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On the other hand, Morf4l1-/ MEFs showed lower expression levels of Brca1 and Brca2, but results were variable for Rad51 - Palb2 levels could not be assessed because the antibodies tested did not cross-react in mouse cell extracts.
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An experiment resembling this one has been recently tried in a murine-to-porcine iSCNT system, whereby mouse ES cell extracts were injected along with a mouse nucleus into mtDNA-depleted recipient porcine oocytes.
The commercial anti-vimentin antibody showed a somewhat weaker signal for vimentin in the M210B4 mouse cell line extract which we attributed to the lower reactivity of this antibody with rodent vimentin than with human vimentin as described previously for this antibody [47].
The mouse monoclonal anti-fiber antibody TB5 was generated by immunisation of a Balb/C mouse with whole cell extracts of Balb/C 3T3 cells infected with Ad5.
Serum samples were collected from age- and sex-matched mice and SaOS2 cell extracts were harvested in radioimmunoprecipitation assay buffer (Santa Cruz Biotechnology) using a standard protocol.
We observed the in vivo binding of AATYK1A to Cdk5/p35 using anti-AATYK1 coimmunoprecipitation from HEK293 cell extracts and mouse brain extracts.
For immunoblotting, protein concentration of whole cell extracts and mouse brain lysates was measured using the Bradford protein assay.
293T whole cell extracts and mouse liver lysates were prepared using Lysis buffer containing 1%TX-100 as previously described (Lamia et al., 2004).
Whole cell extracts of mouse D3 cells infected with control non-target (NT) lentiviruses or with lentiviruses targeting XPC (shXPC) or DKC1 (shDKC1-1 and shDKC1-2) analyzedyzed by western blotting.
Although the underlying kinase could not be identified, using a partially purified kinase fraction derived from nuclear cell extracts of mouse leukemia cells, it was shown that histone H3 can be arginine phosphorylated at R2 as well as R128, R129, and R131 in the C-terminus of the protein.
The founder mice were mated with C57BL/6 mice and both the transmittance of the transgene and the successful expression of human G0S2 protein were examined by western blot analysis of total cell extracts of mouse tails using one of the anti-G0S2 monoclonal antibodies (clone #3-1) we generated (see section 3.4 and Supplementary Fig. S2).
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