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sc 29373 itgb4 sirna human santa cruz biotechnology  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology sc 29373 itgb4 sirna human santa cruz biotechnology
    Sc 29373 Itgb4 Sirna Human Santa Cruz Biotechnology, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sc+29373/Integrin+%CE%B1V+siRNA/pm41702399-284-44-48
    Average 93 stars, based on 17 article reviews
    sc 29373 itgb4 sirna human santa cruz biotechnology - by Bioz Stars, 2026-09
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    Article Title: Cas phosphorylation regulates focal adhesion assembly
    Article Snippet: siITGAV , Santa Cruz, Cat: sc-29373 , sc-29373A: GCAUCUAUCUUGAAAGUAATT sc-29373B: CUGGUUUGAACGAUAGAAATT sc-29373C: GAAGCUGUGUAGUAUAUCATT.



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    (A) Western blot showing that endothelial cell gC1qR binds to C . glabrata coated with fresh serum. Results are representative of 3 independent experiments. (B-E) Effects of inhibiting gC1qR function with <t>siRNA</t> knockdown (B and C) and specific monoclonal antibodies (D and E) on the endocytosis (B and D) and cell-association (C and E) of C . glabrata coated with fresh serum. Antibody 74.5.2 recognizes the high molecular weight kininogen binding site in the C-terminus of the gC1qR and antibody 60.11 is directed against the C1q binding site in the N-terminus of the gC1qR. Results shown in (B-E) are the mean ± SD of 3 experiments each performed in triplicate. Heat inact., heat inactivated serum; orgs/HPF, organisms per high-power field; ns, not significant, * P < 0.05, ** P < 0.01 by Student’s t-test (B and C) or ANOVA with the Dunnett’s test for multiple comparisons (D and E).
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    Figure 2. Apelin enhances integrin αvβ3-dependent prostate cancer motility. (A) Cells were treated with apelin for 24 hours, the indicated integrin expression was examined by qPCR (n=3). (B&C) Cells were treated with integrin αvβ3 or α5β1 antibody then with apelin, the wound healing and cell migration was examined (n=3). (D) Integrin αv and β3 gene levels in normal and prostate cancer patients retrieved from the GEO database. (E&F) Representative images showing the results of IHC staining for integrin αvβ3 in tissue samples from healthy individuals (n=3) and prostate cancer patients (n=3). (G&H) Cells were co-transfected with integrin αv and β3 siRNA then with apelin, the wound healing and cell migration was examined (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Journal: International Journal of Biological Sciences

    Article Title: Apelin facilitates integrin αvβ3 production and enhances metastasis in prostate cancer by activating STAT3 and inhibiting miR-8070

    doi: 10.7150/ijbs.113161

    Figure Lengend Snippet: Figure 2. Apelin enhances integrin αvβ3-dependent prostate cancer motility. (A) Cells were treated with apelin for 24 hours, the indicated integrin expression was examined by qPCR (n=3). (B&C) Cells were treated with integrin αvβ3 or α5β1 antibody then with apelin, the wound healing and cell migration was examined (n=3). (D) Integrin αv and β3 gene levels in normal and prostate cancer patients retrieved from the GEO database. (E&F) Representative images showing the results of IHC staining for integrin αvβ3 in tissue samples from healthy individuals (n=3) and prostate cancer patients (n=3). (G&H) Cells were co-transfected with integrin αv and β3 siRNA then with apelin, the wound healing and cell migration was examined (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Article Snippet: JNK (SC-474), p38 (SC-4972), ERK (SC-1647), STAT3 (SC-482), p-JNK (SC-6254), p-p38 (SC-166182), p-ERK (SC-7383) and integrin αvβ3 (SC-7312) antibodies as well as JNK (sc-29380), p38 (sc-29433), STAT3 (sc-29493), integrin αv (sc-29373), integrin β3 (sc-29375) and apelin (sc-44741) siRNA were purchased from Santa Cruz Biotechnology (CA, USA).

    Techniques: Expressing, Migration, Immunohistochemistry, Transfection, Control

    Figure 3. MAPK pathway is regulated apelin-induced integrin expression and prostate cancer migration. (A&B) IPA pathway enrichment figure showing pathways that were changed in the GSE7930 dataset (Orange color indicated upregulated gene profile; blue color indicated downregulated gene profile). (C-H) Cells were treated with ERK (ERK II inhibitor; 10 μM), p38 (SB203580; 10 μM) and JNK (SP600125; 10 μM) inhibitors or transfected with ERK, p38 and JNK siRNA for 24 hours then with apelin, the wound healing, cell migration and integrin mRNA expression was examined (n=3). (I) PC3 cells were stimulated with apelin and ERK, p38 and JNK phosphorylation was examined by Western blotting (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Journal: International Journal of Biological Sciences

    Article Title: Apelin facilitates integrin αvβ3 production and enhances metastasis in prostate cancer by activating STAT3 and inhibiting miR-8070

    doi: 10.7150/ijbs.113161

    Figure Lengend Snippet: Figure 3. MAPK pathway is regulated apelin-induced integrin expression and prostate cancer migration. (A&B) IPA pathway enrichment figure showing pathways that were changed in the GSE7930 dataset (Orange color indicated upregulated gene profile; blue color indicated downregulated gene profile). (C-H) Cells were treated with ERK (ERK II inhibitor; 10 μM), p38 (SB203580; 10 μM) and JNK (SP600125; 10 μM) inhibitors or transfected with ERK, p38 and JNK siRNA for 24 hours then with apelin, the wound healing, cell migration and integrin mRNA expression was examined (n=3). (I) PC3 cells were stimulated with apelin and ERK, p38 and JNK phosphorylation was examined by Western blotting (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Article Snippet: JNK (SC-474), p38 (SC-4972), ERK (SC-1647), STAT3 (SC-482), p-JNK (SC-6254), p-p38 (SC-166182), p-ERK (SC-7383) and integrin αvβ3 (SC-7312) antibodies as well as JNK (sc-29380), p38 (sc-29433), STAT3 (sc-29493), integrin αv (sc-29373), integrin β3 (sc-29375) and apelin (sc-44741) siRNA were purchased from Santa Cruz Biotechnology (CA, USA).

    Techniques: Expressing, Migration, Transfection, Phospho-proteomics, Western Blot, Control

    Figure 4. Apelin promotes integrin production and cell motility via the STAT3 pathway. (A-F) Cells were treated with STAT3 inhibitor (10 μM) or transfected with STAT3 siRNA for 24 hours then with apelin, the wound healing, cell migration and integrin mRNA expression was examined (n=3). (G&H) PC3 cells were treated with apelin or pretreated with ERK, p38 and JNK inhibitor then with apelin, the STAT3 phosphorylation was examined by Western blotting (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Journal: International Journal of Biological Sciences

    Article Title: Apelin facilitates integrin αvβ3 production and enhances metastasis in prostate cancer by activating STAT3 and inhibiting miR-8070

    doi: 10.7150/ijbs.113161

    Figure Lengend Snippet: Figure 4. Apelin promotes integrin production and cell motility via the STAT3 pathway. (A-F) Cells were treated with STAT3 inhibitor (10 μM) or transfected with STAT3 siRNA for 24 hours then with apelin, the wound healing, cell migration and integrin mRNA expression was examined (n=3). (G&H) PC3 cells were treated with apelin or pretreated with ERK, p38 and JNK inhibitor then with apelin, the STAT3 phosphorylation was examined by Western blotting (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Article Snippet: JNK (SC-474), p38 (SC-4972), ERK (SC-1647), STAT3 (SC-482), p-JNK (SC-6254), p-p38 (SC-166182), p-ERK (SC-7383) and integrin αvβ3 (SC-7312) antibodies as well as JNK (sc-29380), p38 (sc-29433), STAT3 (sc-29493), integrin αv (sc-29373), integrin β3 (sc-29375) and apelin (sc-44741) siRNA were purchased from Santa Cruz Biotechnology (CA, USA).

    Techniques: Transfection, Migration, Expressing, Phospho-proteomics, Western Blot, Control

    Figure 5. Apelin enhances integrin expression and promotes cell migration by inhibiting miR-8070 expression. (A) The diagrams depict the selection of miRNA candidates targeting integrin αv and β3. (B) PC3 cells were treated with apelin, the miRNAs expression was examined by qPCR (n=3). (C) Cells were treated with apelin for 24 hours, the miR-8070 expression was examined by qPCR (n=3). (D-F) Cells were transfected with miR-8070 mimic for 24 hours then with apelin, the wound healing, cell migration and integrin mRNA expression was examined (n=3). (G-I) Cells were treated with ERK, p38 and JNK inhibitor or siRNA then with apelin, the 3’UTR activity and miRNA expression was examined by luciferase activity and qPCR (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Journal: International Journal of Biological Sciences

    Article Title: Apelin facilitates integrin αvβ3 production and enhances metastasis in prostate cancer by activating STAT3 and inhibiting miR-8070

    doi: 10.7150/ijbs.113161

    Figure Lengend Snippet: Figure 5. Apelin enhances integrin expression and promotes cell migration by inhibiting miR-8070 expression. (A) The diagrams depict the selection of miRNA candidates targeting integrin αv and β3. (B) PC3 cells were treated with apelin, the miRNAs expression was examined by qPCR (n=3). (C) Cells were treated with apelin for 24 hours, the miR-8070 expression was examined by qPCR (n=3). (D-F) Cells were transfected with miR-8070 mimic for 24 hours then with apelin, the wound healing, cell migration and integrin mRNA expression was examined (n=3). (G-I) Cells were treated with ERK, p38 and JNK inhibitor or siRNA then with apelin, the 3’UTR activity and miRNA expression was examined by luciferase activity and qPCR (n=3). * p < 0.05 compared with the control group. # p < 0.05 compared with the apelin-treated group.

    Article Snippet: JNK (SC-474), p38 (SC-4972), ERK (SC-1647), STAT3 (SC-482), p-JNK (SC-6254), p-p38 (SC-166182), p-ERK (SC-7383) and integrin αvβ3 (SC-7312) antibodies as well as JNK (sc-29380), p38 (sc-29433), STAT3 (sc-29493), integrin αv (sc-29373), integrin β3 (sc-29375) and apelin (sc-44741) siRNA were purchased from Santa Cruz Biotechnology (CA, USA).

    Techniques: Expressing, Migration, Selection, Transfection, Activity Assay, Luciferase, Control

    Figure 6. Apelin blockade inhibits prostate cancer metastasis in vivo. (A-C) Cells were transfected with apelin siRNA, the integrin expression, wound healing and cell migration was examined (n=3). (D&E) IHC analysis of prostate cancer tissue samples stained with integrin αvβ3 antibody (n=3). (F) IHC analysis of leg bone (n=3), liver (n=3), and lung (n=3) sections stained with apelin and integrin αvβ3 antibodies. * p < 0.05 compared with the control group.

    Journal: International Journal of Biological Sciences

    Article Title: Apelin facilitates integrin αvβ3 production and enhances metastasis in prostate cancer by activating STAT3 and inhibiting miR-8070

    doi: 10.7150/ijbs.113161

    Figure Lengend Snippet: Figure 6. Apelin blockade inhibits prostate cancer metastasis in vivo. (A-C) Cells were transfected with apelin siRNA, the integrin expression, wound healing and cell migration was examined (n=3). (D&E) IHC analysis of prostate cancer tissue samples stained with integrin αvβ3 antibody (n=3). (F) IHC analysis of leg bone (n=3), liver (n=3), and lung (n=3) sections stained with apelin and integrin αvβ3 antibodies. * p < 0.05 compared with the control group.

    Article Snippet: JNK (SC-474), p38 (SC-4972), ERK (SC-1647), STAT3 (SC-482), p-JNK (SC-6254), p-p38 (SC-166182), p-ERK (SC-7383) and integrin αvβ3 (SC-7312) antibodies as well as JNK (sc-29380), p38 (sc-29433), STAT3 (sc-29493), integrin αv (sc-29373), integrin β3 (sc-29375) and apelin (sc-44741) siRNA were purchased from Santa Cruz Biotechnology (CA, USA).

    Techniques: In Vivo, Transfection, Expressing, Migration, Staining, Control

    Figure 7. Schematic diagram illustrating the mechanism underlying the effects of apelin in prostate cancer metastasis. Apelin stimulation enhances integrin αvβ3-dependent prostate cancer migration and metastasis. The activation of STAT3 and inhibition of miR-8070 via the ERK, p38 and JNK pathways mediate apelin-facilitated integrin synthesis and cell motility.

    Journal: International Journal of Biological Sciences

    Article Title: Apelin facilitates integrin αvβ3 production and enhances metastasis in prostate cancer by activating STAT3 and inhibiting miR-8070

    doi: 10.7150/ijbs.113161

    Figure Lengend Snippet: Figure 7. Schematic diagram illustrating the mechanism underlying the effects of apelin in prostate cancer metastasis. Apelin stimulation enhances integrin αvβ3-dependent prostate cancer migration and metastasis. The activation of STAT3 and inhibition of miR-8070 via the ERK, p38 and JNK pathways mediate apelin-facilitated integrin synthesis and cell motility.

    Article Snippet: JNK (SC-474), p38 (SC-4972), ERK (SC-1647), STAT3 (SC-482), p-JNK (SC-6254), p-p38 (SC-166182), p-ERK (SC-7383) and integrin αvβ3 (SC-7312) antibodies as well as JNK (sc-29380), p38 (sc-29433), STAT3 (sc-29493), integrin αv (sc-29373), integrin β3 (sc-29375) and apelin (sc-44741) siRNA were purchased from Santa Cruz Biotechnology (CA, USA).

    Techniques: Migration, Activation Assay, Inhibition

    RGDmix hydrogel enhances the secretion function of hAMSCs through the integrin αv/PI3K/AKT axis. (A) qRT-PCR confirmed the knockdown of integrin αv. (B) ELISA experiments showed that silencing integrin αv significantly reduces the expression levels of growth factors VEGF and TGF-β in hAMSCs encapsulated in RGDmix hydrogel. (C) CCK-8 assay demonstrated that knockdown of integrin αv does not affect the proliferation of hAMSCs. (D) Representative photo images, (E) wound healing rates, and (F) Hematoxylin and eosin stained images of excisional wounds treated with different treatments. The inner diameters of the rubber rings were 8 mm. The blackarrow heads mark the edges of the original excision sites. (G) Quantification of epidermal thickness and the number of hair follicles (n = 5). (H) Expression levels of growth factors VEGF and TGF-β in hAMSCs encapsulated in RGDmix hydrogel when the PI3K/AKT pathway was inhibited by LY294002 (n = 3). Significance levels were set at: * P < 0.05, ** P < 0.01, *** P < 0.001 vs. control.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: RGDSP-functionalized peptide hydrogel stimulates growth factor secretion via integrin αv/PI3K/AKT axis for improved wound healing by human amniotic mesenchymal stem cells

    doi: 10.3389/fbioe.2024.1385931

    Figure Lengend Snippet: RGDmix hydrogel enhances the secretion function of hAMSCs through the integrin αv/PI3K/AKT axis. (A) qRT-PCR confirmed the knockdown of integrin αv. (B) ELISA experiments showed that silencing integrin αv significantly reduces the expression levels of growth factors VEGF and TGF-β in hAMSCs encapsulated in RGDmix hydrogel. (C) CCK-8 assay demonstrated that knockdown of integrin αv does not affect the proliferation of hAMSCs. (D) Representative photo images, (E) wound healing rates, and (F) Hematoxylin and eosin stained images of excisional wounds treated with different treatments. The inner diameters of the rubber rings were 8 mm. The blackarrow heads mark the edges of the original excision sites. (G) Quantification of epidermal thickness and the number of hair follicles (n = 5). (H) Expression levels of growth factors VEGF and TGF-β in hAMSCs encapsulated in RGDmix hydrogel when the PI3K/AKT pathway was inhibited by LY294002 (n = 3). Significance levels were set at: * P < 0.05, ** P < 0.01, *** P < 0.001 vs. control.

    Article Snippet: A total of forty picomoles of synthetic small interfering RNAs (siRNAs) were transfected into human amniotic mesenchymal stem cells (hAMSCs) in 24-well plates, targeting either the human integrin subtype αv (sc-29373, Santa Cruz) or a scrambled siRNA (sc-37007, Santa Cruz), following the manufacturer’s instructions.

    Techniques: Quantitative RT-PCR, Knockdown, Enzyme-linked Immunosorbent Assay, Expressing, CCK-8 Assay, Staining, Control

    Journal: eLife

    Article Title: Cas phosphorylation regulates focal adhesion assembly

    doi: 10.7554/eLife.90234

    Figure Lengend Snippet:

    Article Snippet: siITGAV , Santa Cruz, Cat: sc-29373 , sc-29373A: GCAUCUAUCUUGAAAGUAATT sc-29373B: CUGGUUUGAACGAUAGAAATT sc-29373C: GAAGCUGUGUAGUAUAUCATT.

    Techniques: Negative Control

    Journal: eLife

    Article Title: Cas phosphorylation regulates focal adhesion assembly

    doi: 10.7554/eLife.90234

    Figure Lengend Snippet:

    Article Snippet: siITGAV , Santa Cruz, Cat: sc-29373 , sc-29373A: GCAUCUAUCUUGAAAGUAATT sc-29373B: CUGGUUUGAACGAUAGAAATT sc-29373C: GAAGCUGUGUAGUAUAUCATT.

    Techniques: Negative Control

    (A) Western blot showing that endothelial cell gC1qR binds to C . glabrata coated with fresh serum. Results are representative of 3 independent experiments. (B-E) Effects of inhibiting gC1qR function with siRNA knockdown (B and C) and specific monoclonal antibodies (D and E) on the endocytosis (B and D) and cell-association (C and E) of C . glabrata coated with fresh serum. Antibody 74.5.2 recognizes the high molecular weight kininogen binding site in the C-terminus of the gC1qR and antibody 60.11 is directed against the C1q binding site in the N-terminus of the gC1qR. Results shown in (B-E) are the mean ± SD of 3 experiments each performed in triplicate. Heat inact., heat inactivated serum; orgs/HPF, organisms per high-power field; ns, not significant, * P < 0.05, ** P < 0.01 by Student’s t-test (B and C) or ANOVA with the Dunnett’s test for multiple comparisons (D and E).

    Journal: PLoS Pathogens

    Article Title: Serum bridging molecules drive candidal invasion of human but not mouse endothelial cells

    doi: 10.1371/journal.ppat.1010681

    Figure Lengend Snippet: (A) Western blot showing that endothelial cell gC1qR binds to C . glabrata coated with fresh serum. Results are representative of 3 independent experiments. (B-E) Effects of inhibiting gC1qR function with siRNA knockdown (B and C) and specific monoclonal antibodies (D and E) on the endocytosis (B and D) and cell-association (C and E) of C . glabrata coated with fresh serum. Antibody 74.5.2 recognizes the high molecular weight kininogen binding site in the C-terminus of the gC1qR and antibody 60.11 is directed against the C1q binding site in the N-terminus of the gC1qR. Results shown in (B-E) are the mean ± SD of 3 experiments each performed in triplicate. Heat inact., heat inactivated serum; orgs/HPF, organisms per high-power field; ns, not significant, * P < 0.05, ** P < 0.01 by Student’s t-test (B and C) or ANOVA with the Dunnett’s test for multiple comparisons (D and E).

    Article Snippet: The endothelial cells were transfected with gC1qR siRNA (Santa Cruz Biotechnology, Cat. # sc-42880), integrin α5 siRNA (Santa Cruz Biotechnology, Cat. # sc-29372), integrin αv siRNA (Santa Cruz Biotechnology, Cat. # sc-29373), or scrambled control siRNA (Qiagen, Cat. # 1027281) using Lipofectamine 2000 (Thermo Fisher Scientific) following the manufacturer’s instructions.

    Techniques: Western Blot, Knockdown, Bioprocessing, High Molecular Weight, Binding Assay

    (A-F) Effects of inhibiting αv integrin function with siRNA knockdown (A and B or)specific monoclonal antibodies (C-F) and on the endocytosis (A, C, D) and cell-association (B, E, F) of serum-coated C . glabrata . (G and H) Inhibition of gC1qR (with monoclonal antibody 74.5.2) and αv integrins has an additive effect on decreasing the endocytosis (G) but not cell-association of serum-coated C . glabrata (H). Results are the mean ± SD of 3 experiments, each performed in triplicate. Orgs/HPF, organisms per high power field; ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by ANOVA with the Dunnett’s test for multiple comparisons (A, B, G, H) or the Student’s t-test (C-F).

    Journal: PLoS Pathogens

    Article Title: Serum bridging molecules drive candidal invasion of human but not mouse endothelial cells

    doi: 10.1371/journal.ppat.1010681

    Figure Lengend Snippet: (A-F) Effects of inhibiting αv integrin function with siRNA knockdown (A and B or)specific monoclonal antibodies (C-F) and on the endocytosis (A, C, D) and cell-association (B, E, F) of serum-coated C . glabrata . (G and H) Inhibition of gC1qR (with monoclonal antibody 74.5.2) and αv integrins has an additive effect on decreasing the endocytosis (G) but not cell-association of serum-coated C . glabrata (H). Results are the mean ± SD of 3 experiments, each performed in triplicate. Orgs/HPF, organisms per high power field; ns, not significant; * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by ANOVA with the Dunnett’s test for multiple comparisons (A, B, G, H) or the Student’s t-test (C-F).

    Article Snippet: The endothelial cells were transfected with gC1qR siRNA (Santa Cruz Biotechnology, Cat. # sc-42880), integrin α5 siRNA (Santa Cruz Biotechnology, Cat. # sc-29372), integrin αv siRNA (Santa Cruz Biotechnology, Cat. # sc-29373), or scrambled control siRNA (Qiagen, Cat. # 1027281) using Lipofectamine 2000 (Thermo Fisher Scientific) following the manufacturer’s instructions.

    Techniques: Knockdown, Bioprocessing, Inhibition

    (A and B) Endocytosis of C . glabrata coated with either human or mouse serum by the indicated endothelial cells after 45 min (A) and 180 min (B). (C) Endocytosis of C . glabrata coated with fresh human serum by mouse liver endothelial cells expressing human gC1qR, integrin αv, or integrin β5. Data are the mean ± SD of 3 experiments each performed in triplicate. HUVEC, human umbilical vein endothelial cell; orgs/HPF, organisms per high power field; ns, not significant; ** P < 0.01, **** P < 0.0001. *** P < 0.001, **** P < 0.0001 by ANOVA with the Dunnett’s test for multiple comparisons.

    Journal: PLoS Pathogens

    Article Title: Serum bridging molecules drive candidal invasion of human but not mouse endothelial cells

    doi: 10.1371/journal.ppat.1010681

    Figure Lengend Snippet: (A and B) Endocytosis of C . glabrata coated with either human or mouse serum by the indicated endothelial cells after 45 min (A) and 180 min (B). (C) Endocytosis of C . glabrata coated with fresh human serum by mouse liver endothelial cells expressing human gC1qR, integrin αv, or integrin β5. Data are the mean ± SD of 3 experiments each performed in triplicate. HUVEC, human umbilical vein endothelial cell; orgs/HPF, organisms per high power field; ns, not significant; ** P < 0.01, **** P < 0.0001. *** P < 0.001, **** P < 0.0001 by ANOVA with the Dunnett’s test for multiple comparisons.

    Article Snippet: The endothelial cells were transfected with gC1qR siRNA (Santa Cruz Biotechnology, Cat. # sc-42880), integrin α5 siRNA (Santa Cruz Biotechnology, Cat. # sc-29372), integrin αv siRNA (Santa Cruz Biotechnology, Cat. # sc-29373), or scrambled control siRNA (Qiagen, Cat. # 1027281) using Lipofectamine 2000 (Thermo Fisher Scientific) following the manufacturer’s instructions.

    Techniques: Expressing