eamag/protocols-with-steps huggingface dataset:
TITLE: Adquisición Desideratas Biblioteca UCAM
AUTHORS: Antonio Rex Alegria

[DESCRIPTION]
Procedimiento para la Adquisición de material bibliográfico

[STEPS]
1. Ve a la página web de la Biblioteca de la UCAM  https://www.ucam.edu/biblioteca

  

2. Pulsa en el icono de Adquisiciones

  

3. Se abre una nueva pantalla.

  

4. Seleccionamos el icono de Solicitud de Adquisiciones/Soporte.

  

5. Nos identificamos con nuestro usuario y contraseña.

  

6. Introducimos los datos que nos solicita el soporte de Solicitud Desideratas Biblioteca.

  

7. Cuando tengamos los datos pulsamos ENVIAR y nos confirman que la solicitud ha sido dada de alta. A la persona encargada de tramitar la solicitud le llega un email.
TITLE: iPad_Lidar_surface_roughness_processing
AUTHORS: Alex White

[DESCRIPTION]
This protocol was used to process LIDAR data acquired over 3-m transects of forest floor, using an Apple iPad Pro 2022 app entitled 3D Scanner App in “LIDAR Advanced” mode set to the smallest possible maximum depth (30 cm) and resolution (5 mm), as documented in "Soil Surface Roughness in Temperate Forest During SMAPVEX19-22" by Walker et al. (2024).

[STEPS]
1. Open CloudCompare.


2. Open textured output file:
3. Select the file in the DB Tree on the left. 
    
    A bounding box will appear around the mesh. 
 

4. Click the Cross Section icon in the toolbar. 
 

2.1. Click the folder icon. 
 

2.2. Navigate to a transect folder (e.g. MA404-1-EW_20_02_48) in Box > SMAPVEX22_data > MA_lidar_scans.
Load from Box Drive, or download files to PC and load from there.
There are 36 surface roughness transects, in folders named according to the site (e.g. MA404), plot (1-3), and orientation (NS or EW). Skip any BD folders.
2.3. Open "textured_output.obj".

    The object will appear in the 3D view.
5. Set box thickness to length = 3.0, width = 0.01, and leave height unchanged.

X,Y,Z labeling differs between files. Compare the handle colors with the axis labels in the lower right corner of the 3D view to determine which is which.
6. Click left-hand icon under "Slices" to export selection as new entities, then close the toolbox. 
 

7. Uncheck the original "textured_output" file in the DB Tree to view the result.
8. Select the new object ("textured_output.section") in the DB Tree, click the Save icon in the toolbar, and save in the original folder as "textured_output_slice_3m_1cm.obj". File type should be OBJ.
9. Click the icon for "Sample points on a mesh" in the toolbar, enter 3000 for Points Number, and click OK. 
 
 

10. Select the new object ("textured_output.section.sampled") in the DB Tree, click the Save icon in the toolbar, and save in the original folder as type ASCII:
MA###-*-??_textured_output_slice_3m_1cm_sampled_3K.txt
### is site number, e.g. 404
* is plot number, e.g. 1
?? is transect orientation, e.g. EW
(from folder name)
Use default settings for ASCII file.
TITLE: Quantitate Library
AUTHORS: Eric L. Van Nostrand, Thai B. Nguyen, Chelsea Gelboin-Burkhart, Ruth Wang, Steven M. Blue, Gabriel A. Pratt, Ashley L. Louie, Gene W. Yeo

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">Profiling of RNA binding protein targets in vivo provides critical insights into the mechanistic roles they play in regulating RNA processing. The enhanced crosslinking and immunoprecipitation (eCLIP) methodology provides a framework for robust, reproducible identification of transcriptome-wide protein-RNA interactions, with dramatically improved efficiency over previous methods. Here we provide a step-by-step description of the eCLIP method, along with insights into optimal performance of critical steps in the protocol. In particular, we describe improvements to the adaptor strategy that enables single-end enhanced CLIP (seCLIP), which removes the requirement for paired-end sequencing of eCLIP libraries. Further, we describe the observation of contaminating RNA present in standard nitrocellulose membrane suppliers, and present options with significantly reduced contamination for sensitive applications. These notes further refine the eCLIP methodology, simplifying robust RNA binding protein studies for all users.</div></div>

[STEPS]
?. Quantitate using D1000 DNA Tapes for the Agilent TapeStation.
TITLE: AFM tip functionalization with glutaraldehyde
AUTHORS: George Lykotrafitis

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">Attach ligand protein to the AFM cantilever tip through functionalization. Further use it in the single molecule force spectroscopy to detect corresponding receptors on the sample surface (such as the red blood cell membrane).</div></div>

[STEPS]
?. Silanize the tip with 2% v/v 3-aminopropyltiethoxysilane (APTES) in acetone for 10 min at 25°C.
?. Rinse the tip with deionized (DI) water.
?. Immerse the tip in 0.5% v/v glutaraldehyde in DI water for 30 min at 25°C.
?. Rinse the tip with DI water.
?. Incubate the tip in protein solution (100-300 µg/mL, eg. 100µg/mL αvβ3 protein) for 30 min at 25°C.
?. Rinse the tip with DI water.
?. To block remaining aldehyde groups on the probe surface, treat the probe with 100 µg/mL bovine serum albumin (BSA) in tris buffered saline (TBS) for 1 min at 25°C.
?. Functionalized tips can be stored at 4°C in phosphate buffered saline (PBS) for 3 days.
TITLE: A New Absolute Quantification Method for Protein
AUTHORS: 181830691 

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block"><span>Absolute quantification method is essential for biological research. For absolute quantification, it is usually necessary to draw standard curves according to molecules with known concentrations. A new method using tandem mass spectrometry(</span><a href="https://www.creative-proteomics.com/services/absolute-quantification-aqua.htm" style = "text-decoration:underline;color:blue;cursor:pointer;"><span style = ":;:UNDERLINE;">AQUA mass spectrometry</span></a><span>) to make absolute quantification of multiple proteins was published on </span><span style = "font-style:italic;">Nature Communications</span><span> by researchers at the Massachusetts Institute of Technology, the Mayo Clinic and Seymour Fisher Scientific.</span></div></div>

[STEPS]
TITLE: Biochemical Measures of Neuropathy - GSSG (Non-Enzymatic)
AUTHORS: Eva Feldman

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block"><span style = "font-weight:bold;">Summary:</span></div><div class = "text-block">Oxidative stress is highly correlated with the metabolic changes caused by hyperglycemia. Increased levels of glucose overload mitochondria and result in the production of reactive oxygen species (ROS). In addition, the flow of excess glucose through cellular pathways decreases the cell’s normal ability to detoxify ROS. As a result, the neurons and axons of the peripheral nervous system contain increased levels of ROS and decreased antioxidant capacity. The following assays are used to measure these changes in rodent models of diabetic neuropathy. </div><div class = "text-block"><span style = "font-weight:bold;">Diabetic Complication:</span></div><div style = "text-align :; float : ;"><img style = "" src = "https://s3.amazonaws.com/pr-journal/biw64kcn.jpg" /></div></div>

[STEPS]
?. [Sample Preparation:]
Prior to dissection, perfuse tissue with PBS pH7.4 with 0.16 mg/ml heparin.1.  If using extract from GSH add 100 μl 0.04 M N-ethylmaleimide to 200 μl homogenate then skip to Performing the Assay or2. Label 3 sets 1.5 ml and 1 set of 0.6 ml micro centrifuge tubes.3. Prepare 3 M HClO4 and freeze.4. Keeping labeled 1.5ml tubes on dry ice, add 3 volumes of 3 M HClO4.5. Cut tissue into segments and weigh. (~10 mg)6. Place weighed segment in tube on top of HClO4.7. Place tubes in an alcohol bath maintained at –8º to –10ºC. and agitate 15 minutes or until the acid completely penetrates the tissue fragments. (Make sure the temperature does not go below –10º to completely extract the ice. (2 M HClO4 will freeze at -12ºC.)8. Add 333 μl of ddH²O for each 100 μl HClO4 and shake at 4ºC for 10 min. (May include 1 mM EDTA in ddH²O)9. Pull off 25 μl and place in a 0.6 ml micro-centrifuge tube for protein analysis.10. Centrifuge samples at 5000 x g for 10 min at 4º.11. Transfer supernatant to a new labeled tube. Discard protein precipitate.12. Immediately neutralize with 290 μl/ml of a mixture of 2 N KOH, 0.4 M imidazole base, and 0.4M KCl . (Leaving a solution at pH 7.)13. Centrifuge at 4000 x g for 5 min to precipitate insoluble KClO4.
?. [Performing the assay:]
Prepare standards as follows: (0-1000uM)1. On a clear 96 well plate add 40 µl standards to each well in duplicate. 2. Add 40 µl sample extract to each sample well in duplicate or triplicate. 3. Add 160 µl imidazole-HCl buffer to each well. Add 0.2-10 µM NADPH 4. Begin reaction by adding 0.3 U of glutathione reductase. 5. Set up Fluroskan layout and area.. 6. Read using 340 nm excitation and 460 nm emission. 7. Place plate into Fluroskan holder and click START. 8. From the drop down menu under sheet select curve fit. Choose the appropriate data to organize (usually Measure1), then click OK. This calculates your standard curve. 9. Save the curve fit sheet as an Excel file into your data folder. Use the naming convention GSXXXXXX.xls, where XXXXXX is the date in yymmdd.xls.
TITLE: Synthesis of Carbon Dots using Citric acid (Solvent Free reaction)
AUTHORS: qurashiubaid

[DESCRIPTION]
Carbon Dots are the fluorescent nanoparticles that have wide range of applications. Facile synthesis of Carbon Dots paves the way for making this material mainstream for use. Synthesis of Carbon Dots by using Citric acid as the precursor in a solvent free reaction is a easy method in which the synthesized Carbon Dots shows fluorescence in the range of 520nm. This mode is simple and doesn't require complex instrumentation.  

[STEPS]
SECTION: Synthesis of Carbon Dots using Citric acid (Solvent Free reaction)
1.   2 g 120 °C 

SECTION: Synthesis of Carbon Dots using Citric acid (Solvent Free reaction)
2. Once you get the yellow molten compound , drop it in the 0.1 Mass Percent   100ml solution, dropwise and stir it on magnetic stirrer.

SECTION: Synthesis of Carbon Dots using Citric acid (Solvent Free reaction)
3. Then centrifuge the solution at 15000rpm for25 min  and collect the supernatant and characterize it for fluorescence by using UV-Vis spectrophotometer and subsequently by using PL instrument.

SECTION: Synthesis of Carbon Dots using Citric acid (Solvent Free reaction)
3.1.
TITLE: No Title
AUTHORS: 

[DESCRIPTION]
<p>This study aimed to investigate the effects of lactic acid bacterial fermentation extract (LABEF) on cystitis induced by <em>Escherichia coli</em> lipopolysaccharide (LPS) in the mouse bladder by pathological analyses and measurement of the levels of tumor necrosis factor-alpha (TNF-α) and interleukin-18 (IL-18). LABEF was administered orally (5 μg/L) to mice for 10 days following which, the study group (n = 12) was injected intravesically with 5 μg/L LPS. The bladder tissue was then harvested after 24 hours and subjected to hematoxylin and eosin (H-E) staining. A semiquantative score was used to evaluate inflammation (bladder inflammation index; BII). TNF-α immunohistochemical staining and multiplex cytokine assay were also performed. TNF-α and IL-18 levels were determined. The results were compared with those of the control group (n = 12). The BII in the control and study groups was 2.7 ± 0.5 and 1.1 ± 0.7, respectively, with the control group scores significantly differing from the study group scores (p value &lt; 0.001). TNF-α immunohistochemical staining showed similar results. The TNF-α levels determined by the multiplex cytokine assay were 2.82 ± 1.35 pg/mg and 1.55 ± 0.56 pg/mg for the control and study groups, respectively, and the difference in values between these groups was statistically significant (p value = 0.007). Thus, oral administration of LABEF appears to have a preventive effect against the inflammatory responses and TNF-α expression induced by intravesical instillation of LPS in the mouse bladder. Further studies are required to determine the clinical application of this finding.</p>

[STEPS]
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?.
TITLE: Crystallisation of Enterovirus D68 3C protease
AUTHORS: ryan Lithgo, Peter Marples, Lizbé Koekemoer, Daren Fearon

[DESCRIPTION]
The development of effective broad-spectrum antivirals forms an important part of preparing for future pandemics. A cause for concern is the currently emerging pathogen Enterovirus D68 (EV-D68) which primarily spreads through respiratory routes causing mostly mild to severe respiratory illness but, in severe cases, acute flaccid myelitis. The 3C protease of EV-D68 is a potential target for the development of antiviral drugs due to its essential role in the viral life cycle and high sequence conservation. This protocol was used to grow D68 3C ProB crystals that were applied high-throughput crystallographic follow up compound screening on D68 3C.

[STEPS]
SECTION: Crystallisation experiment
4. Protein and buffer requirements:
14.4 µL35 mg/mL 
2.88 mL 
7.2 µL seeds, dilution 1:1 000 000

SECTION: Crystallisation experiment
6. Dispense 30 µL into SwissCI 3 lens plate reservoir wells using a 100 µl multi-channel pipette.
Dispense 50 nL35 mg/mL  to each lens using the SPT mosquito.
Dispense  100 nL to each lens using the SPT mosquito.
Dispense  25 nL to each lens using the SPT mosquito.

Drop ratio: 2:4:1 
Final drop volume: 175 nl
SECTION: Crystallisation experiment
5. ccCrystallisation screen composition:
0.1 Molarity (M)  Tris pH 7.8 
0.2 Molarity (M)  Ammonium acetate
26% w/v PEG 3350

Stock solutions used:
1 Molarity (M)  Tris adjusted to pH 7.8  with NaOH
1 Molarity (M) Ammonium acetate
50% w/v PEG 3350

 

SECTION: Crystallisation experiment
8. 
 


SECTION: Crystallisation experiment
7. Incubate at 20 °C for 1440 min in Formulatrix Rock Imager.

Imaging Schedule: The first images are taken after 12 h and the imaging schedule follows a Fibonacci sequence of days for further collections. 
SECTION: Equipment needed
2. Formulatrix Rock Imager (or incubator of choice)
SPT mosquito 
 
P100 8 multi-channel pipette
SwissCI 3 lens plate

SECTION: Crystallisation experiment
3. Prepare seed stock:
 
1: 1 000 000 dilution    seeds
SECTION: Data collection at Synchrotron
9. Diamond Light Source
Unattended Data Collection (UDC)
Data Collection Temperature: 100K
Detector: DECTRIS EIGER2 X 9M
Beamline: I04-1
Wavelength:  0.9212 Å
Resolution (Å): 1.62
Beam Size (μm): 60 X 50
Number of images: 3600
Oscillation: 0.10°
Exposure (s): 0.0020
Transmission (%): 100
Flux (ph/s): 9.50e+11
SECTION: Enterovirus D68 3C protease expression and purification
1. The protein used for crystallisation was expressed and purified using the following protocol.
TITLE: No Title
AUTHORS: 

[DESCRIPTION]
<div>
<div>
<div>
<p>This protocol is from 'Flower Ca<sup>2+</sup> channel in CME and ADBE' of Yao CK et al.</p>
<div>
<div>
<p> </p>
<p>Please see the manuscript for the full method details.</p>
</div>
</div>
</div>
</div>
</div>

[BEFORE_START]
<p>You'll need: </p>
<p> </p>
<p><strong>0 mM Ca<sup>2+</sup> hemolymph-like (HL)-3 solution:</strong></p>
<ul>
<li>70 mM NaCl</li>
<li>5 mM KCl</li>
<li>10 mM MgCl<sub>2</sub></li>
<li>10 mM NaHCO<sub>3</sub></li>
<li>5 mM trehalose</li>
<li>5 mM HEPES (pH 7.2) </li>
<li>115 mM sucrose</li>
</ul>
<p> </p>
<p><strong>90 mM K<sup>+</sup>/0.5 mM Ca<sup>2+</sup> stimulation:</strong></p>
<p>(or alternative 60mM K<sup>+</sup>/1mM Ca<sup>2+</sup>)</p>
<ul>
<li>25 mM NaCl</li>
<li>90 mM KCl</li>
<li>10 mM MgCl<sub>2</sub></li>
<li>10 mM NaHCO<sub>3</sub></li>
<li>5 mM trehalose</li>
<li>5 mM HEPES (pH 7.2)</li>
<li>30 mM sucrose</li>
<li>0.5 mM CaCl<sub>2</sub></li>
</ul>
<p> </p>
<p> </p>
<p> </p>
<p> </p>

[STEPS]
?. 
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TITLE: Immunostaining of iPSC-derived neurons for quantification of synaptic proteins
AUTHORS: Dan Dou, Erika Holzbaur

[DESCRIPTION]
Here, we fix, permeabilize, and stain human iPSC-derived neurons for the purpose of observing and quantifying somal proteins of interest. For preceding culture of neurons, see "Protocol: Culture and transfection of iPSC-derived neurons for live-imaging of axonal cargoes."

[STEPS]
1. At DIV14, fix human iNeurons in 4% paraformaldehyde supplemented with 4% sucrose for 15 minutes at 37 degrees C

2. Wash four times with PBS
3. Permeabilize for 15 minutes in 0.2% Triton-X in PBS
4. Block for 1 hour with 5% goat serum and 1% BSA in PBS
5. Incubate in primary antibody diluted in blocking solution at room termperature for 1 hour
6. Wash three times with PBS
7. Incubate in secondary antibody diluted in blocking solution for 1 hour at room temperature

8. Wash three times with PBS
9. Remove PBS and add 40 µL Prolong Gold (Thermo Fisher). Using forceps, apply coverglass.
TITLE: Processing a Viral Metagenome Using iVirus
AUTHORS: Benjamin Bolduc

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block"><span>A collection of protocols designed to guide the user in processing a viral metagenome from raw sequence data to assembly, and subsequent analysis. The user uses </span><span style = "font-style:italic;">actual</span><span> reads from </span><a href="https://github.com/MicroB3-IS/osd-analysis" style = "text-decoration:underline;color:blue;cursor:pointer;"><span style = ":;">Ocean Sampling Day (2014)</span></a><span> and processes them entirely within Cyverse, a NSF-supported cyberinfrastructure.</span></div></div>

[STEPS]
TITLE: Immunohistochemical labelling of lower urinary tract afferents in spinal cord
AUTHORS: Janet R Keast, Peregrine B Osborne, John-Paul  Fuller-Jackson

[DESCRIPTION]
This protocol is used for immunohistochemical visualisation of cholera toxin subunit B within afferents innervating the lower urinary tract in cryosections of rat lumbosacral spinal cord. Free-floating sections are processed in a double labelling protocol to distinguish regions of innervation by these afferents.
Cholera toxin B antibody [lower urinary tract afferents]
Choline acetyltransferase antibody [preganglionic autonomic neurons and motoneurons]

[STEPS]
SECTION: Preparation of cryosections
1. Cryoprotect fixed tissue (L5-S2 spinal cord) in phosphate-buffered saline (PBS; 0.1 M, pH7.2) containing 30% sucrose. This should be performed at 4C, 24-72h prior to cutting.
SECTION: Preparation of cryosections
2. Embed tissue in cryomold using OCT, freeze in cryostat and cut sections (40 µm), collecting sections progressively across sets of 4 wells to collect 160 µm spaced series.
SECTION: Immunostaining
3. Wash sections in PBS (3 x 10 min)
SECTION: Immunostaining
4. Incubate sections in blocking solution at room temperature for 2 h
SECTION: Immunostaining
5. Incubate sections in appropriate dilutions of primary antibodies (or combinations of primary antibodies) for 48-72h. Antibodies are diluted in PBS containing 0.1% sodium azide, 2% horse serum, and 0.5% triton-X.
SECTION: Immunostaining
6. Wash sections in PBS (3 x 10 min)
SECTION: Immunostaining
7. Incubate sections in appropriate dilutions of secondary antibodies (or combinations of secondary antibodies) 4 h in the dark. Antibodies are diluted in PBS containing 2% horse serum, and 0.5% triton-X.

 

SECTION: Immunostaining
8. Wash sections in PBS (3 x 10 min)
SECTION: Immunostaining
9. Mount sections onto glass slides and coverslip in preferred anti-fade mountant.
SECTION: Microscope
10. Labeled lower urinary tract afferents with cholera toxin subunit B should be most visible along the boundaries of each dorsal horn. Look for the lateral projections, which are the most prominent, as well as the medial projections, which are comparatively fainter. 

Urethra injections of cholera toxin subunit B will occasionally result in the uptake of tracer by preganglionic neurons if the tracer injection site is near intramural or serosal pelvic ganglion neurons. These neurons will be visible within the sacral preganglionic nucleus in the intermediolateral column. If the urethral rhabdosphincter is exposed to tracer, this will be evident by labelling of motor neurons in the ventral horn.
TITLE: Inoue transformation buffer
AUTHORS: Andreas Sagen

[DESCRIPTION]
The Inoue method of transformation is a chemical transformation method of prokaryotes (bacteria), which add significant improvements to methods such as the classic Calcium chloride transformation method.

[STEPS]
SECTION: 10x Inoue transformation buffer
1. Add 80 mL distilled water to a 100 mL tube
SECTION: 10x Inoue transformation buffer
2. Measure and add 10.89 g Manganese chloride, 2.2 g Calcium chloride, 3.0 g PIPES and 18.65 g Potassium chloride

Materials:
 
  
 
SECTION: 10x Inoue transformation buffer
3. Add distilled water to 100 mL
SECTION: 10x Inoue transformation buffer
4. Filter sterilize with a 0.2 µm pore-size filter and store frozen at -20 °C
TITLE: Detection of Cryptosporidium in stool sample by PCR-RFLP
AUTHORS: botchiesenyo  

[DESCRIPTION]
Nested PCR-RFLP adapted from Nichols, R.A.B., Campbell, B.M. and Smith, H.V., 2003. Identification of Cryptosporidium spp. oocysts in United Kingdom noncarbonated natural mineral waters and drinking waters by using a modified nested PCR-restriction fragment length polymorphism assay. Applied and environmental microbiology, 69(7), p.4183.

[STEPS]
SECTION: Nested PCR
1. Extract whole genomic DNA from stool samples. 

Positive control DNA for Cryptosporidium parvum may be obtained from ATCC. Alternatively you can extract genomic DNA from wild type Cryptosporidium parvum purchased from Bunchgrass Farms (Deary, Idaho, USA), Waterborne Inc (New Orleans, Louisiana, USA), or Sterling Labs (Tucson, Arizona, USA).
SECTION: Nested PCR
2. First round of PCR to amplify 18SrRNA
SECTION: Nested PCR
2.1. Combine the following in a PCR tube:
5 μl of DNA (from positive control, experimental sample, or water for negative control)
0.1 μM Forward Primer ("out NDIAGF2": CAATTGGAGGGCAAGTCTGGTGCCAGC)
0.1 μM Reverse Primer ("out NDIAGR2": CCTTCCTATGTCTGGACCTGGTGAGT)
1x GoTaq Master Mix (Promega)
Ultrapure water to bring total volume to 25 microliters
SECTION: Nested PCR
2.2. Thermocycler program:
95 ºC -5 minutes,
30 cycles:
    94 ºC -30 seconds
    58 ºC - 1 minute
    72 ºC - 30 seconds

SECTION: Nested PCR
3. Second round of PCR to amplify 18SrRNA
SECTION: Nested PCR
3.1. Combine the following in a PCR tube:
1 μl of PCR product from Step 2
0.1 μM Forward Primer ("DIAGF": AAGCTCGTAGTTGGATTTCTG)
0.1 μM Reverse Primer ("DIAGR": TAAGGTGCTGAAGGAGTAAGG)
1x GoTaq Master Mix (Promega)
Ultrapure water to bring total volume to 25 microliters
SECTION: Nested PCR
3.2. Thermocycler program:
95 ºC -5 minutes,
45 cycles:
    94 ºC -30 seconds
    58 ºC - 1 minute
    50 ºC - 1 minute
SECTION: Nested PCR
4. Run 7 μl of PCR product from Step 3 on a 2% agarose gel and visualise by staining with ethidium bromide.
SECTION: RFLP
5. Combine the following and incubate at 37 ºC for 4 hours:

5 μl PCR product from step 4 above
20u Restriction enzyme (Ssp1, Vsp1, Ase1)
1x final concentration Restriction enzyme digestion buffer (corresponds to enzyme used)
1x final concentration BSA
SECTION: RFLP
6. Run digested PCR product from Step 5 on a 2% agarose gel and visualize by staining with ethidium bromide.
TITLE: Protocol to apply saliva samples to quantum mechanical tunneling current real-time point-of-care COVID-19 sensor.
AUTHORS: Massood Tabib-Azar

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">This protocol is used to operate an electronic rapid (1 min) point-of-care SARS-CoV-2 sensor</div></div>

[STEPS]
?. Apply a small amount (~1 uL) of saliva on the sensor element at room temperature.
?. 2. Wait for 30 s. The sensor sytem wil turn on a green LED to alert you at the end of the 30 s.
?. Measure the sensor I-V using the paired smart phone APP or click on the "Read" botton on the sensor system.
?. Apply 60 C water on the sensor for 30 s.
?. If the result is "positive", redo the test to increase confidence.
?. Re-apply 60 C water on the sensor for 30 s.
?. The sensor is ready to be used for another test.