Figure 1.
Figure 1. Cy3-KCK-hVASPCCC-SSA and unlabeled hVASP are functionally equivalent. (A) Cartoon of Cy3-KCK-hVASP1-380aa (C7S, C64S, C334A) domain architecture. (B) Cosedimentation of 2 µM F-actin with VASP, KCK-VASP, or Cy3-KCK-VASP (0–5 µM monomeric concentrations). VASP migrates slower than predicted. Note that Cy3-VASP is slightly brighter due to spectral overlap with SYPRO Red. (C) Pyrene actin polymerization assay. VASP and KCK-VASP (63 nM tetrameric/250 nM monomeric) equally enhance the polymerization of 2 µM actin (5% pyrene labeled). (D) Concentration-dependent increase in the barbed end polymerization rate of single actin filaments in the presence of 1 µM Mg-ATP-actin (30% Alexa Fluor 488, 50–100 mM KCl) in the presence of VASP or Cy3-VASP. Error bars indicate SD (n ≥ 30 filaments from ≥2 slides).

Cy3-KCK-hVASPCCC-SSA and unlabeled hVASP are functionally equivalent. (A) Cartoon of Cy3-KCK-hVASP1-380aa (C7S, C64S, C334A) domain architecture. (B) Cosedimentation of 2 µM F-actin with VASP, KCK-VASP, or Cy3-KCK-VASP (0–5 µM monomeric concentrations). VASP migrates slower than predicted. Note that Cy3-VASP is slightly brighter due to spectral overlap with SYPRO Red. (C) Pyrene actin polymerization assay. VASP and KCK-VASP (63 nM tetrameric/250 nM monomeric) equally enhance the polymerization of 2 µM actin (5% pyrene labeled). (D) Concentration-dependent increase in the barbed end polymerization rate of single actin filaments in the presence of 1 µM Mg-ATP-actin (30% Alexa Fluor 488, 50–100 mM KCl) in the presence of VASP or Cy3-VASP. Error bars indicate SD (n ≥ 30 filaments from ≥2 slides).

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