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Image Search Results
Journal: OncoImmunology
Article Title: An epitope-specific novel anti-EMMPRIN polyclonal antibody inhibits tumor progression
doi: 10.1080/2162402x.2015.1078056
Figure Lengend Snippet: Figure 1: EMMPRIN structure and peptide design, and specificity of 161-Ab: (A) Partial
Article Snippet: One strip was probed with the 1:1,000 diluted commercial
Techniques:
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: Measurement of HAb18G/CD147 expression on resting and activated CD 24+ and CD 8+ T cell subsets. Purified resting T cells and activated T cells were stained with PE- conjugated anti-CD147, FITC-conjugated anti-CD4 or CD8, and were analysed by flow cytometry. (A) Histogram shows expression of CD147 on resting and activated CD 24+ T cells. (B) Histogram shows expression of CD147 on resting and activated CD 8+ T cells. These data are representative of a minimum of three separate experiments.
Article Snippet:
Techniques: Expressing, Purification, Staining, Flow Cytometry
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: HAb18G/CD147 accumulates to the cap and lipid rafts in T cells upon TCR stimulation confirmed by confocal microscopy and Western blot. (A, B, C, D) HAb18G/CD147 co-caps with CD4/CD8/CD48/GM1. T cells were prepared and stained as described previously in ‘Materials and methods’. HAb18G/CD147, TCR co-receptor CD4 and CD8, lipid raft marker CD48 and GM1 diffusely distribute on the cell membrane of resting T cells (upper panel of –D), whereas stimulation results in translocation of these molecules to the cap induced by TCR/CD3 (lower panel of –D), scale bar, 5 μm. (E) HAb18G/CD147 is recruited to lipid rafts upon T cell activation. Lipid rafts were isolated as described previously in ‘Materials and methods’. Sucrose fractions were analysed by Western blot with HAb18, anti-Fyn and anti-Rab5 antibodies. Detergent-insoluble membrane fractions containing isolated rafts were identified by the presence of the raft marker protein Fyn. Non-raft components of the membrane ( e.g. Rab5) were purified in the heavy fraction (HF). HAb18G/CD147 appeared constitutively in the HF (7–9) with the non-raft marker Rab5 in resting T cells, a significant fraction of HAb18G/CD147 was localized within raft fractions (1–4) after T cell activation.
Article Snippet:
Techniques: Confocal Microscopy, Western Blot, Staining, Marker, Membrane, Translocation Assay, Activation Assay, Isolation, Purification
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: HAb18G/CD147 together with CD48 and GM1 are enriched into the IS. Raji cells were labelled with the blue fluorescent cytoplasmic probe CMAC first. Jurkat cells were then incubated with CMAC-labelled and 1 μg/ml of SEB-loaded (or not) Raji cells. Conjugates were then plated onto cover slip, fixed, stained with antibodies to HAb18G/CD147 and to CD48 or GM1 , and visualized by confocal fluorescence microscopy. The red and green images represent the localization and distribution of HAb18G/CD147 and CD48/GM1, respectively. Raji cells are shown in blue. Scale bar, 5 μm.
Article Snippet:
Techniques: Incubation, Staining, Fluorescence, Microscopy
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: Influence of HAb18G/CD147 mAbs on T cell proliferation. Proliferation was determined on day 4 following stimulation as described in ‘Materials and methods’. This figure shows the [ 3 H]-thymidine incorporation in c.p.m. (mean ± S.D. of triplicated wells). Data are a representative of three independent experiments. ***, P , 0.001.
Article Snippet:
Techniques:
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: Cross-linking of HAb18G/CD147 with mAb 5A12 affects surface expression of CD25 and cytokine production. (A) mAb 5A12 down-regulates surface expression of CD25. Red-tinted histogram represents isotype control. Black and green lines represent anti-CD3 mAb plus isotype-matched irrelevant control mAb (mouse IgG1) or 5A12 intervention, respectively. (B, C, D) mAb 5A12 decreases IL-2 and IL-4 but increases IFN-γ production. Purified T cells were stimulated with immobilized 1 μg/ml of anti-CD3 mAb or 1 μg/ml of anti-CD3 mAb plus 10 μg/ml anti-CD28 mAb in the presence of 10 μg/ml mAb 5A12 or isotype-matched irrelevant control for 72 hrs. Bar graphs, (mean ± S.D.) levels of IL-2, IL-4 and IFN-γ in culture supernatants as measured by ELISA. *, P , 0.05.
Article Snippet:
Techniques: Expressing, Control, Purification, Enzyme-linked Immunosorbent Assay
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: Inhibition of anti-CD3 stimulated redistribution of the CD48 molecule by HAb18G/CD147 mAb 5A12. Purified peripheral blood T cells were cultured and stimulated with immobilized CD3 mAb in the presence or absence of 10 μg/ml of HAb18G/CD147 mAb 5A12 or isotype-matched irrelevant control mAb for 2 hrs. Then, cells were collected, fixed and stained with FITC-labelled CD48 as described in ‘Materials and methods’. The percentage of cells showing cap was assessed by analysing the distribution of the fluorescence intensity on the cell membrane of CD48-FITC stained cells using FV10-ASW (version 1.6) software. The images are a representative of three experiments. Scale bar, 5 μm. **, P , 0.01.
Article Snippet:
Techniques: Inhibition, Purification, Cell Culture, Control, Staining, Fluorescence, Membrane, Software
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: Cross-linking of HAb18G/CD147 with mAb 5A12 affects intracellular signalling pathway upon T cell activation. (A) Extracellular Ca 2+ influx triggered by TCR stimulation is inhibited by mAb 5A12. The figure is a representative of three experiments. (B) HAb18G/CD147 mAb 5A12 slightly decreases the tyrosine phosphorylation level upon TCR triggering. Purified T cells were stimulated using CD3 mAb (plus mAb CD28) in the presence of mAb 5A12 or isotype-matched irrelevant control. After 2 hrs of stimulation, the cells were lysed and analysed for tyrosine phosphorylation level using Western blot. The figure is a representative of three experiments. Top, the representative image; bottom, quantitative analysis of the image.
Article Snippet:
Techniques: Activation Assay, Phospho-proteomics, Purification, Control, Western Blot
Journal: Journal of Cellular and Molecular Medicine
Article Title: Involvement of HAb18G/CD147 in T cell activation and immunological synapse formation
doi: 10.1111/j.1582-4934.2010.01012.x
Figure Lengend Snippet: Computer-assisted molecular docking of HAb18G/CD147 antigen-antibody complex. (A) The modelled structure of the variable domain of mAb HAb18 was docked to the most membrane-distal region of HAb18G/CD147 in a head-to-head manner. (B) The variable domain of mAb 6H8 was docked to C-terminal domain II of HAb18G/CD147. (C) The interaction between mAb 5A12 and HAb18G/CD147. The binding zone localizes at the functional N-terminal domain I. (D) Overview of docking the three mAbs to HAb18G/CD147 extracellular portion.
Article Snippet:
Techniques: Membrane, Binding Assay, Functional Assay
Journal: bioRxiv
Article Title: Non-canonical alternate interactors of SARS CoV-2 Spike protein implicated in placental susceptibilty
doi: 10.64898/2026.10.08.757814
Figure Lengend Snippet: Expression of candidate proteins – CD147, EGFR and LDLR in the placenta tissue. Distinct bands were observed for all three receptors. The observed band size for Basigin, EGFR and LDLR are 40kDa, 175kDa and 100kDa respectively.
Article Snippet: The protein of interest, CD147 was immobilised on agarose beads using 1.52ug of
Techniques: Expressing, Tissue
Journal: bioRxiv
Article Title: Non-canonical alternate interactors of SARS CoV-2 Spike protein implicated in placental susceptibilty
doi: 10.64898/2026.10.08.757814
Figure Lengend Snippet: Representative figures of protein expression and localisation of ACE2, CD147/basigin, EGFR and LDLR as determined by immunohistochemistry. The left panel shows the protein expression level in control group and the right panel shows receptor protein expression changes in pregnant women with high exposure risk to SARS-CoV-2.
Article Snippet: The protein of interest, CD147 was immobilised on agarose beads using 1.52ug of
Techniques: Expressing, Immunohistochemistry, Control
Journal: bioRxiv
Article Title: Non-canonical alternate interactors of SARS CoV-2 Spike protein implicated in placental susceptibilty
doi: 10.64898/2026.10.08.757814
Figure Lengend Snippet: Protein expression (by quantification of IHC) and mRNA expression (by qRT-PCR) of (A) ACE2 (B) CD147/basigin (C) EGFR (D) LDLR in placental samples obtained from control women and those with exposure risk to COVID during pregnancy. Blue triangles indicate mRNA expression; red dots indicate the corresponding protein expression.
Article Snippet: The protein of interest, CD147 was immobilised on agarose beads using 1.52ug of
Techniques: Expressing, Quantitative RT-PCR, Control
Journal: bioRxiv
Article Title: Non-canonical alternate interactors of SARS CoV-2 Spike protein implicated in placental susceptibilty
doi: 10.64898/2026.10.08.757814
Figure Lengend Snippet: In all cases the protein of interest (A) CD147, (B) EGFR and (c) LDLR was immobilised on agarose beads using specific antibody which was incubated with placental lysates expressing these proteins. Interaction with spike was assessed by incubation with spike expressing 293T cell lysates. Presence of spike was observed via immunoblotting for spike using specific antibody. +S indicates cell homogenate expressing spike, -S indicates control cell homogenate without spike, B indicates antibody bound fraction, UB the unbound fraction, +ANTIBODY: lysate with antibody for target receptor protein, -ANTIBODY: lysate without antibody for target receptor protein. Observed band size for spike is 110 kDa for A, B and C.
Article Snippet: The protein of interest, CD147 was immobilised on agarose beads using 1.52ug of
Techniques: Incubation, Expressing, Western Blot, Control