Anti gapdh antibody 60004 1 ig

Western blot analysis was performed as previously described [22 (link)]. Antibodies used in this study are as follows: anti-PARP1 (#9532), anti-Caspase-3 (#9662), anti-Cleaved Caspase-3 (#9661), anti-Caspase-9 (#9502), anti-Cleaved Caspase-9 (#9505), anti-p53 (#9282) antibodies obtained from Cell Signaling Technology (Beverly, MA, USA), anti-Bcl-2 (ab32124), anti-Bax (ab32503), and anti-Phospho-FOXO3a(Thr32) (#9464) antibodies obtained from Abcam (Abcam, Cambridge, UK), anti-PUMA antibody (ER31215) obtained from HuaBio (Hangzhou, China), anti-WTIP antibody (PA5-48292) obtained from Thermo Fisher Scientific (Thermo Fisher Scientific, Waltham, USA), anti-FLAG antibody purchased from Sigma-Aldrich (St. Louis, MO, USA), anti-FOXO3a (#2497) and anti-GAPDH antibody (60004-1-Ig) obtained from Proteintech (Proteintech Group, Chicago, IL, USA).

Total protein of fresh mycelia (100 mg) was extracted with 1 ml RIPA extraction buffer and 10 μl protease inhibitor cocktail (Gu et al., 2015). The protein sample was mixed with loading buffer and boiled for 10 min before 10 μl of the sample was separated by 10% SDS polyacrylamide gel electrophoresis (SDS‐PAGE) and transferred onto a polyvinylidene fluoride membrane with a Bio‐Rad electroblotting apparatus.
The FgNTH‐3 × FLAG fusion strain was generated by complementing the ΔFgNTH deletion mutants with a fusion fragment carrying the 3 × FLAG gene. FgGPI‐GFP and FgPK‐GFP fusion constructs were transformed into the FgNTH‐3 × FLAG fusion strain to generate double‐label strains FgNTH‐3 × FLAG‐FgPK‐GFP and FgNTH‐3 × FLAG‐FgGPI‐GFP. All strains carrying label were confirmed by western blot analyses. For Co‐IP assays, total proteins were extracted and incubated with GFP‐Trap_MA beads. Proteins eluted from the agarose were analysed by western blotting with monoclonal anti‐FLAG 390002 (Zenbio) and monoclonal anti‐GFP antibodies 300943 (Zenbio), respectively. Each protein sample was also detected with anti‐actin antibody 700068 (Zenbio) or anti‐GAPDH antibody 60004–1‐Ig (Proteintech) as a reference. Incubation with a secondary antibody and chemiluminescent detection were performed as described previously (Zhou et al., 2020).

The Western blot analysis was performed as described in a previous study [55 (link)] using anti-DTYMK antibody (15360-1-AP, Proteintech, IL, USA), anti-MAPKAPK2 antibody (13949-1-AP, Proteintech, IL, USA), anti-GAPDH antibody (60004-1-Ig, Proteintech, IL, USA), anti-phospho-HSP27 (Ser82) antibody (9709 T, Cell Signaling Technology, MA, USA), anti-NF-κB p65 antibody (8242 s, Cell Signaling Technology), and anti-Histone H3 antibody (Cell Signaling Technology).

C57BL/6J mice were purchased from the Animal Institute of Southern Medical University (Guangzhou, China). KM mice were purchased from the Animal Institute of Kunming Medical University (Kunming, China). All mice were kept in a pathogen-free environment with the temperature maintained at 21 °C–23 °C and relative humidity at 50%–60% under a 12-h:12-h light: dark cycle. All animal experiments in this study were approved by the Welfare and Ethical Committee for Experimental Animal Care of Southern Medical University and Kunming University of Science and Technology.
3-TC (Lamivudine, PHR1365) and G 418 disulfate salt (A1720) were purchased from Sigma-Aldrich. Anti-hnRNPA2B1 antibody (sc-32316, diluted 1:500) was purchased from Santa Cruz (Santa Cruz, CA, USA). Anti-GAPDH antibody (60004-1-Ig, diluted 1:30,000) was purchased from Proteintech (Chicago, IL, USA). TBK1/NAK rabbit mAb (38066, diluted 1:1000), phospho-TBK1/NAK (Ser172) rabbit mAb (5483, diluted 1:1000), IRF-3 rabbit mAb (4302, diluted 1:1000), and phospho-IRF-3 (Ser396) rabbit mAb (29047, diluted 1:1000) were purchased from Cell Signaling Technology (Danvers, MA, USA). Anti-HBV core antigen/HBcAg antibody (ab8637, diluted 1:500) was purchased from Abcam (Cambridge, UK).