lsm5 pascal software version 3.2 (Carl Zeiss)
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90
Structured Review
Carl Zeiss
lsm5 pascal software version 3.2
Lsm5 Pascal Software Version 3.2, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/zeiss+histogram+analysis+function/5+confocal+lsm+microscope+pascal/pmc01831817-223-2-11
Average 90 stars, based on 1 article reviews
Lsm5 Pascal Software Version 3.2, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/zeiss+histogram+analysis+function/5+confocal+lsm+microscope+pascal/pmc01831817-223-2-11
Average 90 stars, based on 1 article reviews
lsm5 pascal software version 3.2 - by Bioz Stars,
2026-09
90/100 stars
Images
1) Product Images from "Clathrin-dependent pathways and the cytoskeleton network are involved in ceramide endocytosis by a parasitic protozoan, Giardia lamblia"
Article Title: Clathrin-dependent pathways and the cytoskeleton network are involved in ceramide endocytosis by a parasitic protozoan, Giardia lamblia
Journal:
doi: 10.1016/j.ijpara.2006.09.008
Figure Legend Snippet: Quantitative analysis of confocal images. Fluorescence intensities for Bodipy-ceramide in the presence and absence of anti-cytoskeleton agent were measured by Zeiss LSM 5 PASCAL software version 3.2. Labeled trophozoites were randomly selected and analyzed as described Materials and methods. Results (fluorescence/area × 104) show that vinorelbine reduces ceramide uptake significantly.
Techniques Used: Fluorescence, Software, Labeling
Figure Legend Snippet: Potassium-depletion affects the colocalization of Bodipy-ceramide with anti-clathrin antibody. Both control and K+-depleted cells were first treated with Bodipy-ceramide (200 nM) for 30 min before reacting with anti-clathrin antibody. A) a) identifies clathrin-positive structures in trophozoites cultured in normal growth medium. b) is the 3D reconstruction of the same picture (a) using VIS-ART software (Carl Zeiss). Insets (a and b) show the association of vesicles with plasma membranes. B) c) demonstrates the localization of clathrin-positive vesicles in the presence of ceramide, which reveals enlargement of vesicles and migration towards endoplasmic reticulum/perinuclear regions. d) depicts Bodipy-ceramide labeling of trophozoites; and e) is the colocalization of ceramide with clathrin-coated vesicles in the endoplasmic reticulum/perinuclear regions. f, g) show clathrin-positive structures and Bodipy-ceramide labeling of K+-depleted cells. K+-depletion causes puffiness of trophozoites, illuminates discrete and isolated clathrin-like vesicles (f), and lowers ceramide uptake significantly (g). h) is the merger of images of (f) and (g). Histograms of fluorescence images (fluorescence/area × 104, measured by Zeiss LSM5 PASCAL software version 3.2) in (C) show the relative amount of Bodipy-ceramide internalized by parasites in control and K+-depleted cells. Arrowheads denote endoplasmic reticulum/perinuclear membranes and arrows indicate vesicle-like structures. Bars: 5 μM.
Techniques Used: Control, Cell Culture, Software, Clinical Proteomics, Migration, Labeling, Isolation, Fluorescence
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