eamag/protocols-with-steps huggingface dataset:
TITLE: Attentional function in fibromyalgia and rheumatoid arthritis
AUTHORS: Carmen M Galvez-Sanchez, Pablo de la Coba, José M. Colmenero, Gustavo A. Reyes del Paso, Stefan Duschek

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block"><div class = "justify" style = "text-align:justify">Concentration difficulties, forgetfulness and mental slownessare common in fibromyalgia syndrome (FMS); initial findings suggest that rheumatoid arthritis (RA) may also be accompanied by cognitive impairments. This study aimed to compare attentional performance between patients with FMS and RA. Attention was quantified in the domains of alerting, orienting and executive control using the Attentional Network Test – Interaction (ANT-I) in 56 women with FMS, 41 women with RA and 50 healthy women. Pain severity was statistically controlled in the group comparison. While FMS patients exhibited longer reaction times and made more errors on the ANT-I than RA patients and healthy women, performance did not differ between RA patients and healthy women. The magnitude of group differences did not vary by the experimental conditions of the ANT-I, suggesting a general attentional deficit in FMS rather than specific impairments in the domains of alerting, orienting and executive control. Differences between patient groups may relate to the different pathogenetic mechanisms involved in the disorders, i.e. inflammatory processes in RA and central nervous sensitization in FMS. In FMS, heightened activity in the pain neuromatrix may interfere with attention, because it requires enhanced neural resources in brain areas that are involved in both pain and attentional processing.</div><style>
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[STEPS]
TITLE: Bland-Altman plots Squat, Single Leg Squat, Countermovement Jump
AUTHORS: Wolfgang Teufl, Markus Miezal, Bertram Taetz, Michael Fröhlich, Gabriele Bleser

[DESCRIPTION]
<p>Find enclosed the Bland-Altman plots of hip-, knee-, ankle joint and the global pelvis felxion, obliquity and rotation belonging to the publication “Validity of inertial sensor based 3D joint kinematics of static and dynamic functional movement tasks”.</p>

[STEPS]
TITLE: Illumina TruSeq Library quantification with qPCR probe method
AUTHORS: Kentaro Itokawa

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">A homemade solution for quantification of Illumina library.</div><div class = "text-block">Because the method uses a quenched-probe (not intercalator), it is expected to be relatively stable for the difference of size distribution of libraries.</div><div class = "text-block">Currently, we confirmed this protocol with a probe for TruSeq type adapter.</div></div>

[STEPS]
?. [Preparing calibrators and primer/probe]
Prepare low-TE buffer (10 mM Tris-HCl, 0.1 mM EDTA, pH 8.0) containing 5 ng/μl salmon sperm DNA.  AB11 M Tris-HCl, pH8.0100 μl20.5 M EDTA10 μl3UltraPure™DNA Solution 10 mg/mL5  μl4milli-Q water9889  μl5Total10 mLStore in -20 °C.
AB11 M Tris-HCl, pH8.0100 μl20.5 M EDTA10 μl3UltraPure™DNA Solution 10 mg/mL5  μl4milli-Q water9889  μl5Total10 mL
?. [Preparing calibrators and primer/probe]
Prepare 20x primers & probe mix solution as below.  AB1Probe5 μM2P5 primer5 μM3P7 primer5 μMStore in -20 °C.Double-quenched probe (IDT): /56-FAM/ACACTCTTT/ZEN/CCCTACACGACGCTCTTC/3IABkFQ/P5 primer: 5'-AATGATACGGCGACCACCGA-3'P7 primer: 5'-CAAGCAGAAGACGGCATACGA-3’
AB1Probe5 μM2P5 primer5 μM3P7 primer5 μM
?. [Preparing calibrators and primer/probe]
Prepare the following qPCR master mix per reactions for the number of your samples (+ calibrators).   AB1Prime Time PCR master mix10 μl220x primers & probe mix1 μl3H2O8 μlDistribute above to each well.Add 1 μl of template (diluted library or calibrator) to each well.
AB1Prime Time PCR master mix10 μl220x primers & probe mix1 μl3H2O8 μl
?. [Result]
Calculate the original concentration of your library.
?. Conduct PCR with the following condition.95 °C for 2 min30 cycles of    97 °C for 5s    62 °C for 10s    68 °C for 15s (photo with a filter appropriate for SYBR-green or FAM)
?. [Preparing calibrators and primer/probe]
Prepare dilution series of PhiX control with low-TE buffer containing 5 ng/μl salmon sperm DNA in 8-strip PCR tubes.These are used as calibrators.  AB150 pM100 μl25 pM100 μl30.5 pM100 μl 40.05 pM100 μl Store in -20 °C.
AB150 pM100 μl25 pM100 μl30.5 pM100 μl 40.05 pM100 μl
TITLE: No Title
AUTHORS: 

[GUIDELINES]
<p><strong>Application Notes:<br /></strong>Immunoprecipitation is a procedure by which proteins or peptides that react specifically with an antibody are removed from solution and examined for quantity or physical characteristics. Immunoprecipitation can also be used to “enrich”a protein population prior to Western Blotting. For example, one can perform immunoprecipitation with a pan-specific antibody against a protein of interest followed by Western blotting with a modification-specific antibody (such as a<br />phospho-specific antibody or an acetylation-specific antibody).</p>
<p> </p>
<p><strong>Tips:</strong></p>
<p>1. The choice of lysis buffer depends on the location of the protein (membrane, cytosolic, nuclear).</p>
<p>2. Immunoprecipitates allowed to incubate overnight may have a higher background than ones processed for shorter periods of time due to time-dependent aggregation or denaturation of cellular proteins.</p>
<p>3. Always use an isotype-matched irrelevant control antibody (monoclonal) or same-species serum from a non-immunized animal to remove non-specific antibody binding in cellular lysates.</p>
<p> </p>
<p><strong>Solutions and Reagents:</strong></p>
<p><strong>1X Cell Lysis Buffer:</strong></p>
<table>
<tbody>
<tr>
<td>25 mM Tris-HCl, pH 7.5</td>
<td>1 µg/ml aprotinin</td>
</tr>
<tr>
<td>150 mM NaCl</td>
<td>1 mM Na<sub>3</sub>PO<sub>4</sub></td>
</tr>
<tr>
<td>0.1% Triton X-100</td>
<td>1 mM PMSF</td>
</tr>
<tr>
<td>2 mM EDTA</td>
<td>5 mM NaF</td>
</tr>
<tr>
<td>1 µg/ml leupeptin</td>
<td> 3 mM Na<sub>4</sub>P<sub>2</sub>O<sub>4</sub></td>
</tr>
</tbody>
</table>
<p> </p>
<p> </p>
<p><strong>5X SDS sample Buffer:</strong></p>
<p>312.5 mM Tris-HCl (pH 6.8) 10% SDS (w/v)</p>
<p>250 mM DTT</p>
<p>50% Glycerol</p>
<p>0.05% Bromophenol Blue (w/v)</p>
<p>Use at 1X</p>
<p> </p>
<p><strong>10X SDS Running Buffer:</strong></p>
<p>Dissolve 144 g of Glycine, 30 g of Tris base and 10 g SDS in 800 ml of distilled H2O.</p>
<p>Add distilled H2O to 1 liter</p>
<p>Use at 1X</p>
<p> </p>
<p><strong>Transfer Buffer:</strong></p>
<p>2.25 g Tris base</p>
<p>10.5 g Glycine 1 g SDS</p>
<p>200 ml Methanol</p>
<p>Add distilled water to 1.0 L</p>

[STEPS]
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TITLE: No Title
AUTHORS: 

[DESCRIPTION]
This protocol provides a method for predicting the proportions of phage replication cycles within the skin virome. We will be looking at three markers for temperate phages: 1) presence of integrase genes, 2) presence of ACLAME database prophage elements, and 3) similarity to bacterial genomes. Based on the methods found in the following publication: <br /><br />Hannigan, Geoffrey D., et al. "The Human Skin Double-Stranded DNA Virome: Topographical and Temporal Diversity, Genetic Enrichment, and Dynamic Associations with the Host Microbiome." <em>mBio</em> 6.5 (2015): e01578-15.<br /><br />

[BEFORE_START]
Perl scripts and other supplementary information available at:<br /><br /><a href="https://figshare.com/articles/The_Human_Skin_dsDNA_Virome_Topographical_and_Temporal_Diversity_Genetic_Enrichment_and_Dynamic_Associations_with_the_Host_Microbiome/1281248" target="_blank">https://figshare.com/articles/The_Human_Skin_dsDNA_Virome_Topographical_and_Temporal_Diversity_Genetic_Enrichment_and_Dynamic_Associations_with_the_Host_Microbiome/1281248</a>

[GUIDELINES]
<strong>Required Software:</strong><br />
<ul>
<li>UniProt</li>
<li>ACLAME</li>
<li>NCBI Bacterial Genomes</li>
<li>NCBI's BLAST+ v2.2.0</li>
</ul>
<br /><strong>Relevent Files</strong><br />Output:<br />
<ul>
<li>Phage_replication_cycle/end_contig_counts_final.tsv</li>
<li>Phage_replication_cycle/final_contig_quant_annotation_ncbi.tsv</li>
<li>Phage_replication_cycle/phage_lifecycle_otu_table_for_rel_abund.tsv</li>
</ul>
Perl script: remove_block_fasta_format.pl<br />R script: <a href="https://www.protocols.io/view/Script-R11-Replication-Cycle-ejfbcjn" target="_blank">R11</a>

[STEPS]
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TITLE: Exp_02
AUTHORS: José Eduardo De la Cruz Luna

[DESCRIPTION]
Creacionde l segundo experimento

[STEPS]
SECTION: Protocolo del Segundo Experimento: Influencia del Color en la Transferencia de Calor de Agua a 100ºC a Temperatura Ambiente (25ºC)
1. Objetivo:
Determinar si el color de las botellas afecta la velocidad de transferencia de calor del agua a 100ºC a la temperatura ambiente del laboratorio (25ºC).
Materiales:
Tres botellas de plástico transparente de diferentes colores (rojo, verde y azul).
Agua a 100ºC.
Tres sensores de temperatura DS18B20.
Placa Arduino con capacidad para conectar los tres sensores DS18B20.
Cableado necesario para conectar los sensores a la placa Arduino.
Ordenador con software de lectura y registro de datos Arduino IDE.
Procedimiento:
Preparación de las Botellas:
a. Llenar cada botella con la misma cantidad de agua a 100ºC.
b. Etiquetar cada botella con su respectivo color.
Instalación de Sensores:
a. Conectar los tres sensores DS18B20 a la placa Arduino según las instrucciones del fabricante.
b. Posicionar un sensor en el centro de cada botella, asegurándose de que esté sumergido completamente en el agua.
Conexión a la Placa Arduino:
a. Conectar la placa Arduino a la computadora mediante el cable USB.
b. Abrir el software Arduino IDE en la computadora.
Programación del Arduino:
a. Escribir un código en el Arduino IDE para leer y registrar las temperaturas de los tres sensores a intervalos regulares.
b. Configurar el código para que registre los datos durante un período de tiempo suficiente para observar la diferencia en la transferencia de calor.
Inicio del Experimento:
a. Colocar las botellas en un lugar donde estén expuestas a la temperatura ambiente del laboratorio.
b. Iniciar el registro de datos a través del Arduino IDE.
Registro de Datos:
a. Registrar las lecturas de temperatura de cada sensor en intervalos regulares.
b. Asegurarse de anotar el tiempo transcurrido desde el inicio del experimento.
Análisis de Datos:
a. Analizar los datos recopilados para cada botella y determinar la velocidad de transferencia de calor.
b. Comparar las velocidades de transferencia entre las botellas de diferentes colores.
Conclusiones:
a. Concluir si existe alguna relación entre el color de las botellas y la velocidad de transferencia de calor.
b. Interpretar los resultados y discutir posibles implicaciones.
TITLE: Making electro-competent cells 
AUTHORS: Ashwinuday 

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">This protocol can be used for obtaining of electro-competent bacterial cells.</div></div>

[STEPS]
?. Streak the cells on LB agar plates and incubate at  for
37 °C
?. Pick single colony and inoculate it in  2X LB broth and incubate at for -  on shaker incubator
20 mL
37 °C
?. Take 2ml of primary inoculum and inoculate it in  2X LB broth and incubate it at   on shaker.
200 mL
37 °C
?. Grow till the OD reaches 0.6
?. Place the culture at  for
4 °C
?. Aliquot infalcon and spin at
50 mL
Centrifuge: 4000 33, 25 min, 4 10
?. Discard the supernatant and resuspend well in  10% glycerol
40 mL
?. Spin at
Centrifuge: 4000 33, 25 min, 4 10
?. Discard the supernatant and resuspend in  10% glycerol
25 mL
?. Spin at
Centrifuge: 4000 33, 25 min, 4 10
?. Discard the supernatant and resuspend in 10% glycerol. Mix the contents of 2 falcons together such that only 2 falcons of  contents is present
20 mL
40 mL
?. Spin at
Centrifuge: 4000 33, 25 min, 4 10
?. Discard the supernatant and resuspend in 10% glycerol.
1 mL
?. Make aliquots of  in autoclaved  eppendorfs,flash freeze and store at
50 µl
600 µl
-80 °C
TITLE: ELISA for anti-HIV peptide antibodies in the egg yolks of brown Leghorn layer hens.
AUTHORS: Angel  Justiz-Vaillant

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">These are three ELISAs for detection of anti-HIV antibodies. These test were highly specific, sensitive and reproducible. They detect specific immunoglobulin Y against HIV peptides in the egg yolk of  brown Leghorn layer hens. A modification of these methods were used to detect anti-HIV antibodies in Humans. </div></div>

[STEPS]
?. Coating buffer is prepared as follows: 3.7 g Sodium Bicarbonate (NaHCO3) and 0.64 g Sodium Carbonate (Na2CO3) in 1L of distilled water.
?. Phosphate buffered-saline Tween-20 (10% PBS-Tween 20, pH 7.2) is prepared as follows: Dissolve the following: 0.2g of KCl, 8g of NaCl, 1.45g of Na2HPO4, 0.25g of KH2PO4, and 2ml of tween-20 in 800 ml of distilled water. After that, adjust pH to 7.2, add additional distilled water to adjust the volume to 1L, and then may sterilize by autoclaving.
?. Blocking solution is prepared as follows: add 0.1 g KCl, 0.1 g K3PO4, 1.16 g Na2HPO4, and 4.0 g NaCl to 500 ml distilled water, pH 7.4. Then, to complete the preparation of this solution, 15g of non-fat dry milk should be added.
?. Sample/Conjugate Diluent is prepared as follows: Add 15 g of non-fat dry milk and 2.5 ml of 10% Tween 20 to 500 ml of PBS.
?. The 96-well polystyrene microplates (U- shaped bottom, Sigma-Aldrich) is coated with 100 ng of 579-601 of the HIV gp41, fragments 308-331 or 421-438 from HIV gp120 in coating buffer for 4.1 h at 37°C.
?. Then, each microplate is washed four times with 10% PBS-Tween 20 and the blocking solution (3% non-fat milk in PBS) added in the amount of 51 µl into each well.
?. The microplate is incubated at  1.30 h at RT. After that, the microplate is washed as previously.
?. Fifty µl of water soluble fraction (WSF) diluted 1:50 with the sample diluent is added to the  wells.
?. Then, each microplate is incubated for 1h at RT and  washed four times as previously.
?. Then,  50 µl of horseradish peroxidase labeled anti-IgY conjugate (Sigma-Aldrich) diluted 1:30,000 is  poured into each well.
?. Each microtiter plate is  incubated again for 1h at RT and then, washed four times.
?. A volume  of 50 µl of tetramethylbenzidine (TMB, Sigma-Aldrich) is added; and after a further incubation of 16 min in the dark, the reaction is stopped with a solution of 3M HCl.
?. After that, each microplate is read in a microplate reader at 450 nm.
?. The cut-off value is assessed from the mean optical density (OD) of the negative control times 2.
?. The cut-off points of ELISAs for the detection of anti-HIV peptide (579-601), anti-HIV peptide (308-331) and anti-HIV peptide (421-438) were 0.42, 0.40 and 0.44 respectively.
TITLE: ADP Glo Protocol
AUTHORS: Annan SI Cook, Xuefeng Ren

[DESCRIPTION]
Protocol for ADP Glo (Promega) assay to measure the catalytic activity of the lipid kinase VPS34 on small unilammelar vesicles.

[STEPS]
SECTION: Preparation of Small Unilamellar Vesicles (SUVs)
1. Dehydrate 0.4 mg of the lipid mixture (40% DOPC, 20% DOPE, 20% DOPS, 20% liver phosphatidylinositol, Avanti Polar Lipids) in a glass tube using a gentle N2 stream.
SECTION: Preparation of Small Unilamellar Vesicles (SUVs)
2. Allow the lipids to dry   in a vacuum desiccator to remove excess chloroform.
SECTION: Preparation of Small Unilamellar Vesicles (SUVs)
3. Rehydrate the dried lipids by adding 25 millimolar (mM) HEPES pH 7.5 and 200 millimolar (mM) NaCl.
SECTION: Preparation of Small Unilamellar Vesicles (SUVs)
4. Vortex the mixture to resolubilize the lipids.
SECTION: Preparation of Small Unilamellar Vesicles (SUVs)
5. Perform 10 cycles of freeze-thaw by immersing the lipids in liquid nitrogen for a few seconds and then in a 37 °C water bath.
SECTION: Preparation of Small Unilamellar Vesicles (SUVs)
6. Sonicate the lipids using a small probe tip sonicator at 50% power in 2-second on/off cycles for a total of 15 min on ice and a water mixture.
SECTION: Preparation of Buffers
7. Prepare a kinase dilution buffer.

Kinase dilution buffer
      HEPES pH 7.5  25 mM    NaCl  200 mM    MgCl2  10 mM    MnCl2  1 mM    TCEP  2 mM  

SECTION: Preparation of Buffers
8. Prepare a 2x lipid dilution buffer. 
 
2x lipid dilution buffer
      HEPES pH 7.5  25 mM    NaCl  200 mM    MgCl2  20 mM    MnCl2  2 mM    TCEP  4 mM  

SECTION: ADP-Glo assay
9. In a reaction tube, combine the following components:
 
      50 nM PI3KC3-C1  9 μL    0.1 mg/mL SUVs in the 2x lipid dilution
  buffer  9 μL    500 μM ATP in the same buffer  2 μL  

SECTION: ADP-Glo assay
10. Mix the components gently.
SECTION: ADP-Glo assay
11. Allow the reaction to proceed for 60 min at Room temperature.
SECTION: ADP-Glo assay
12. After the incubation, add 20 µL of the ADP-Glo ATP depletion reagent to each reaction tube.
SECTION: ADP-Glo assay
13. Incubate the reaction tubes with the ADP-Glo ATP depletion reagent for 40 min at Room temperature.
SECTION: ADP-Glo assay
14. Measure the luminescent output for each condition tested using a luminometer or a plate reader.
TITLE: No Title
AUTHORS: 

[DESCRIPTION]
<p>1<sup>st</sup> purification: a-FLAG (A2220; Sigma-Aldrich)</p>
<p>2<sup>nd</sup> purification: GFP TRAP_A (ChromoTek)</p>

[STEPS]
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TITLE: No Title
AUTHORS: 

[DESCRIPTION]
<p>BLAST (Basic Local Alignment Search Tool) is an algorithm for comparing primary biological sequence information, such as the amino-acid sequences of different proteins or the nucleotides of DNA sequences (Wikipedia).</p>
<p> </p>
<p style="text-align: center;"><img id="s-mce-img" class="s-mce-img" src="https://s3.amazonaws.com/pr-journal/d9fc2w6.png" data-src="https://s3.amazonaws.com/pr-journal/d9fc2w6.png" data-ofn="Screen Shot 2016-07-12 at 11.44.23 AM.png" /></p>
<p style="text-align: center;">http://www.hypothesisjournal.com/wp-content/uploads/2011/08/boutros-3-1-fig2.png</p>
<p style="text-align: center;"> </p>
<p style="text-align: left;">Compare tara_med_examplegenome protein sequences to a custom collection of carbon fixation related genes (downloaded from KEGG)</p>
<p style="text-align: left;"> </p>
<p style="text-align: left;">Collection contains marker genes for:</p>
<p style="text-align: left;">CBB, Wood-Ljundahl, reductive TCA, 3-hydroxypropionate, 3-hydroxypropionate/4-hydroxybutyrate</p>
<p style="text-align: left;"> </p>
<p style="text-align: left;">As a cyanobacteria - which carbon fixation pathway?</p>
<p> </p>

[STEPS]
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TITLE:           ELISA for measurement of monocyte chemoattractant protein-1 (MCP-1/CCL2) in human serum.
AUTHORS: Angel  Justiz-Vaillant, Belkis Ferrer-Cosme

[DESCRIPTION]
<div class = "text-blocks"><div class = "text-block">MCP-1 is believed to play an important role in monocyte infiltration into tumor tissues. [1] MCP-1 plays an important role in the pathogenesis of atherosclerosis. There is considerable evidence that supports that monocytes containing MCPs and macrophages influence the growth of other cell types within the atherosclerotic lesion. [2]</div><div class = "text-block">References</div><div class = "text-block"><span>1. Deshmane SL, Kremlev S, Amini S, Sawaya BE. Monocyte chemoattractant protein-1 (MCP-1): an overview. </span><span style = "font-style:italic;">J Interferon Cytokine Res</span><span>. 2009;29(6):313-326. doi:10.1089/jir.2008.0027</span></div><div class = "text-block">2. Lin J, Kakkar V, Lu X. Impact of MCP-1 in atherosclerosis. Curr Pharm Des. 2014;20(28):4580-4588. doi:10.2174/1381612820666140522115801</div></div>

[STEPS]
?. An anti-human MCP-1/CCL2 coating antibody is adsorbed onto the microwells by incubation overnight at 4°C with carbonate-bicarbonate buffer.
?. Add 50 µl of human serum or plasma. Human MCP-1/CCL2 present in the serum or plasma binds to antibodies adsorbed into the microwells.
?. The microplate is blocked with 3% non-fat milk-PBS buffer and later wash to remove unbound proteins.
?. Fifty (50) µl of biotin-conjugated anti-MCP-1/CCL2 antibody is added. The optimal dilution must be investigated.
?. The microplate is rewashed with PBS-Tween 20 buffer, pH 7.4.
?. One hundred µl of streptavidin-HRP conjugate is added and it binds to the biotin-conjugated anti-MCP-1/CCL2 antibody. The optimal dilution of this conjugate must be investigated.
?. The plate is washed following incubation to remove the unbound Streptavidin-HRP.
?. Add 100 µl of 3',3',5',5'- tetramethylbenzidine (TMB; Sigma-Aldrich) into each well.
?. Incubate the microwells in the dark for 20 min.
?. A colored product is formed in proportion to the quantity of MCP-1/CCL2 present in the sample or standard.
?. The reaction is terminated by addition of 100 µl 3M H2SO4  and the absorbance is measured at 450 nm.
?. A standard curve is made from 7 human MCP-1/CCL2 standard dilutions and the human MCP-1/CCL2 sample concentration is determined.
?. For better results place the microplate on a microplate shaker in every incubation.
TITLE: MDA for virome analysis
AUTHORS: Frej   Larsen

[DESCRIPTION]
This protocol is not intended for amplification of DNA. Rather, it uses the Phi29 DNA polymerase enzyme to turn single stranded DNA (ssDNA) into double stranded DNA (dsDNA). This is required for ssDNA viruses to be sequenced.

The procedure should be performed in a fume hood with a UV-light. Prior to starting, the UV-light should be turned on to disinfect the workspace and UV-tolerant materials such as empty PCR-plates, lids, and pipette tips.

Whenever working with the samples, keep them on ice.

[STEPS]
1. Place materials that tolerate UV-treatment in fume hood and turn on the UV light and recirculation for 30 minutes before use. 
2. Pick up a bucket of ice and thaw samples on ice
4. Add 10 ng DNA in 10 µL  MQ water to the PCR tube and mix by pipetting.
If sample has a concentration below 1 ng/ul, add 10 µL  of undiluted sample to the tube and mix by pipetting
3. Add 10 µL denaturation buffer to a PCR tube

5. Briefly centrifuge the plate
6. Denature template DNA by 95 degrees for 3 minutes in a ThermoCycler. Directly after, put the samples back on ice
7. Add all 20 µL sample content to the MDA cake tube. Keep both sample and cake on ice while transfering the sample

8. Seal tube with provided lid and briefly centrifuge the sample
9. Run sample on a ThermoCycler with the following program:

 30 °C for 30 min 
 65 °C for 10 min
 4 °C
10. Purify samples with bead purification or store sample at -20 °C  or -80 °C
TITLE: LB Agar (1 Liter)
AUTHORS: Alba Balletbó

[STEPS]
?. Add LB agar components in a 1 L autoclavable. LB agar components (1 L):  AB1NaCl10 gram2Tryptone10 gram3Yeast Extract5 gram4Agar15 gram
AB1NaCl10 gram2Tryptone10 gram3Yeast Extract5 gram4Agar15 gram
?. Add 1 L of distilled water into the bottle.
?. Vigorously shake the bottle.
?. Place the bottle into the autoclave and sterilize.