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AB289791

Recombinant human PGAM1 protein (Active) (His tag N-Terminus)

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(1 Publication)

Recombinant human PGAM1 protein (Active) is a Human Full Length protein in the 1 to 254 aa range with >=90% purity and suitable for SDS-PAGE and Functional studies. The predicted molecular weight of ab289791 protein is 30.9 kDa.

- Save time and ensure accurate results - use our recombinant PGAM1 protein as a control
- Optimal protein bioactivity, stability and reproducibility

View Alternative Names

PGAMA, CDABP0006, PGAM1, Phosphoglycerate mutase 1, BPG-dependent PGAM 1, Phosphoglycerate mutase isozyme B, PGAM-B

1 Images
SDS-PAGE - Recombinant human PGAM1 protein (Active) (His tag N-Terminus) (AB289791)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human PGAM1 protein (Active) (His tag N-Terminus) (AB289791)

15% SDS-PAGE (3μg)

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific activity is >300 units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C

Accession

P18669

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.24% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Ensure the validity of your result using our recombinant human PGAM1 protein ab289791 as a positive control in SDS-PAGE.


Check out our protein gel staining guide for SDS-PAGE here

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKAKK","proteinLength":"Full Length","predictedMolecularWeight":"30.9 kDa","actualMolecularWeight":null,"aminoAcidEnd":254,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P18669","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Phosphoglycerate mutase 1 (PGAM1) also known as PGAM-M or brain PGAM is an enzyme with a molecular weight of approximately 29 kDa. PGAM1 catalyzes the conversion of 3-phosphoglycerate to 2-phosphoglycerate in the glycolytic pathway. This enzyme is expressed in a wide range of tissues with significant levels found in brain and muscle cells. It plays an important role in energy metabolism by facilitating the intermediate steps of glycolysis.
Biological function summary

PGAM1 acts within the glycolysis and gluconeogenesis processes interacting with other metabolic enzymes to maintain cellular energy balance. It functions as a part of the phosphoglycerate mutase enzyme complex. The activity of PGAM1 is important for optimal glycolytic flux directly linking it to energy production and regulation within the cell. By maintaining the concentrations of glycolytic intermediates PGAM1 supports various cellular processes that depend on energy generated through glycolysis.

Pathways

The activity of PGAM1 integrates glycolysis with other vital metabolic processes in the cell. One key pathway involving PGAM1 is the glycolytic pathway where it collaborates with the enzymes phosphoglycerate kinase and enolase to efficiently drive the conversion of glucose to pyruvate. Additionally PGAM1 is linked to the pentose phosphate pathway where it indirectly influences nucleotide biosynthesis and antioxidant responses by affecting the flux of metabolites into the pathway.

PGAM1's involvement in energy metabolism connects it to various cancer types. Many cancer cells display elevated levels of PGAM1 which can promote enhanced aerobic glycolysis also known as the Warburg effect. This shift in metabolism is associated with increased cancer cell proliferation and survival. Furthermore PGAM1's interaction with other proteins like p53 a tumor suppressor highlights its potential role in tumorigenesis where dysregulation of these interactions can contribute to cancer progression.

Specifications

Form

Liquid

General info

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate (PubMed : 23653202). Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate (PubMed : 23653202).

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Post-translational modifications

Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme.

Product protocols

Target data

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate (PubMed : 23653202). Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate (PubMed : 23653202).
See full target information PGAM1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Synthetic biology (Oxford, England) 8:ysad016 PubMed38149045

2023

Cell-free expression of RuBisCO for ATP production in the synthetic cells.

Applications

Unspecified application

Species

Unspecified reactive species

Shugo Sugii,Katsumi Hagino,Ryo Mizuuchi,Norikazu Ichihashi
View all publications

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