caki 2  (ATCC)

Journal: Journal of Cannabis Research

Article Title: Design, synthesis, and biological profiling of fluorinated cannabidiol and cannabigerol derivatives as promising therapeutic agents

doi: 10.1186/s42238-026-00403-1

Figure Lengend Snippet: Inhibitory effects of CBD ( A ) and CBG derivatives ( B ) on human renal cancer cells. A-498 and CAKI-2 cell lines plated with 6 × 10 3 density were treated with 10, 30 and 60 µM of the examined compounds, respectively, and fluorescence intensities of living cells were measured to determine the cytotxic effect of the compounds. The intensity of treated samples was normalized to the untreated control samples. Value of 0.05 was set as the threshold for statistical significance. The figure represents mean ± SD

Article Snippet: Human renal carcinoma cell lines, A-498 and CAKI-2 obtained from the American Type Culture Collection (ATCC, Rockville, MD, USA) were cultured in Iscove’s Modified Dulbecco’s Medium (IMDM) supplemented with 10% Fetal Bovine Serum (FBS) and antibiotics (100 U/ml penicillin and 100 μg/ml streptomycin) and maintained at 37 °C in a humidified atmosphere under 5% CO 2 /95% air.

Techniques: Fluorescence, Control

Journal: Communications Medicine

Article Title: Targeting and dissociating HIF2α from the molecular chaperone Hsp70 triggers apoptosis in kidney cancer

doi: 10.1038/s43856-025-01356-x

Figure Lengend Snippet: a Caki-2 cells were treated with 30 μM Compound-c2 for the indicated durations. The stability of HIF1α was assessed by immunoblotting. β-actin was used as a loading control. LE Long Exposure, SE Short Exposure. b Lysate from 786-O cells was challenged with the indicated amounts of Biotin-Compound-c2 for 1 h. HIF2α binding and input was assessed by immunoblotting. c Empty vector (EV) and HA-HIF2α were transiently expressed in HEK293 cells and lysates were challenged with the indicated amounts of Biotin-Compound-c2 for 1 h. HIF2α binding to Compound-c2 was assessed by immunoblotting. d Amino acid sites of the HIF2α PAS-B domain predicted to contact Compound-c2. Residues shown are those within 3.5 Å of the docked model of Compound-c2. e HEK293 cells were transiently transfected with indicated HA-HIF2α mutants. Lysates were challenged with 1 µM of Biotin-Compound-c2 for 1 h and HIF2α binding to Compound-c2 was assessed by immunoblotting. Densitometry was performed using Photoshop v.23.5.1 to quantify Western blot band signal intensity. Bars represent the mean signal intensity values of HIF2α pulldown:HIF2α input compared to that of WT for three independent measurements. Error bars represent the standard deviation (S.D.) of three independent measurements. A Student’s t test (two-sided) was performed to assess statistical significance compared to WT control (NS- not significant). (See also Fig. S3B-C).

Article Snippet: Cultured human embryonic kidney (HEK293) (ATCC, Cat# CRL-1573; RRID:CVCL_0045), (Human, unknown) and HK-2 (ATCC, Cat# CRL-2190; RRID:CVCL_0302), (Human, Male) cells were grown in Dulbecco’s Modified Eagle Medium (DMEM, Sigma-Aldrich), 786-O cells (ATCC Cat# CRL-1932; RRID:CVCL_1051), (Human, Male) OS-RC-2 (RIKEN Cell Bank, Tsukuba, Japan, RRID:CVCL_1626) cells (Human, Male), and TUHR14TKB (RIKEN Cell Bank, Tsukuba, Japan, RRID:CVCL_5953) cells (Human, Male) in Roswell Park Memorial Institute (RPMI)1640 Medium (Sigma-Aldrich), A498 cells (ATCC Cat# CRL-44; RRID:CVCL_1056), (Human, Female) in Minimum Essential Medium (MEM, Sigma-Aldrich), Caki-1 (ATCC Cat# HTB-46; RRID:CVCL_0234), (Human, Male) and Caki-2 cells (ATCC Cat# HTB-47; RRID:CVCL_0235), (Human, Male) in McCoy’s 5 A Medium (Sigma-Aldrich) all supplemented with 10% fetal bovine serum (FBS, Sigma-Aldrich).

Techniques: Western Blot, Control, Binding Assay, Plasmid Preparation, Transfection, Standard Deviation