We used the following antibodies: anti-Flag M2 (F3165) (Sigma-Aldrich, St Louis, MO), mouse anti-Myc (sc-40), rabbit anti-Myc (sc-789), mouse anti-HA (sc-805), anti-Parp1 (sc-25780), mouse anti-TRAF3 (sc-6933), rabbit anti-TRAF3 (sc-1828), anti-p65 (sc-8008) (Santa Cruz Biotechnology, Santa Cruz, CA), anti-NIK (4994), anti-p52 (4882), anti-RelB (4922s) (Cell Signaling, Beverly, MA), anti-CnAα (07-067), anti-CnAβ (07-068), anti-tubulin (CP06) (Millipore, Darmstadt, Germany). The following reagents used were in experiments: MG132 (Peptide Institute, Osaka, Japan) and an agonistic anti-LtβR antibody (Alexis Biochemicals, Läufelfingen, Switzerland).
In vitro virus selection was performed as reported previously22 (link). Briefly, a cDNA library was prepared from mouse fetal thymus RNA (embryonic day 18.5). NIK mRNA was used as bait, and prey were co-translated in a wheat germ extract (Molecuence, Yokohama, Japan) using a Qiagen Biorobot 8000. After four rounds of selection, we identified interaction sequence tags obtained by in vitro virus and verified them as reported previously23 (link)40 (link).
In vitro virus selection was performed as reported previously22 (link). Briefly, a cDNA library was prepared from mouse fetal thymus RNA (embryonic day 18.5). NIK mRNA was used as bait, and prey were co-translated in a wheat germ extract (Molecuence, Yokohama, Japan) using a Qiagen Biorobot 8000. After four rounds of selection, we identified interaction sequence tags obtained by in vitro virus and verified them as reported previously23 (link)40 (link).
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