Pedro J. Llanos, Kristina Andrijauskaite, Vijay V. Duraisamy, Francisco Pastrana, Erik L. Seedhouse, Sathya Gangadharan, Leonid Bunegin and Mariel Rico
% duplicate packets in the data and a 0.3% dropped packet count as provided by the NanoRacks team to maximize the data collection for the next mission. The data observed in Figure 5 were provided by Blue Origin at 100 Hz and shows evidence of some very short shock events at CC separation ( Figure 5d), drogue chute deployment ( Figure 5g), and main chute deployment ( Figure 5h). These pulses are only a single data point wide, suggesting pulse durations <100 ms. These pulses were the result of the reaction control system when firing their thrusters right after capsule
L. Chen, E.A. Selimovic, M. Daunis, T.A. Bayers T, L.J. Vargas, I.T. O’Brien, C.B. McEnroe, A.E. Kozerski, A.C. Vanhoover, W.D. Gray and J.F. Caruso
; greater (p<0.05) than the other treatment means for that velocity. PT, peak torque; SEM, standard error of the mean.
Knee extensor TTPT (mean ± SEM in seconds) results.
SEM, standard error of the mean; TTPT, time to peak torque
Kibrom M. Alula, James H. Resau and Osman V. Patel
Effect of HG on Temporal Distribution of VDR Protein
The time-trend quantitative profile of mammary gland lobular VDR in SC and HG rats is depicted in Figure 2e and f . VDR protein concentration declined by about 50% (p<0.001) in SC animals during the transition from G20 (3.6±0.24 px) to P1 (1.8±0.05 px). Subsequently, the VDR levels increased approximately fivefold (p<0.001) at P3 (10.8±0.52 px) versus P1 levels in the SC group ( Fig. 2e) . On the other hand, the HG-G20 (7.03±0.28 px) rats had about 300% (p<0.001) more VDR expressed than their P1 (2.09±0.11 px
Arayik Martirosyan, Lawrence J. DeLucas, Christina Schmidt, Markus Perbandt, Deborah McCombs, Martin Cox, Christopher Radka and Christian Betzel
reaction was incubated for 1 h at room temperature with continuous stirring. The labeled tetramer was separated from free dye using a Sephadex® G-25 prepacked gel filtration column. The column was first equilibrated with PBS buffer and then loaded with a reaction mixture and eluted with PBS buffer solution. Labeling degree (DOL) of tetramer was calculated using following calculations:
Protein concentration ( M ) = [ A 280 − ( CF × A 494 ) ] × dilution factor ε ( protein ) $$ \text
and 3 g during ascent for about 2.5 min, between 1 g and 5 g during descent for nearly 1.5 min, and some instances with accelerations between 2 g and 3 g during parachute recovery for almost 30 sec, total time of about 5 min. Then they were either placed in 2, 5, or 15 mL tubes with and without cytokines and maintained in water baths at the following temperatures: 37℃, 30℃, 34℃, and 40℃ for various time points. Cells were also exposed to other thermal baths at 10℃ and 20℃ to account for extreme temperature variations during launch conditions as we will refer to