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blood brain barrier bbb  (Abbott Laboratories)

 
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    Abbott Laboratories blood brain barrier bbb
    Blood Brain Barrier Bbb, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/bbb/barrier+blood+brain/pm42309152-84-9-20
    Average 86 stars, based on 1 article reviews
    blood brain barrier bbb - by Bioz Stars, 2026-10
    86/100 stars

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    Related Articles

    In Vitro:

    Article Title: Functional and targeted proteomics characterization of a human primary endothelial cell model of the blood-brain barrier (BBB) for drug permeability studies.
    Article Snippet: The blood-brain barrier (BBB) protects the brain from toxins but hinders the penetration of neurotherapeutic drugs.. Therefore, the blood-to-brain permeability of chemotherapeutics must be carefully evaluated.. Here, we aimed to establish a workflow to generate primary cultures of human brain microvascular endothelial cells (BMVECs) to study drug brain permeability and bioavailability.

    Permeability:

    Article Title: Functional and targeted proteomics characterization of a human primary endothelial cell model of the blood-brain barrier (BBB) for drug permeability studies.
    Article Snippet: The blood-brain barrier (BBB) protects the brain from toxins but hinders the penetration of neurotherapeutic drugs.. Therefore, the blood-to-brain permeability of chemotherapeutics must be carefully evaluated.. Here, we aimed to establish a workflow to generate primary cultures of human brain microvascular endothelial cells (BMVECs) to study drug brain permeability and bioavailability.

    Diffusion-based Assay:

    Article Title: Breaking barriers: how cytomegaloviruses manipulate myeloid cells to invade tissues
    Article Snippet: .. BBB allows for the selective diffusion of nutrients and essential macromolecules and restricts access of toxic substances, immune cells, and pathogens to the parenchyma (Abbott et al, ). ..

    Article Title: Breaking barriers: how cytomegaloviruses manipulate myeloid cells to invade tissues.
    Article Snippet: .. BBB allows for the selective diffusion of nutrients and essential macromolecules and restricts access of toxic substances, immune cells, and pathogens to the parenchyma (Abbott et al, 2010). ..

    other:

    Article Title: Amyloid-Beta Peptides 40 and 42 Employ Distinct Molecular Pathways for Cell Entry and Intracellular Transit at the Blood-Brain Barrier Endothelium.
    Article Snippet: BBB is a physiologic interface between blood and the brain that maintains the brain homeostasis by delivering essential nutrients to the brain and removing toxic metabolites out of the brain (Ballabh et al., 2004; Abbott et al., 2010).

    Virus:

    Article Title: Distinct ZIKV strain signatures and type I IFN modulation reveal a protective role of brain endothelial interferon signaling in vitro and in vivo
    Article Snippet: .. Neuroinvasion by systemic viruses often involves virus crossing through the BBB, a complex structure composed of microvascular endothelial cells associated with astrocytes, microglia, and pericytes, which regulates the traffic of cells, solutes, and pathogens into the central nervous system (CNS) (rev in Abbott et al., 2010; Kadry et al., 2020). ..



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    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of <t>two-photon</t> <t>microscopy</t> to assess the <t>BBB</t> penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).
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    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of <t>two-photon</t> <t>microscopy</t> to assess the <t>BBB</t> penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).
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    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of <t>two-photon</t> <t>microscopy</t> to assess the <t>BBB</t> penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).
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    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of <t>two-photon</t> <t>microscopy</t> to assess the <t>BBB</t> penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).
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    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of <t>two-photon</t> <t>microscopy</t> to assess the <t>BBB</t> penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).
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    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of <t>two-photon</t> <t>microscopy</t> to assess the <t>BBB</t> penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).
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    Image Search Results


    Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of two-photon microscopy to assess the BBB penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).

    Journal: Bioactive Materials

    Article Title: Cyanobacteria-derived near-infrared autofluorescent exosomes enabling synergistic brain lesion imaging and neuroprotection

    doi: 10.1016/j.bioactmat.2026.04.027

    Figure Lengend Snippet: Fabrication and characterizations of sExo. (A) Schematic diagram of the preparation of sExo. (B) TEM image of SYN and sExo. (C) In vivo fluorescence imaging of SYN and sExos intravenously injected into tMCAO mice. (D) The average fluorescence intensity ratio between the right brain and the left brain in the mice. (E) Ex vivo fluorescence imaging of mouse organs in each group. H, heart; Li, liver; S, spleen; Lu, lung; K, kidney; B, brain. (F) Average radiation efficiency in each group on the basis of tissue fluorescence intensity (n = 3). (G) Comparison of the average fluorescence intensity between the SYN and sExo groups across major ex vivo mouse tissues. (H) The schematic shows the use of two-photon microscopy to assess the BBB penetration of SYN and sExo. A cranial window was created after fixing the mouse head on a brain locator, allowing direct observation of brain regions. (I) In vivo two-photon imaging showing the penetration of SYN and sExo from blood vessels into the brain parenchyma 30 min after intravenous injection in tMCAO mice. Red, Cy5.5 (sExo: Ex 644 nm/Em 655 nm); green, FITC-dextran (MW = 2000 KDa). (J) Expression of cyanobacteria-related proteins. (K) Three-dimensional binding model between integrin α 4 β 1 (green) and Q31PR1 (magenta) (left), and schematic diagram of interface residue interactions (right). (L) Three-dimensional binding model between ICAM-1 (green) and Q9KHA8 (magenta) (left), and schematic diagram of interface residue interactions (right). (M) Three-dimensional binding model between P-gp (green) and Q8VPU8 (magenta) (left), and schematic diagram of interface residue interactions (right). One-way ANOVA, two-way ANOVA or two-tailed unpaired t-tests were used to calculate p -values. (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ns, not significant).

    Article Snippet: Finally, the microstructure of the BBB was observed and imaged via transmission electron microscopy (JEM-1400FLASH, JEOL).

    Techniques: In Vivo, Fluorescence, Imaging, Injection, Ex Vivo, Comparison, Microscopy, Expressing, Binding Assay, Residue, Two Tailed Test

    sExo-mediated protection of BBB structure and function following ischemic stroke. (A) Digital images showing the extravasation of Evans blue dye from the damaged BBB. (B) Quantitative analysis of the Evans blue content in the different groups (n = 4). (C) Brain water content in different groups. (n = 4). (D) The process of detecting the integrity of the BBB by two-photon microscopy is schematically demonstrated. (E) In vivo two-photon imaging showing FITC-dextran (MW = 3500 Da) penetrating damaged vessels into the brain parenchyma. (F) WB analysis of VE-cadherin, Claudin-5, occludin and ZO-1 in the ischemic brains of different mice. (G) TEM images of BBB in different groups. TJ, tight junction; BM, basement membrane. One-way ANOVA was used to calculate p values (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001).

    Journal: Bioactive Materials

    Article Title: Cyanobacteria-derived near-infrared autofluorescent exosomes enabling synergistic brain lesion imaging and neuroprotection

    doi: 10.1016/j.bioactmat.2026.04.027

    Figure Lengend Snippet: sExo-mediated protection of BBB structure and function following ischemic stroke. (A) Digital images showing the extravasation of Evans blue dye from the damaged BBB. (B) Quantitative analysis of the Evans blue content in the different groups (n = 4). (C) Brain water content in different groups. (n = 4). (D) The process of detecting the integrity of the BBB by two-photon microscopy is schematically demonstrated. (E) In vivo two-photon imaging showing FITC-dextran (MW = 3500 Da) penetrating damaged vessels into the brain parenchyma. (F) WB analysis of VE-cadherin, Claudin-5, occludin and ZO-1 in the ischemic brains of different mice. (G) TEM images of BBB in different groups. TJ, tight junction; BM, basement membrane. One-way ANOVA was used to calculate p values (∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001).

    Article Snippet: Finally, the microstructure of the BBB was observed and imaged via transmission electron microscopy (JEM-1400FLASH, JEOL).

    Techniques: Microscopy, In Vivo, Imaging, Membrane