Sample Preparation. Users are responsible for preparing their own samples; however, the Facility Manager must approve the prepared samples (see #6) and may disallow samples that are not stable and could damage the instrument. The Facility Manager will train Members in sample preparation and may provide assistance in special cases, but in general Members are responsible for their own samples.
Sample Preparation. (1) Sample to be processed should correlate with stage and site to be treated.
(2) Cut one 5 µM section, mount on glass slide.
(3) Cut four 10 µM sections, mount on four separate regular glass slides. Glass slides should be regular glass, uncoated and uncharged. Do not bake slides and do not use coverslip. Slides must contain a sufficient quantity of tumor tissue to be successfully microdissected.
(4) Send above referenced samples or specimens by overnight delivery in approved slide holder, placed in a bubble-lined envelope and in a Federal Express Diagnostic Specimen Envelope, to the laboratory designated by Response at Response's direction. Portions of this Exhibit were omitted and have been filed separately with the Secretary of the Commission pursuant to the Company’s application requesting confidential treatment under Rule 406 of the Securities Act.
Sample Preparation a. Laboratory Molded Specimens - Use cylindrical specimens that have been compacted using the gyratory compactor (AASHTO T 312). Specimen diameter must be 6 inches (150 mm) and a specimen height must be 4.5 inches +/- 0.2 inches (115 +/- 5 mm).
Sample Preparation. ]” shall mean, individually and collectively, the major [...***...]
Sample Preparation. 1. Add 1 µL Activator to 100 µL patient sample or control. Mix and allow to sit at room temperature for 10 minutes.
2. If testing fewer than 10 samples, remove one Applicator Blade Assembly from the packaging. If testing 11 to 20 samples, remove two disposable Applicator Blade Assemblies from the packaging.
3. Place the Applicator Blade into the vertical slot 6 in the Applicator Assembly. If using two Applicator Blades, place them into the vertical slots numbered 6 and 12.
Sample Preparation. Human calmodulin (CaM) was expressed and purified in Escherichia coli BL21(DE3) cells, as described F xxxxx://xxx.xxx/10.1021/jacs.2c02201 previously.9 Two site-directed mutations at A17C and A128C in the NTD and CTD domains of CaM, respectively, were introduced as sites of attachment for the nitroxide spin-labels.9 Full deuteration was achieved by growing the bacteria in deuterated minimal medium, with U-[12C/2H]-glucose as the sole carbon source. R1 nitroxide labeling was carried out with S-(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H- pyrrol-3-yl)methyl methanesulfonothioate (MTSL; Toronto Research Chemicals), as described previously.9 The purity of A17C-R1/ A128C-R1 nitroxide-labeled calmodulin was verified by mass spectrometry. Solutions for DEER EPR comprised 50 μM CaM (A17C-R1/ A128-R1), 8 mM CaCl2, 100 mM NaCl, 25 mM d-HEPES pH 6.4, and 20% (v/v) d8-glycerol, placed in 1.0 mm inner diameter (1.2 mm outer diameter) quarts EPR tubes (VitoCom). Freezing of the DEER samples was carried out using three different approaches: slow rate freezing (∼40 s) by placing the EPR tube in a −80 °C freezer;43 intermediate rate freezing (∼1.5 s) by directly placing the EPR tube in liquid N2;43 and rapid freeze-quenching (∼0.5 ms) by spraying a high- speed jet onto a spinning copper plate cooled to 77 K, as described previously.18,45 Q-Band DEER. Pulsed EPR data were collected at Q-band (33.8 GHz) and 50 K on a Bruker E-580 spectrometer equipped with a 150 W traveling-wave tube amplifier, a model ER5107D2 resonator, and a cryofree cooling unit, as described previously.52 DEER experiments were acquired using a conventional four-pulse sequence (Figure S1).53 The observer and XXXXX pump pulses were separated by ca. 90 MHz, with the observer π/2 and π pulses set to 12 and 24 ns, respectively, and the XXXXX π pulse to 10 ns. The pump frequency was centered at the Q-band nitroxide spectrum located at +40 MHz from the center of the resonator frequency. The τ1 value of 350 ns for the first echo period time was incremented eight times in 16 ns steps to average 2H modulation; the position of the XXXXX pump pulse was incremented in steps of Δt = 10 ns. The bandwidth of the overcoupled resonator was 120 MHz. All DEER echo curves were acquired for tmax = 7.5 μs, with the exception of the DEER echo curve for τ2 < 7.5 μs, where tmax was set to the value of τ2. DEER data were recorded with values of the dipolar evolution time T (=2τ2) set to 10, 15, 20, 25, 30, and 35 μs. Measurement t...
Sample Preparation. In order to determine if a patient is eligible to donate a unit of blood, 4 vials of blood will be drawn according to STBTC SOPs. Blood counts and infectious disease screening tests will be performed on these samples. If eligible, approximately 450 milliliters of blood will be collected from study participants in a CP2D (Citrate Phosphate Double Dextrose) bag at STBTC according to their SOPs. Peripheral blood mononuclear cells (PBMCs) from this sample will be isolated by XBiotech scientists, and RNA will be extracted. At this point, the sample can be flash frozen and stored at -80° Celsius for future testing. The plasma will be stored at -80°C freezer for further testing as well. If necessary to isolate additional PBMCs, donors may be asked to donate a second unit of whole blood. If a second blood draw is requested, this should be scheduled at least 56 days after the initial unit of blood is drawn.
Sample Preparation. Phase I: Samples for initial screening will be drawn according to STBTC standard operating procedures. The residual volume, 2-3 ml of Na-EDTA Plasma will be stored at -65° Celsius pending the screening tests for infections disease. Only those samples that are negative for blood-borne pathogens will be shipped to XBiotech. These samples will be shipped on dry ice via courier to XBiotech in weekly batches. Scientists at XBiotech will use these samples to test for the presence of various antibody patterns of interest using a FACS followed by a proprietary ELISA.
Sample Preparation. Tree bark samples will be prepared and analyzed in basic accordance with the procedures specified in SOP EPA-XXXXX-2012-12, Sampling and Analysis of Tree Bark for Asbestos (see Appendix B), with the following project modifications: 3 Copies of all Xxxxx Laboratory Modifications are available in the Xxxxx Lab eRoom. ▪ Only one 0.25 gram aliquot of the resulting ash residue (rather than the total mass) will be filtered. In brief, each sample is dried and ashed, and an aliquot of the resulting ash residue is acidified, suspended in water, and filtered. The resulting filter will be used to prepare a minimum of three grids using the grid preparation techniques described in Section 9.3 of ISO 10312:1995(E). Any remaining ash material will be archived for possible future analysis. For 10% of the tree bark samples, two additional ash aliquots will be prepared to filters and analyzed to gain an understanding of the within-sample variability. These samples will be selected post hoc by the FTL (or their designee) so that a range of tree bark levels are represented. Grids will be examined by TEM using high magnification (~20,000x) in basic accordance with the recording procedures described in ISO 10312:1995(E), as modified by SOP EPA-XXXXX-2012-
Sample Preparation. A total of 10 µg of IgG was digested using trypsin Gold. Samples were buffer exchanged into PBS to a concentration of 1 mg/mL. 10 µL of the protein solution was transferred into an Eppendorf vial and 4 µL of 0.5 mg/mL trypsin in 0.1 M acetic acid in water was added. The mixture was incubated for 1 h at 55°C with sonication. The sample pots were cooled to room temperature and 5 μL of the V-Tag labelling reagent was added directly to each digested sample. The samples were vortexed and briefly centrifuged. The labelling reaction was allowed to proceed for 1 hour at 37 °C. The V-Tag labelled samples were cleaned up using hydrophilic interaction amide LC-A cartridges. Each sample was loaded onto a primed cartridge in 76% aqueous acetonitrile. The cartridge was washed with 76% acetonitrile, 0.1% TFA in water solution. The purified V-Tag labelled glycopeptides were eluted from the amide cartridge in 0.5 mL of a solution containing 40 % ACN and 0.1% TFA in water.
