Tryptophan Inhibitor

Solid. Powder

98.00%

Store at -20 degree C for 3 years powder
-80 degree C for 2 years in solvent

204.22

<1mg/ml refers to the product slightly soluble or insoluble

C11H12N2O2

C1=CC=C2C(=C1)C(=CN2)CC(C(=O)O)N

54-12-6

Others

Herein we tested whether the introduction of analogous, 'pseudo-pathogenic' Tryptophan mutations immediately after the bn cysteine (bn+1) in other cbEGF domains also caused protein folding/secretion challenges. We found that introduction of Tryptophan mutations into each of the four other F3 canonical cbEGF domains caused a significant reduction in protein secretion ranging from 2.7 to 56% of wild-type (WT) F3 levels. Surprisingly, an R185W mutation in the first canonical cbEGF domain of F3 yielded the highest amount of secretion among the F3 Tryptophan mutants, and its secretion defect could be rescued to near WT levels (95%) after growth temperature reduction. Interestingly, when similarly positioned Tryptophan mutations were introduced into any of the canonical cbEGF domains of the highly homologous protein, fibulin-5 (F5), there was no effect on secretion. In an attempt to make F3 tolerant of Tryptophan residues (like F5), we genetically engineered F3 to have a higher sequence homology with F5 by deleting three insert regions present in F3, but not F5. However, deletion of one or more of these regions did not have a beneficial effect on R345W F3 secretion.