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In the presence of calcium and magnesium ions, 1% Brij 97 is a relatively weak detergent that is known to largely maintain tetraspanin tetraspanin interactions.
Highly soluble, highly abundant proteins are concentrated in a relatively weak detergent while less soluble, less abundant membrane proteins are extracted in progressively stronger detergents.
Immunoprecipitation of tetraspanins CD9, CD151 and Tspan9, and the CD151-associated integrin, α6β1, from surface biotinylated platelets revealed a distinct pattern of proteins in the relatively weak detergent Brij 97, in which tetraspanin microdomains are thought to remain largely intact [ 5, 38].
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Rat aortas were decellularized using a sequential combination of weak detergents followed by a nuclease treatment that resulted in 96.5 ± 1.3% DNA removal, while ECM components and mechanical properties were well maintained.
Ammonia can be found at some grocery stores and drug stores, but take care not to purchase the weaker "detergent" variety.
Although both E-cadherin and P-cadherin are found in areas of cell-cell contact, the relative ease with which P-cadherin can be extracted from cells, using a non-ionic detergent, demonstrated weaker anchorage of this protein to the actin cytoskeleton when compared with E-cadherin.
Briefly, with the reconstructed epidermis, either commercially available or produced in our lab, we have shown that following suggestions made by Corsini and Galli [ 10, 11], very typical behaviours in term of viability and release of interleukins 1alpha and 8 differentiated a surfactant with sensitising potential from other detergents with weak, mild and strong irritation potential [ 7, 36].
This is mostly likely due to the formation of weak aggregates which dissociate upon detergent solubilization and SDS-PAGE, since the truncated Q368X protein lacks the olfactomedin presumptive protein-protein interaction domain.
Firstly, we were able to separate the weaker electron density of the detergent micelle from that of YidC.
Since quantitative measurement does not tolerate usage of detergents, which may disrupt weak and transient interactions, a membrane fractionation protocol has been devised to prepare tight junction-containing membranes in the absence of detergent (see Methods).
Biochemical purification of membrane components remains a challenge to cell biologist because the procedure necessitates the use of detergents, which undoubtedly disrupt weak and transient protein complexes.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com