 to investigate its function, regulation, and potential as a drug target. The enzyme’s activity can be measured using specific assays, and its structure can be analyzed using techniques like X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy .

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THE BIOTEK
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