recombinant mouse egfr  (R&D Systems)

Journal: Molecular Cancer Therapeutics

Article Title: Targeted Nanofitin-drug Conjugates Achieve Efficient Tumor Delivery and Therapeutic Effect in an EGFR pos Mouse Xenograft Model

doi: 10.1158/1535-7163.MCT-22-0805

Figure Lengend Snippet: Intratumoral infiltration 90 minutres after systemic administration. A, Intratumoral infiltration of antiEGFR Nanofitins or Cetuximab, revealed by anti-HA and anti-IgG IHC, respectively. Host vasculature is revealed by anti-CD31 staining of consecutive slice sections. Zoom of selected regions illustrates EGFR labeling at the vessel proximity. B, Labeling index, on the basis of cells positively labeled, in the whole tumor. C, Labeling index relative to the distance from the closest blood vessel. ****, P < 0.0001; ***, P < 0.0005.

Article Snippet: Affinities were also determined for cysteine-free and HA-tagged ( ) Nanofitins (500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 0 nmol/L), either on human EGFR as described above, or on murine EGFR by using Recombinant Mouse EGFR Fc chimera protein (1280-ER, R&D Systems) for the loading step.

Techniques: Staining, Labeling

Journal: Molecular Cancer Therapeutics

Article Title: Targeted Nanofitin-drug Conjugates Achieve Efficient Tumor Delivery and Therapeutic Effect in an EGFR pos Mouse Xenograft Model

doi: 10.1158/1535-7163.MCT-22-0805

Figure Lengend Snippet: Biochemical profiles of Nanofitin-drug conjugates. A, Schematic representation of a Nanofitin-drug conjugate. The single chain of the Nanofitin scaffold (rainbow cartoon) is engineered to target EGFR by randomizing up to 14 amino acids (spheres in lieu of carbon alpha). Each Nanofitin is genetically fused to a C-terminal cysteine (gray/yellow stick) to allow the regioselective chemistry on the only thiol group. The vc-MMAE payload (structural formula) is coupled via its maleimide-based moiety (black) and releases the MMAE toxin (red) after proteolytic cleavage of the valine-citrulline linker (orange). B, UPLC-RP/MS profiles. Peaks were identified by ESI-MS spectral deconvolution to determine their mass. Percentages of corresponding species were determined from the area under the absorbance curves. C, Determination of the binding characteristics of the antiEGFR Nanofitin-drug conjugates D8-vc-MMAE (left) and B10-vc-MMAE (right) by biolayer interferometry on human EGFR, using the antiEGFR Nanofitin at concentrations of 500, 125, 31.25, and 7.81 nmol/L. Fittings are represented as solid red lines.

Article Snippet: Affinities were also determined for cysteine-free and HA-tagged ( ) Nanofitins (500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 0 nmol/L), either on human EGFR as described above, or on murine EGFR by using Recombinant Mouse EGFR Fc chimera protein (1280-ER, R&D Systems) for the loading step.

Techniques: Binding Assay

Journal: Molecular Cancer Therapeutics

Article Title: Targeted Nanofitin-drug Conjugates Achieve Efficient Tumor Delivery and Therapeutic Effect in an EGFR pos Mouse Xenograft Model

doi: 10.1158/1535-7163.MCT-22-0805

Figure Lengend Snippet: Affinity determination against human and mouse EGFR.

Article Snippet: Affinities were also determined for cysteine-free and HA-tagged ( ) Nanofitins (500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 0 nmol/L), either on human EGFR as described above, or on murine EGFR by using Recombinant Mouse EGFR Fc chimera protein (1280-ER, R&D Systems) for the loading step.

Techniques: