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AB198455

Recombinant human PHGDH/Malate dehydrogenase protein (His tag C-Terminus)

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(1 Publication)

Recombinant human PHGDH/Malate dehydrogenase protein (His tag C-Terminus) is a Human Full Length protein, in the 1 to 533 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE, FuncS.

View Alternative Names

PGDH3, PHGDH, D-3-phosphoglycerate dehydrogenase, 3-PGDH, 2-oxoglutarate reductase, Malate dehydrogenase

2 Images
Functional Studies - Recombinant human PHGDH/Malate dehydrogenase protein (His tag C-Terminus) (AB198455)
  • FuncS

Supplier Data

Functional Studies - Recombinant human PHGDH/Malate dehydrogenase protein (His tag C-Terminus) (AB198455)

Specific activity of ab198455.

SDS-PAGE - Recombinant human PHGDH/Malate dehydrogenase protein (His tag C-Terminus) (AB198455)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human PHGDH/Malate dehydrogenase protein (His tag C-Terminus) (AB198455)

4-20% SDS-PAGE analysis of ab198455 with Coomassie staining.

Predicted Molecular Weight : 58 kDa

Apparent Molecular Weight : 58 kDa

Key facts

Purity

>80% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: ≥80 pmol/min/μg
Assay Conditions: The reaction mixture contained 100 mM Tris-HCl, pH 8.8, 400 mM NaCl2, 0.2 mM DTT, 2.5 mM 3-phospho-D-glyceric acid, 1 mM NAD, and various amount of ab198455 in a final volume of 50 μL. Reactions were initiated with the addition of ab198455, and the increase in NADH fluorescence (Ex340/Em460 nm) was continuously monitored for 10 min at room temperature.

Accession

O43175

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Preservative: 1.16% Imidazole Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.04% Sorbitan monolaurate, ethoxylated, 0.02% Potassium chloride

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

This product was previously labelled as PHGDH

Sequence info

[{"sequence":"MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHFHHHHHH","proteinLength":"Full Length","predictedMolecularWeight":"58 kDa","actualMolecularWeight":null,"aminoAcidEnd":533,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"O43175","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

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

Phosphoglycerate dehydrogenase also known as PHGDH is an enzyme that catalyzes the conversion of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It has an approximate mass of 57 kDa. The PHGDH is located in the cytoplasm and mitochondria where it plays a role in serine biosynthesis. Malate dehydrogenase might also get mentioned together with PHGDH because both enzymes link to metabolic processes. The expression of PHGDH is noted in various tissues with higher levels observed in some cancer cells.
Biological function summary

PHGDH is essential for the serine synthesis pathway and cellular metabolism regulation. It does not form part of large complexes but operates independently to convert substrates necessary for cell growth and proliferation. The enzyme supports the synthesis of nucleotides and proteins impacting cell cycle and survival. Researchers investigate PHGDH to understand its role in metabolic reprogramming especially in cancer cells.

Pathways

PHGDH is important in the serine biosynthesis pathway which is part of the larger glycolytic process. It connects to pathways that contribute to cellular carbon metabolism and energy production. PHGDH interacts with glutamate dehydrogenase protein (GDH) and also influences one-carbon metabolism and redox balance within the cell. These pathways play important roles in providing building blocks for nucleotide and lipid biosynthesis.

PHGDH has relevance in cancer and neurological disorders. Alterations and overexpression of PHGDH have been linked to oncogenesis and tumor growth particularly in breast cancer. The enzyme also associates with neurodegenerative diseases as proper serine levels are important for neuron function. In both conditions PHGDH becomes connected with glutamate dehydrogenase as alterations can impact amino acid metabolism and neurotransmitter balance. The study of PHGDH inhibitors is gaining attention for therapeutic potentials in these diseases.

Specifications

Form

Liquid

General info

Function

Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Product protocols

Target data

Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
See full target information PHGDH

Publications (1)

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

Nature chemical biology 13:494-500 PubMed28263965

2017

L-2-Hydroxyglutarate production arises from noncanonical enzyme function at acidic pH.

Applications

Unspecified application

Species

Unspecified reactive species

Andrew M Intlekofer,Bo Wang,Hui Liu,Hardik Shah,Carlos Carmona-Fontaine,Ariën S Rustenburg,Salah Salah,M R Gunner,John D Chodera,Justin R Cross,Craig B Thompson
View all publications

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