Product Description
Size: 50µg
Recombinant Human PHOSPHO2 protein is a Human Full Length protein, in the 1 to 241 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
Key facts
Purity:>85% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:Mass Spec, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:Q8TCD6,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
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
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
PHOSPHO2 also known as Phosphatase Orphan 2 is a protein that functions mechanically as a phosphatase involved in removing phosphate groups from substrates. This protein has an approximate mass of 31 kDa. PHOSPHO2 is expressed in various tissues including the liver and kidney where it acts in regulating phosphorylation states important for cellular function.
Biological function summary
The activity of PHOSPHO2 significantly impacts several cellular processes. It is not known to be part of any substantial complexes. Its enzymatic activity regulates the phosphorylation of proteins this is important for signal transduction and cellular communication. By modulating phosphoproteins PHOSPHO2 ensures balanced cellular activities like response to environmental stimuli.
Pathways
PHOSPHO2 participates in or influences the phosphate metabolism pathway and plays a role in regulatory networks that control signaling pathways. It interacts with other proteins such as phosphoproteins in these pathways. While further research is needed to elucidate its exact partners fully PHOSPHO2's function in phosphorylation suggests general interactions with a variety of signaling proteins within these biological pathways.
There is evidence suggesting a link between PHOSPHO2 activity and metabolic disorders like diabetes. Abnormal regulation of phosphorylation can lead to improper signal transduction contributing to disease pathogenesis. PHOSPHO2 also shares a functional relationship with other phosphatases like PPM1A in these conditions which collectively affects metabolic homeostasis. Understanding these connections may help in developing therapeutic strategies targeting metabolic dysfunctions.
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Collaboration
Tony Tang
Email: Tony.Tang@iright.com
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