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Proteins were either detected with Coomassie brilliant blue or transferred to PVDF membranes (Bio-Rad), then blocked with 1% bovine serum albumin (BSA).

Citrullinated and uncitrullinated proteins (1 μg/well) were separated on NuPAGE® Bis-Tris 10% gels (Bio-Rad Laboratories), stained with Coomassie brilliant blue, or transferred to nitrocellulose membranes.

The proteins were then either stained with Coomassie brilliant blue or transferred to a polyvinylidene difluoride membrane (no. LC2002; Invitrogen) for Western blot immunoassay.

The gels were either fixed and stained with Coomassie Brilliant Blue or transferred to Optitran membrane for western blot with anti-CENP-A antibody according to manufacturer's protocol (Millipore).

They were either visualised by Coomassie Brilliant Blue R250 staining, transferred to PVDF membranes for NH2-terminal microsequencing or transferred to nitrocellulose membranes for Western blot analysis as described elsewhere [ 25].

Proteins were either stained with Coomassie Brilliant Blue or were transferred to Protran nitrocellulose membranes (Schleicher & Schuell) using a Transblot semi-dry transfer system (BioRad).

Samples were loaded onto SDS-12% polyacrylamide gels and either stained with Coomassie brilliant blue or electrophoretically transferred to nitrocellulose according to manufacturer's instructions (Bio-Rad).The gels were blotted for 1 h at 50 V using a Criterion blotter (Bio-Rad).

Proteins were visualized with Coomassie Brilliant Blue G250 or transferred to nitrocellulose membranes.

Glands were fragmented by in situ, non-invasive wounding (squeeze wounds) without opening the cuticle right before transferring to Brilliant blue FCF-supplemented medium.

Protein samples were visualized by staining with Coomassie Brilliant Blue or, alternatively, transferred onto nitrocellulose membranes and stained with Ponceau red dye.

Gels were either stained by Coomassie Brilliant Blue or equilibrated to be transferred into transfer buffer (0.7% acetic acid).