n65a mutant gene Search Results


n65a mutant gene  (GenScript corporation)
90
GenScript corporation n65a mutant gene
a , The FimH-binding high-mannose glycan attached to UMOD N275 is located in the groove between the β-hairpin and D10C domain moieties of the protein’s decoy module (left panel). Although this sequon is not conserved in the decoy module of GP2, the groove of the latter contains a different, but closely spaced, N-glycosylation site at position 65 (right panel). b , SEC analysis of the material eluted after incubating an E. coli periplasmic extract containing untagged FimH L with wild-type or <t>N65A</t> mutant GP2 decoy modules immobilized on IMAC beads (left panels). Reducing SDS-PAGE analysis of the corresponding peak fractions (right panels) shows that FimH L binds to the wild-type GP2 decoy module but not to the N65A mutant. n = 2.
N65a Mutant Gene, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/n65a mutant gene/product/GenScript corporation
Average 90 stars, based on 1 article reviews
n65a mutant gene - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


a , The FimH-binding high-mannose glycan attached to UMOD N275 is located in the groove between the β-hairpin and D10C domain moieties of the protein’s decoy module (left panel). Although this sequon is not conserved in the decoy module of GP2, the groove of the latter contains a different, but closely spaced, N-glycosylation site at position 65 (right panel). b , SEC analysis of the material eluted after incubating an E. coli periplasmic extract containing untagged FimH L with wild-type or N65A mutant GP2 decoy modules immobilized on IMAC beads (left panels). Reducing SDS-PAGE analysis of the corresponding peak fractions (right panels) shows that FimH L binds to the wild-type GP2 decoy module but not to the N65A mutant. n = 2.

Journal: Nature Structural & Molecular Biology

Article Title: Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH

doi: 10.1038/s41594-022-00729-3

Figure Lengend Snippet: a , The FimH-binding high-mannose glycan attached to UMOD N275 is located in the groove between the β-hairpin and D10C domain moieties of the protein’s decoy module (left panel). Although this sequon is not conserved in the decoy module of GP2, the groove of the latter contains a different, but closely spaced, N-glycosylation site at position 65 (right panel). b , SEC analysis of the material eluted after incubating an E. coli periplasmic extract containing untagged FimH L with wild-type or N65A mutant GP2 decoy modules immobilized on IMAC beads (left panels). Reducing SDS-PAGE analysis of the corresponding peak fractions (right panels) shows that FimH L binds to the wild-type GP2 decoy module but not to the N65A mutant. n = 2.

Article Snippet: A corresponding gene and an equivalent UMOD construct, as well as GP2 Δ31-59, Δ31-88 and N65A mutant genes, were also synthesized (GenScript) and all constructs were cloned into pLJ6, a mammalian expression vector derived from pHLsec3 (ref. ).

Techniques: Binding Assay, Glycoproteomics, Mutagenesis, SDS Page