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Journal: The Journal of Biological Chemistry
Article Title: Glycolipid transfer protein modulates vesicular trafficking from the endoplasmic reticulum in HeLa cells
doi: 10.1016/j.jbc.2026.111378
Figure Lengend Snippet: Cells do not compensate for the lack of GLTP by increasing levels of UGCG or LTPs, although protein localizations are altered in the absence of GLTP . A , Western blot of analysis of the levels of UGCG, FAPP2 and CERT in WT HeLa, GLTP KO, GLTP rescue and ΔFFAT-GLTP HeLa cells. Antibodies used are described in the Materials section. Beta-actin was used as a loading control. The protein band in the upper blot that runs between FAPP2, and beta-actin is unidentified. B , representative fluorescence images of coimmunostaining of glucosylceramide synthase UGCG ( green ) and Golgi marker golgin-97 ( red ) in HeLa WT cells and, ( C ) GLTP KO HeLa cells. D , immunostaining of UGCG ( green ) and golgin-97 ( red ) in GLTP rescue HeLa cells and ( E ) ΔFFAT-GLTP expressing HeLa cells. The scale bar represents 200 μm. The subpanels are higher magnifications (2x) of representative cells. CERT, ceramide transport protein; FAPP2, four-phosphate adaptor protein 2; UGCG, UDP-glucose ceramide glucosyltransferase; GLTP, glycolipid transfer protein; GLTP KO, GLTP knockout.
Article Snippet: The primary commercial antibodies used were α-Sec12 (rabbit, AB181212 ; Abcam), α-Sec16 (rabbit, HPA005684; Sigma-Aldrich), α-Sec23 A (goat, PA5-19011; Invitrogen), α-Sec23 B (mouse, MA5-27262; Invitrogen), α-Sec31 A (rabbit, PA5-52147; Invitrogen),
Techniques: Western Blot, Control, Fluorescence, Marker, Immunostaining, Expressing, Knock-Out
Journal: bioRxiv
Article Title: A lipid-binding protein in black-legged tick saliva selectively recognizes Borrelia burgdorferi lipids
doi: 10.64898/2026.05.04.722819
Figure Lengend Snippet: Extracted B. burgdorferi lipids (∼0.7-0.8 nmol total) were spotted on nitrocellulose films, along with spots of palmitoyl oleoyl phosphatidylcholine (POPC) (39 nmol), cholesteryl stearate (47 nmol), 1,2-dipalmitoyl-sn-glycerol (DAG) (80 nmol), and ⍺-galactosyl ceramide (21 nmol). After blocking with bovine serum albumin, films were equilibrated with TULIP2, washed, developed with mouse anti-TULIP2 antibody and horseradish peroxidase-linked anti-mouse IgG, and imaged by chemiluminescence. Spot intensities, quantified by ImageJ, were normalized to B. burgdorferi lipids. Statistical significance (t-test): **, P < 0.005; ***, P< 0.0005; n.s., not significant
Article Snippet: Control samples for the lipid dot blots were selected to contain functional groups representative of the known composition of B. burgdorferi membrane lipids – : 1-palmitoyl-2-oleoylphosphatidylcholine (Avanti), cholesteryl stearate (Sigma), 1,2-dipalmitoylglycerol (Avanti), and
Techniques: Blocking Assay