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glutathione reductase fad

glutathione reductase fad is made up of highly conserved domains such as two Rossmann fold domains Schematic representation of the role

SKU: 20711053294

4.2
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Description

dihexa binds hepatocyte growth factor with high affinity, with a value of 65 pM, and potentiates its activity on the receptor c-Met

glutathione reductase fad is made up of highly conserved domains such as two Rossmann fold domains Schematic representation of the role

Applications in Research As a molecular tool for studying IGF-1 receptor binding and activation dynamics Investigation of growth factormediated intracellular signalling pathways In vitro studies comparing modified and native IGF-1 analogues Use as a reference compound in endocrine and peptide signalling research Handling, Reconstitution & Stability Weigh under dry conditions

glutathione reductase fad is made up of highly conserved domains such as two Rossmann fold domains Schematic representation of the role

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glutathione reductase fad is made up of highly conserved domains such as two Rossmann fold domains Schematic representation of the role

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glutathione reductase fad is made up of highly conserved domains such as two Rossmann fold domains Schematic representation of the role
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