LBL1

LBL1 (100 μM; 30 min) does not intercalate into DNA even at concentrations as high as 100 μM^[1].
LBL1 (2.5-5.0 μM; 24 h) does not induce phosphorylation of histone H2AX (γ-H2AX) in normal primary foreskin fibroblasts at concentrations up to 5.0 μM with a 24 h treatment duration^[1].
LBL1 (2.5 μM; 24 h) does not reduce Rad51 mRNA levels in MDA-MB-231 human breast cancer cells, which indicates that Rad51 is subject to post-translational regulation^[1].
LBL1 (1-100 μM; 1 h) dose-dependently induces higher-order oligomerization of purified recombinant LA (1−387) in vitro^[2].
LBL1 binds to the purified recombinant lamin A fragment LA (1-387), with an apparent dissociation constant K_d of 5.11 μM. This result is confirmed by the dose-dependent increase in the first melting temperature of the protein^[3].
LBL1 (0-2.5 μM; 48 h) dose-dependently arrests the breast cancer cell line MDA-MB-231 at the G2/M phase, and induces G1 peak broadening at concentrations up to 2.5 μM following 48 h of treatment, a phenomenon consistent with the formation of DNA double-strand breaks^[1].
LBL1 significantly increases the number of γ-H2AX foci-positive MDA-MB-231 breast cancer cells, indicating the formation of DNA double-strand breaks^[1].
LBL1 (30 h) induces significant double-strand DNA breaks in breast cancer MDA-MB-231 cells, a result verified by the increased tail DNA content in neutral comet assays^[1].
LBL1 (0-2.5 μM; 24 h) induces proteasome-mediated degradation of the Rad51 protein in breast cancer MDA-MB-231 cells^[1].
LBL1 (72 h) inhibits the growth of MDA-MB-468 and MDA-MB-231 breast cancer cells, with GI₅₀ values of 0.44 μM and 1.60 μM against the two cell lines respectively after 72 h of incubation^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.