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Roppolo, D. et al. Functional and evolutionary analysis of the CASPARIAN STRIP MEMBRANE DOMAIN PROTEIN family.
Group 15 contained 13 DEGs from one hour roots orthologous to Casparian strip membrane domain proteins (CASPs) 1, 3 and 5.
Recent papers established that a family of previously undescribed four-transmembrane-span proteins, called CASPs, forms a central, ring-like membrane domain in the endodermis, called the Casparian strip membrane domain (CSD).
Groups 15, 34, 41, 42, 46, and 53 were largely specific to one hour roots and had homology to Casparian strip membrane proteins, AP2/ERF transcription factors, peroxidases, 2-oxoglutarate (2OG) and Fe(II -dependent oxygenases, nucleotII -dependentite-leucine rich repeat resistance gene hoxygenasesd dirigenucleotideoteins, respectively.
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Dielectric elastomer (DE) strip membranes permit to design mechatronic transducers enabling large-strain, low-energy consumption, and compactness.
PIP strip membranes P-60011 – Echelon) were blocked with 0.1% ovalbumin (in TBST - 0.1M Tris, 1.5M NaCl, 0.1% Tween 20, pH 8.0) for two hours.
Levels of phosphorylated STAT5b were corrected to total STAT5b, using a stripped membrane.
Wash the stripped membrane twice with Western blotting wash buffer, 600 ml each wash, for 10 min with agitation.
The stripped membrane was pre-hybridized with hybridization buffer according to Church and Gilbert for 16 h at 42°C.
For the PIP Strips membrane, hRNase3 interacted with PI3P, PI4P, PI5P, PI (3,4) PI, PI (3,5) PI, PI (3,4,5) PA, Pandand PS, left panel).
Proteins on membranes were stripped with membrane stripping solution (2% SDS, 100 mM mercaptoethanol and 62 mM Tris-cl) after detection.
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