Protein samples for western blot analysis were extracted and separated as described previously.
For Western blot analysis, proteins were separated on SDS PAGE gels, blotted onto nitrocellulose membranes and incubated following standard procedures.
For western blot analysis, samples were separated by electrophoresis in SDS polyacrylamide gels and blotted onto poly vinylidene fluoride membranes), (MilliPore) using a semi-dry blotting apparatus (BioRad).
For western blot analysis, proteins were separated on 8-12% SDS-polyacrylamide gels and transferred to polyvinyl difluoride membranes (Millipore).
For western blot analysis, proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) on 4-12% bis-tris acrylamide gradient gels.
For western blot analysis, proteins were separated by SDS-PAGE, transferred to nitrocellulose membranes (Bio-Rad Laboratories, HerCAles, CA, USA), and overnight incubated in primary antibodies followed by 1 h of incubation in horseradish peroxidase-conjugated secondary antibodies.
Three separate experiments of western blot analysis were performed for each marker, and tissues were done separately for each western blot experiment.
For western blotting analysis, samples were separated by SDS-PAGE and the proteins were transferred to a nitrocellulose membrane.
Western blot analysis was carried out by separating protein extracts on 7% polyacrylamide-SDS gel and blotting onto a nitrocellulose membrane (φ 0.45 μm, Schleicher & Schüell, Germany).
For mRNA gel blot analysis, RNA was separated on denaturing 1% agarose gels and trasferred to nylon membrane (Genescreen Plus, PerkinElmer Inc).
