Fig 5.

 Antibody production and p8 detection. p8 synthesized in transformed Escherichia coli was purified on TALON affinity resin for use as antigen. Protein samples were electrophoresed in sodium dodecyl sulfate (SDS) polyacrylamide gels and either stained with Coomassie blue (A) or transferred to nitrocellulose and detected with Omniprobe (B). Lane 1: extract from bacteria transformed with p8 cDNA; lane 2: extract from bacteria transformed with vector only; lane 3: purified p8. Lanes 1 and 2: 30 μg of protein in A and 10 μg in B; lane 3: 3 μg of protein in A and 0.4 μg in B. Protein extracts prepared from diapause-destined (C, D) and nauplii-destined (E, F) Artemia embryos at daily intervals postfertilization, were electrophoresed in SDS polyacrylamide gels and either stained with Coomassie blue (C, E) or transferred to nitrocellulose and probed with antibody to p8 (D, F). Lanes 1–6: day 0 (fertilization) to day 5 postfertilization, respectively. All lanes received 30 μg of protein. M, molecular mass markers of 116.0, 66.2, 45.0, 35.0, 25.0, 18.4, and 14.4 kDa