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AB100983

Recombinant Human GMPR2 protein

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(1 Publication)

Recombinant Human GMPR2 protein is a Human Full Length protein, in the 1 to 348 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

GMP reductase 2, GMPR 2, Guanosine 5'-monophosphate oxidoreductase 2, Guanosine monophosphate reductase 2, GMPR2

1 Images
SDS-PAGE - Recombinant Human GMPR2 protein (AB100983)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human GMPR2 protein (AB100983)

15% SDS-PAGE showing ab100983 (3 μg) at approximately 40 kDa.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q9P2T1

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl, 0.0154% (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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC","proteinLength":"Full Length","predictedMolecularWeight":"40 kDa","actualMolecularWeight":null,"aminoAcidEnd":348,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q9P2T1","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

The GMPR2 protein also known as Guanosine Monophosphate Reductase 2 plays an important role in nucleotide metabolism by converting guanosine monophosphate (GMP) into inosine monophosphate (IMP). This enzyme has a molecular weight of approximately 38 kDa and operates similarly to other members of the IMPDH/GMPR family. GMPR2 expression occurs in various tissues although it is especially active in those requiring active nucleotide turnover like the liver and lymphoid tissues. Its enzymatic activity contributes to maintaining a balanced supply of nucleotides within the cell.
Biological function summary

GMPR2 influences purine nucleotide metabolism which impacts cellular proliferation and differentiation processes. This protein does not operate alone; it frequently associates with other enzymes in nucleotide synthesis and degradation pathways ensuring efficient metabolic flow. By modulating the concentrations of GMP and IMP GMPR2 directly affects the synthesis of critical nucleic acids and energy carriers in the cell. This control is essential for cells undergoing rapid growth or engagement in vigorous metabolic activities.

Pathways

GMPR2 functions within the salvage and de novo pathways of purine metabolism. It plays a significant role in the salvage pathway by recycling guanosine nucleotides which complements the actions of enzymes like IMP dehydrogenase. Together these proteins ensure proper cellular nucleotide levels important for DNA/RNA synthesis and cell signaling. This coordination within the pathways highlights GMPR2's importance in maintaining cellular health and function.

GMPR2 has connections to cancer and immunodeficiency. Altered GMPR2 activity can disrupt nucleotide balance potentially contributing to the uncontrolled cell proliferation observed in cancers. Additionally shifts in nucleotide metabolism may impair immune cell function leading to immunodeficiency conditions. In these contexts proteins like GMP synthase may interact with GMPR2 influencing the disease outcome due to their shared roles in nucleotide metabolism. Understanding these interactions provides further insight into GMPR2's relevance in health and disease contexts.

Specifications

Form

Liquid

Additional notes

ab100983 is purified using conventional chromatography techniques.

General info

Function

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (PubMed : 12009299, PubMed : 12669231, PubMed : 16359702, PubMed : 22037469). Plays a role in modulating cellular differentiation (PubMed : 12669231).

Sequence similarities

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides (PubMed : 12009299, PubMed : 12669231, PubMed : 16359702, PubMed : 22037469). Plays a role in modulating cellular differentiation (PubMed : 12669231).
See full target information GMPR2

Publications (1)

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

Scientific reports 11:21315 PubMed34716371

2021

Hypothalamic administration of sargahydroquinoic acid elevates peripheral thermogenic signaling and ameliorates high fat diet-induced obesity through the sympathetic nervous system.

Applications

Unspecified application

Species

Unspecified reactive species

Doyeon Kim,Yuna Lee,Hyeung-Rak Kim,Yeo Jin Park,Hongik Hwang,Hyewhon Rhim,Taek Kang,Chun Whan Choi,Bonggi Lee,Min Soo Kim
View all publications

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