Anti sall2

Recombinant proteins corresponding to the entire intracellular regions (ICRs) of PTPRZ1, PTPRA, and PTPRM were expressed using a baculovirus-silkworm expression system, and purified as described^{6 (link)}. The ICRs of PTPRG, PTPRS, and PTPRB and the catalytic domains of PTPN1 and PTPN6 were expressed as glutathione-S-transferase (GST) fusion proteins from each pGEX plasmid in Escherichia coli strain BL21 (ref. 6 (link)). GST fusion proteins were purified by glutathione affinity chromatography as described^{43 (link)}. Chondroitinase ABC (chABC) was purchased from Sigma-Aldrich (catalog #C3667). Anti-PTPRZ-S, rabbit polyclonal antibodies against the extracellular region of PTPRZ was described previously (ref. 44 (link)). The following are the specificities and sources of the commercially available antibodies used in the present study: Anti-RPTPβ (a monoclonal antibody against the intracellular domain of PTPRZ1 receptors, #610179, BD Biosciences), anti-SOX2 (#ab97959, Abcam), anti-POU3F2 (#12137, Cell Signaling), anti-OLIG2 (#AB9610, Millipore), anti-SALL2 (#12679–1-AP, Proteintech Group), anti-GAPDH (#ab9482, Abcam) anti-phosphotyrosine (PY20; #ab16389, Abcam), and anti-pY118-paxillin (#2541, Cell Signaling), mouse anti-paxillin antibody (#610569, BD Bioscience), anti-MBP (#sc-13914, Santa Cruz Biotechnology), and anti-NG2 proteoglycan (#AB5320, Millipore).

Different types of treated HLCZ01 cells were lysed in a RIPA buffer supplemented with proteinase inhibitors. 30 μg of proteins were loaded and separated on SDS-PAGE gel; then, the proteins were transferred onto a PVDF membrane, blocked in 5% (w/v) non-fat milk, and incubated with the primary antibodies. Sources of the primary antibodies were anti-STAT3 (H-190) (Santa Cruz, H-190, sc-7179), p-STAT3 (Tyr705) (Santa Cruz, sc-7993), anti-SALL1 (cat# ab130705), anti-SALL2 (Proteintech, cat#12679-1-AP), and anti-SALL4 mAb (Abcam, cat#ab61703). Protein bands were visualized by enhanced chemiluminescence (Milipore).