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    Santa Cruz Biotechnology resource source identifier itgb1 sirna human santa cruz biotechnology
    Resource Source Identifier Itgb1 Sirna Human Santa Cruz Biotechnology, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 64 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/%CE%B21+integrin+sc+35674/Integrin+%CE%B21+siRNA/pm41702399-284-2-8
    Average 93 stars, based on 64 article reviews
    resource source identifier itgb1 sirna human santa cruz biotechnology - by Bioz Stars, 2026-09
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    Article Title: Interaction of Serratia proteamaculans with Integrins Activates Invasion-Promoting Signaling Pathways
    Article Snippet: .. The expression of host-cell proteins was inhibited using siRNA targeting α5 integrin (sc-29372) and β1 integrin (sc-35674) (Santa Cruz Biotechnology, Dallas, TX, USA). .. Transfection of siRNAs was performed using siRNA Transfection Reagent (sc-29528) as recommended by the manufacturer (Santa Cruz Biotechnology, Dallas, TX, USA).

    Article Title: Interaction of Serratia proteamaculans with Integrins Activates Invasion-Promoting Signaling Pathways.
    Article Snippet: .. The expression of host-cell proteins was inhibited using siRNA targeting α5 integrin (sc-29372) and β1 integrin (sc-35674) (Santa Cruz Biotechnology, Dallas, TX, USA). .. Transfection of siRNAs was performed using siRNA Transfection Reagent (sc-29528) as recommended by the manufacturer (Santa Cruz Biotechnology, Dallas, TX, USA).



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    Santa Cruz Biotechnology itgb1
    ( A ) ELISA assessing the binding specificity of 2E7 scFv-Fc binding to the ITGA3B1 heterodimer and its individual subunits ( ITGA3 and <t>ITGB1</t> ), as well as to the structurally related integrin complex ITGA6B4 and its subunits ( ITGA6 and ITGB4 ). HuIgG and BSA were included as negative controls. Data represent the mean ± SD from three technical replicates. A 450 , absorbance at 450 nm. ( B ) Dose-dependent binding of 2E7 scFv-Fc to immobilized ITGA3 , ITGB1 , and ITGA3B1 , as determined by ELISA. ( C ) Flow cytometry analysis of HEK293 cells transiently transfected with ITGA3 , ITGB1 , or both. ( D ) Flow cytometry of MDA-MB-231 cells following siRNA knockdown of ITGA3 , ITGB1 , or both ITGA3 and ITGB1 . ( E ) SPR sensorgrams showing 2E7 scFv-Fc binding to recombinant ITGA3B1 in the presence of either divalent cations or EDTA. Data shown are representative of three independent experiments.
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    Santa Cruz Biotechnology sirna against integrin β1
    <t>Integrin</t> ß1, but not integrin ß3, is required for the formation of VM HEY-A8 GFP ( A ) or MDA-MB-231 ( B ) cells were incubated with a blocking antibody against <t>integrin</t> <t>β1</t> or integrin β3 before seeding on Matrigel for 96 h. Photographs were taken at 24 and 96 h. Blocking of integrin β1 is enough to stop the formation of VM. ( C ) Airy Scan microscopy demonstrating the presence of integrin ß1 (red) and the cell nucleus stained by DAPI (blue) in both cell lines during VM formation at 2 and 72 h. Scale bar = 100 μm. Panel A &B, representative images from a minimum of three experiments in each cell line. Panel C representative images from two experiments
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    <t>Integrin</t> ß1, but not integrin ß3, is required for the formation of VM HEY-A8 GFP ( A ) or MDA-MB-231 ( B ) cells were incubated with a blocking antibody against <t>integrin</t> <t>β1</t> or integrin β3 before seeding on Matrigel for 96 h. Photographs were taken at 24 and 96 h. Blocking of integrin β1 is enough to stop the formation of VM. ( C ) Airy Scan microscopy demonstrating the presence of integrin ß1 (red) and the cell nucleus stained by DAPI (blue) in both cell lines during VM formation at 2 and 72 h. Scale bar = 100 μm. Panel A &B, representative images from a minimum of three experiments in each cell line. Panel C representative images from two experiments
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    Santa Cruz Biotechnology itgβ1 sirna duplex
    Exosomes derived from MΦs cultured on different specimen surfaces differently regulate internalization and targeted lysosomal degradation of membrane <t>ITGβ1</t> of ECs. A) Immunofluorescence staining images of membrane ITGβ1 (omitted cell permeabilization) and quantitative analysis ( n = 8). B) Immunofluorescence staining images of total ITGβ1 and quantitative analysis ( n = 8). C) Western blotting analysis for cellular total ITGβ1 levels after incubated with the exosomes for 6 h (bafilomycin A was used to inhibit lysosomal degradation). D) ELISA test for cellular total ITGβ1 levels after incubated with the exosomes for 6 h ( n = 9). E) Colocalization analysis of ITGβ1 with LAMP1 after incubated with the exosomes for 4 h. Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.
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    Image Search Results


    ( A ) ELISA assessing the binding specificity of 2E7 scFv-Fc binding to the ITGA3B1 heterodimer and its individual subunits ( ITGA3 and ITGB1 ), as well as to the structurally related integrin complex ITGA6B4 and its subunits ( ITGA6 and ITGB4 ). HuIgG and BSA were included as negative controls. Data represent the mean ± SD from three technical replicates. A 450 , absorbance at 450 nm. ( B ) Dose-dependent binding of 2E7 scFv-Fc to immobilized ITGA3 , ITGB1 , and ITGA3B1 , as determined by ELISA. ( C ) Flow cytometry analysis of HEK293 cells transiently transfected with ITGA3 , ITGB1 , or both. ( D ) Flow cytometry of MDA-MB-231 cells following siRNA knockdown of ITGA3 , ITGB1 , or both ITGA3 and ITGB1 . ( E ) SPR sensorgrams showing 2E7 scFv-Fc binding to recombinant ITGA3B1 in the presence of either divalent cations or EDTA. Data shown are representative of three independent experiments.

    Journal: Science Advances

    Article Title: Phenotypic discovery and therapeutic evaluation of an ITGA3B1 -targeting antibody-drug conjugate for bladder cancer

    doi: 10.1126/sciadv.ady0041

    Figure Lengend Snippet: ( A ) ELISA assessing the binding specificity of 2E7 scFv-Fc binding to the ITGA3B1 heterodimer and its individual subunits ( ITGA3 and ITGB1 ), as well as to the structurally related integrin complex ITGA6B4 and its subunits ( ITGA6 and ITGB4 ). HuIgG and BSA were included as negative controls. Data represent the mean ± SD from three technical replicates. A 450 , absorbance at 450 nm. ( B ) Dose-dependent binding of 2E7 scFv-Fc to immobilized ITGA3 , ITGB1 , and ITGA3B1 , as determined by ELISA. ( C ) Flow cytometry analysis of HEK293 cells transiently transfected with ITGA3 , ITGB1 , or both. ( D ) Flow cytometry of MDA-MB-231 cells following siRNA knockdown of ITGA3 , ITGB1 , or both ITGA3 and ITGB1 . ( E ) SPR sensorgrams showing 2E7 scFv-Fc binding to recombinant ITGA3B1 in the presence of either divalent cations or EDTA. Data shown are representative of three independent experiments.

    Article Snippet: Target-specific siRNAs against ITGA3 (sc-35684) and ITGB1 (sc-35674), along with a nontargeting control siRNA (sc-37007), were obtained from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Flow Cytometry, Transfection, Knockdown, Recombinant

    ( A ) ITGA3 mRNA expression in normal bladder tissues ( n = 18) and primary bladder tumors ( n = 408) based on TCGA data. ( B ) ITGA3 expression across consensus molecular subtypes of bladder cancer from five aggregated clinical cohorts. ( C ) Representative multiplex immunofluorescence images of TMA cores stained for ITGA3 (green), ITGB1 (red), and nuclei [DAPI (4′,6-diamidino-2-phenylindole), blue] of primary bladder carcinomas and normal tissues. Scale bars, 100 μm. ( D to F ) Quantification of ITGA3 expression in tumor versus normal tissues: fluorescence intensity (D), percentage of ITGA3 -positive cells (E), and H -scores (F). **** P < 0.0001.

    Journal: Science Advances

    Article Title: Phenotypic discovery and therapeutic evaluation of an ITGA3B1 -targeting antibody-drug conjugate for bladder cancer

    doi: 10.1126/sciadv.ady0041

    Figure Lengend Snippet: ( A ) ITGA3 mRNA expression in normal bladder tissues ( n = 18) and primary bladder tumors ( n = 408) based on TCGA data. ( B ) ITGA3 expression across consensus molecular subtypes of bladder cancer from five aggregated clinical cohorts. ( C ) Representative multiplex immunofluorescence images of TMA cores stained for ITGA3 (green), ITGB1 (red), and nuclei [DAPI (4′,6-diamidino-2-phenylindole), blue] of primary bladder carcinomas and normal tissues. Scale bars, 100 μm. ( D to F ) Quantification of ITGA3 expression in tumor versus normal tissues: fluorescence intensity (D), percentage of ITGA3 -positive cells (E), and H -scores (F). **** P < 0.0001.

    Article Snippet: Target-specific siRNAs against ITGA3 (sc-35684) and ITGB1 (sc-35674), along with a nontargeting control siRNA (sc-37007), were obtained from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Expressing, Multiplex Assay, Immunofluorescence, Staining, Fluorescence

    Integrin ß1, but not integrin ß3, is required for the formation of VM HEY-A8 GFP ( A ) or MDA-MB-231 ( B ) cells were incubated with a blocking antibody against integrin β1 or integrin β3 before seeding on Matrigel for 96 h. Photographs were taken at 24 and 96 h. Blocking of integrin β1 is enough to stop the formation of VM. ( C ) Airy Scan microscopy demonstrating the presence of integrin ß1 (red) and the cell nucleus stained by DAPI (blue) in both cell lines during VM formation at 2 and 72 h. Scale bar = 100 μm. Panel A &B, representative images from a minimum of three experiments in each cell line. Panel C representative images from two experiments

    Journal: Cell Communication and Signaling : CCS

    Article Title: Extracellular matrix protein signaling promotes multi-step cancer vasculogenic mimicry formation

    doi: 10.1186/s12964-025-02428-0

    Figure Lengend Snippet: Integrin ß1, but not integrin ß3, is required for the formation of VM HEY-A8 GFP ( A ) or MDA-MB-231 ( B ) cells were incubated with a blocking antibody against integrin β1 or integrin β3 before seeding on Matrigel for 96 h. Photographs were taken at 24 and 96 h. Blocking of integrin β1 is enough to stop the formation of VM. ( C ) Airy Scan microscopy demonstrating the presence of integrin ß1 (red) and the cell nucleus stained by DAPI (blue) in both cell lines during VM formation at 2 and 72 h. Scale bar = 100 μm. Panel A &B, representative images from a minimum of three experiments in each cell line. Panel C representative images from two experiments

    Article Snippet: 3-D Culture Matrix Rat Collagen I (3447-020-01) and 3-D Culture Matrix Laminin I (3446-005-01) were purchased from R&D Systems (Minneapolis, MN). siRNA against Integrin β1 (sc-35674), primary antibodies Integrin β1 (P5D2, sc-13590), Cortactin (H-5, sc-55579) and Integrin β3 (2C9.G2, sc-46655) were purchased from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Incubation, Blocking Assay, Microscopy, Staining

    Integrin ß1 is essential for the formation of VM HEY-A8 ( A ) or MDA-MB-231 ( B ) cells were transfected with siScrambled or siRNA against integrin β1 (siIntegrin ß1) before seeding on Matrigel for 96 h. Photographs were taken at 24 and 96 h. Cells that were transfected by siIntegrin β1 do not form VM. ( C )-( E ) Western blot demonstrates that levels of integrin ß1 protein were reduced. * = p < 0.05. Scale bar on panel A = 100 μm. Representative images from a minimum of three experiments in each cell line

    Journal: Cell Communication and Signaling : CCS

    Article Title: Extracellular matrix protein signaling promotes multi-step cancer vasculogenic mimicry formation

    doi: 10.1186/s12964-025-02428-0

    Figure Lengend Snippet: Integrin ß1 is essential for the formation of VM HEY-A8 ( A ) or MDA-MB-231 ( B ) cells were transfected with siScrambled or siRNA against integrin β1 (siIntegrin ß1) before seeding on Matrigel for 96 h. Photographs were taken at 24 and 96 h. Cells that were transfected by siIntegrin β1 do not form VM. ( C )-( E ) Western blot demonstrates that levels of integrin ß1 protein were reduced. * = p < 0.05. Scale bar on panel A = 100 μm. Representative images from a minimum of three experiments in each cell line

    Article Snippet: 3-D Culture Matrix Rat Collagen I (3447-020-01) and 3-D Culture Matrix Laminin I (3446-005-01) were purchased from R&D Systems (Minneapolis, MN). siRNA against Integrin β1 (sc-35674), primary antibodies Integrin β1 (P5D2, sc-13590), Cortactin (H-5, sc-55579) and Integrin β3 (2C9.G2, sc-46655) were purchased from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Transfection, Western Blot

    Integrin β1 is highly expressed and localized on the plasmatic membrane during VM formation A and B Confocal microscopy showing that integrin β1 is localized in the plasmatic membrane of HEY-A8 cells at 2 h of VM formation. ( C ) Quantification of integrin β1 intensity comparing cells grown on denatured Matrigel (control) and cells grown onto Matrigel after 2 h (VM). D HEY-A8 cells were seeded onto Matrigel and fixed at different timepoints. Confocal microscopy shows that integrin β1 is highly localized at 2 h of VM formation but not at 8 and 24 h. E Quantification of integrin β1 intensity comparing different timepoints of VM formation. F 3D reconstruction of z-stacks showing that integrin β1 is localized at the top of the VM tube at 96 h. G Confocal microscopy showing that integrin β1 is more present at the top of the VM tubular structure compared to the bottom and the middle of the tube. For all images integrin β1 (red), F-actin (green) and the cell nucleus stained by DAPI (blue). Representative images from a minimum of three experiments in each cell line. * = p < 0.05

    Journal: Cell Communication and Signaling : CCS

    Article Title: Extracellular matrix protein signaling promotes multi-step cancer vasculogenic mimicry formation

    doi: 10.1186/s12964-025-02428-0

    Figure Lengend Snippet: Integrin β1 is highly expressed and localized on the plasmatic membrane during VM formation A and B Confocal microscopy showing that integrin β1 is localized in the plasmatic membrane of HEY-A8 cells at 2 h of VM formation. ( C ) Quantification of integrin β1 intensity comparing cells grown on denatured Matrigel (control) and cells grown onto Matrigel after 2 h (VM). D HEY-A8 cells were seeded onto Matrigel and fixed at different timepoints. Confocal microscopy shows that integrin β1 is highly localized at 2 h of VM formation but not at 8 and 24 h. E Quantification of integrin β1 intensity comparing different timepoints of VM formation. F 3D reconstruction of z-stacks showing that integrin β1 is localized at the top of the VM tube at 96 h. G Confocal microscopy showing that integrin β1 is more present at the top of the VM tubular structure compared to the bottom and the middle of the tube. For all images integrin β1 (red), F-actin (green) and the cell nucleus stained by DAPI (blue). Representative images from a minimum of three experiments in each cell line. * = p < 0.05

    Article Snippet: 3-D Culture Matrix Rat Collagen I (3447-020-01) and 3-D Culture Matrix Laminin I (3446-005-01) were purchased from R&D Systems (Minneapolis, MN). siRNA against Integrin β1 (sc-35674), primary antibodies Integrin β1 (P5D2, sc-13590), Cortactin (H-5, sc-55579) and Integrin β3 (2C9.G2, sc-46655) were purchased from Santa Cruz Biotechnology (Dallas, TX).

    Techniques: Membrane, Confocal Microscopy, Control, Staining

    Journal: iScience

    Article Title: Mechanical control of the alternative splicing factor PTBP1 regulates extracellular matrix stiffness induced proliferation and cell spreading

    doi: 10.1016/j.isci.2025.112273

    Figure Lengend Snippet:

    Article Snippet: siIntegrin b1 , Santa Cruz , sc-35674.

    Techniques: Recombinant, Selection, Staining, Negative Control, Software

    Exosomes derived from MΦs cultured on different specimen surfaces differently regulate internalization and targeted lysosomal degradation of membrane ITGβ1 of ECs. A) Immunofluorescence staining images of membrane ITGβ1 (omitted cell permeabilization) and quantitative analysis ( n = 8). B) Immunofluorescence staining images of total ITGβ1 and quantitative analysis ( n = 8). C) Western blotting analysis for cellular total ITGβ1 levels after incubated with the exosomes for 6 h (bafilomycin A was used to inhibit lysosomal degradation). D) ELISA test for cellular total ITGβ1 levels after incubated with the exosomes for 6 h ( n = 9). E) Colocalization analysis of ITGβ1 with LAMP1 after incubated with the exosomes for 4 h. Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Journal: Advanced Science

    Article Title: Biomaterial Surface‐Mediated Macrophages Exert Immunomodulatory Roles by Exosomal CCL2‐Induced Membrane Integrin β1 Trafficking in Recipient Cells

    doi: 10.1002/advs.202409809

    Figure Lengend Snippet: Exosomes derived from MΦs cultured on different specimen surfaces differently regulate internalization and targeted lysosomal degradation of membrane ITGβ1 of ECs. A) Immunofluorescence staining images of membrane ITGβ1 (omitted cell permeabilization) and quantitative analysis ( n = 8). B) Immunofluorescence staining images of total ITGβ1 and quantitative analysis ( n = 8). C) Western blotting analysis for cellular total ITGβ1 levels after incubated with the exosomes for 6 h (bafilomycin A was used to inhibit lysosomal degradation). D) ELISA test for cellular total ITGβ1 levels after incubated with the exosomes for 6 h ( n = 9). E) Colocalization analysis of ITGβ1 with LAMP1 after incubated with the exosomes for 4 h. Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Article Snippet: ITGβ1 siRNA duplex (sc‐35674, Santa Cruz Biotechnology, America) and siRNA transfection reagent (sc‐29528, Santa Cruz Biotechnology, America) were used to transfect ECs according to the manufacturer's guidelines.

    Techniques: Derivative Assay, Cell Culture, Membrane, Immunofluorescence, Staining, Western Blot, Incubation, Enzyme-linked Immunosorbent Assay

    Knockdown of ITGβ1 impairs angiogenic capacity of ECs. A) Gene expression of ITGβ1 in normal (Control) and siRNA‐mediated ITGβ1‐knockdown (ITGβ1 KD ) ECs detected by qRT‐PCR after transient transfection for 24 h ( n = 6). B) Protein expression of ITGβ1 analyzed by western blotting after transient transfection for 72 h. C) Cell morphology of normal and ITGβ1 KD ECs after transient transfection for 24, 48, and 72 h. D) Migration behaviors of normal and ITGβ1 KD ECs (optical images and quantitative statistics of cell migration rate) ( n = 6). E) In vitro blood‐vessel formation of normal and ITGβ1 KD ECs (optical images of vascular network and quantitative statistics of vascular network structures) ( n = 5). Data are presented as means ± SD. *** p < 0.001.

    Journal: Advanced Science

    Article Title: Biomaterial Surface‐Mediated Macrophages Exert Immunomodulatory Roles by Exosomal CCL2‐Induced Membrane Integrin β1 Trafficking in Recipient Cells

    doi: 10.1002/advs.202409809

    Figure Lengend Snippet: Knockdown of ITGβ1 impairs angiogenic capacity of ECs. A) Gene expression of ITGβ1 in normal (Control) and siRNA‐mediated ITGβ1‐knockdown (ITGβ1 KD ) ECs detected by qRT‐PCR after transient transfection for 24 h ( n = 6). B) Protein expression of ITGβ1 analyzed by western blotting after transient transfection for 72 h. C) Cell morphology of normal and ITGβ1 KD ECs after transient transfection for 24, 48, and 72 h. D) Migration behaviors of normal and ITGβ1 KD ECs (optical images and quantitative statistics of cell migration rate) ( n = 6). E) In vitro blood‐vessel formation of normal and ITGβ1 KD ECs (optical images of vascular network and quantitative statistics of vascular network structures) ( n = 5). Data are presented as means ± SD. *** p < 0.001.

    Article Snippet: ITGβ1 siRNA duplex (sc‐35674, Santa Cruz Biotechnology, America) and siRNA transfection reagent (sc‐29528, Santa Cruz Biotechnology, America) were used to transfect ECs according to the manufacturer's guidelines.

    Techniques: Knockdown, Gene Expression, Control, Quantitative RT-PCR, Transfection, Expressing, Western Blot, Migration, In Vitro

    Screening of key cytokines on the exosomes involved in the immunomodulation on angiogenesis and osteogenesis. A) Colocalization analysis of ITGβ1 with internalized exosomes in ECs. B) Exosome internalization detection of normal exosomes (N‐Exo) and Proteinase K‐treated exosomes (PKT‐Exo) in ECs (fluorescence images and quantitative analysis of the exosomes taken up by cells) ( n = 9). C) Western blotting analysis for total ITGβ1 levels in ECs mediated by N‐Exo and PKT‐Exo after 6 h of incubation (protein blotting images and quantitative analysis) ( n = 4). D) Cell morphology of ECs mediated by N‐Exo and PKT‐Exo after 6 h of incubation. E) Cytokine array analysis of the exosome suspensions (spot blotting images of cytokines and quantitative analysis) ( n = 4). Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Journal: Advanced Science

    Article Title: Biomaterial Surface‐Mediated Macrophages Exert Immunomodulatory Roles by Exosomal CCL2‐Induced Membrane Integrin β1 Trafficking in Recipient Cells

    doi: 10.1002/advs.202409809

    Figure Lengend Snippet: Screening of key cytokines on the exosomes involved in the immunomodulation on angiogenesis and osteogenesis. A) Colocalization analysis of ITGβ1 with internalized exosomes in ECs. B) Exosome internalization detection of normal exosomes (N‐Exo) and Proteinase K‐treated exosomes (PKT‐Exo) in ECs (fluorescence images and quantitative analysis of the exosomes taken up by cells) ( n = 9). C) Western blotting analysis for total ITGβ1 levels in ECs mediated by N‐Exo and PKT‐Exo after 6 h of incubation (protein blotting images and quantitative analysis) ( n = 4). D) Cell morphology of ECs mediated by N‐Exo and PKT‐Exo after 6 h of incubation. E) Cytokine array analysis of the exosome suspensions (spot blotting images of cytokines and quantitative analysis) ( n = 4). Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Article Snippet: ITGβ1 siRNA duplex (sc‐35674, Santa Cruz Biotechnology, America) and siRNA transfection reagent (sc‐29528, Santa Cruz Biotechnology, America) were used to transfect ECs according to the manufacturer's guidelines.

    Techniques: Fluorescence, Western Blot, Incubation

    Biomaterial surfaces can vary the content of exosomal CCL2 of MΦs to regulate membrane ITGβ1 trafficking and therefore the functions of recipient cells. A–C) Quantitative analysis for levels of the exosome‐bound GM‐CSF, CCL2, and CXCL2 determined by ELISA ( n = 12). D) ELISA test for cellular total ITGβ1 levels of ECs after stimulated with gradient concentrations of GM‐CSF, CCL2, and CXCL2 for 6 h ( n = 9). E) Cell morphology of ECs after stimulated with GM‐CSF, CCL2, and CXCL2 for 6 h. F) Western blotting analysis for total ITGβ1 levels of ECs mediated by exosome/CCR2 binding after incubated with the exosomes for 6 h (protein blotting images and quantitative analysis) ( n = 4). G) Cell morphology mediated by exosome/CCR2 binding after incubated with the exosomes for 6 h. Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Journal: Advanced Science

    Article Title: Biomaterial Surface‐Mediated Macrophages Exert Immunomodulatory Roles by Exosomal CCL2‐Induced Membrane Integrin β1 Trafficking in Recipient Cells

    doi: 10.1002/advs.202409809

    Figure Lengend Snippet: Biomaterial surfaces can vary the content of exosomal CCL2 of MΦs to regulate membrane ITGβ1 trafficking and therefore the functions of recipient cells. A–C) Quantitative analysis for levels of the exosome‐bound GM‐CSF, CCL2, and CXCL2 determined by ELISA ( n = 12). D) ELISA test for cellular total ITGβ1 levels of ECs after stimulated with gradient concentrations of GM‐CSF, CCL2, and CXCL2 for 6 h ( n = 9). E) Cell morphology of ECs after stimulated with GM‐CSF, CCL2, and CXCL2 for 6 h. F) Western blotting analysis for total ITGβ1 levels of ECs mediated by exosome/CCR2 binding after incubated with the exosomes for 6 h (protein blotting images and quantitative analysis) ( n = 4). G) Cell morphology mediated by exosome/CCR2 binding after incubated with the exosomes for 6 h. Data are presented as means ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

    Article Snippet: ITGβ1 siRNA duplex (sc‐35674, Santa Cruz Biotechnology, America) and siRNA transfection reagent (sc‐29528, Santa Cruz Biotechnology, America) were used to transfect ECs according to the manufacturer's guidelines.

    Techniques: Membrane, Enzyme-linked Immunosorbent Assay, Western Blot, Binding Assay, Incubation

    Schematic illustration of the potential mechanisms by which the biomaterial surfaces regulated the compositions of MΦ‐derived exosomes and the exosomes induced differential trafficking of membrane ITGβ1 in recipient cells.

    Journal: Advanced Science

    Article Title: Biomaterial Surface‐Mediated Macrophages Exert Immunomodulatory Roles by Exosomal CCL2‐Induced Membrane Integrin β1 Trafficking in Recipient Cells

    doi: 10.1002/advs.202409809

    Figure Lengend Snippet: Schematic illustration of the potential mechanisms by which the biomaterial surfaces regulated the compositions of MΦ‐derived exosomes and the exosomes induced differential trafficking of membrane ITGβ1 in recipient cells.

    Article Snippet: ITGβ1 siRNA duplex (sc‐35674, Santa Cruz Biotechnology, America) and siRNA transfection reagent (sc‐29528, Santa Cruz Biotechnology, America) were used to transfect ECs according to the manufacturer's guidelines.

    Techniques: Derivative Assay, Membrane