α9β1 Search Results


anti-α9β1 integrin (clone y9a2) blocking antibody  (Chemicom Inc)
90
Chemicom Inc anti-α9β1 integrin (clone y9a2) blocking antibody
Anti α9β1 Integrin (Clone Y9a2) Blocking Antibody, supplied by Chemicom Inc, 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/result/anti-α9β1 integrin (clone y9a2) blocking antibody/product/Chemicom Inc
Average 90 stars, based on 1 article reviews
anti-α9β1 integrin (clone y9a2) blocking antibody - by Bioz Stars, 2026-03
90/100 stars
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goat anti–mouse integrin α9β1  (Absolute Biotech Inc)
90
Absolute Biotech Inc goat anti–mouse integrin α9β1
The EMILIN1 gC1q domain inhibits cell proliferation through the interaction with the α4 and α9 <t>integrin</t> subunit. (A) Proliferation of sarcoma (HT1080 and RD), carcinoma (HeLa and CaCo-2), and immortal keratinocyte (HaCaT) cell lines in the presence or in the absence of 50 µg/ml of soluble gC1q added to the culture medium for 24 h. The percentage of mean values (±SD) of the number of BrdU-positive cells per field of three independent experiments is reported. *, P < 0.05. (B) FACS analysis of α4 and α9 integrin subunit expression levels in HT1080, RD, CaCo-2, HeLa, and HaCaT cells. (C) Cell adhesion of HT1080 and CaCo-2 cells to gC1q. The cells were preincubated with anti–α4 integrin subunit mAb (P1H4), anti–α9 integrin subunit mAb (Y9A2), or anti–β integrin subunit mAb (4B4; final concentration, 10 µg/ml) for 15 min at 37°C and were then allowed to adhere at 37°C for 20 min. Data are expressed as the means ± SD of three independent experiments with six replicates. *, P < 0.05; **, P < 0.001. (D–F) Proliferation inhibition of HT1080, CaCo-2, and HaCaT cells expressed as the percentage versus the respective control (ctrl). The gC1q domain was used at a concentration of 5 µg/ml; the monoclonal antibody anti-gC1q (1H2) and the function blocking monoclonal antibodies anti–α4 integrin subunit (P1H4) and anti–α9 integrin subunit (Y9A2) were used at 10 µg/ml. Data are expressed as the means ± SD of three independent experiments. *, P < 0.05; **, P < 0.001. (G) Effect of gC1q and the mutants E933A, G945A, and the deleted form on CaCo-2 cell proliferation monitored using the XCELLigence system. The cell index after 48 h of dynamic monitoring calculated as the mean ± SD from n = 3 experiments with n = 6 replicates is reported. *, P < 0.001. (H) Representative immunofluorescence images of skin cryostat sections of 7-wk-old WT mice stained for EMILIN1 and for the α9 integrin subunit. Bars, 25 µm.
Goat Anti–Mouse Integrin α9β1, supplied by Absolute Biotech Inc, 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/result/goat anti–mouse integrin α9β1/product/Absolute Biotech Inc
Average 90 stars, based on 1 article reviews
goat anti–mouse integrin α9β1 - by Bioz Stars, 2026-03
90/100 stars
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integrin α9β1  (McLane Research Laboratories)
90
McLane Research Laboratories integrin α9β1
The EMILIN1 gC1q domain inhibits cell proliferation through the interaction with the α4 and α9 <t>integrin</t> subunit. (A) Proliferation of sarcoma (HT1080 and RD), carcinoma (HeLa and CaCo-2), and immortal keratinocyte (HaCaT) cell lines in the presence or in the absence of 50 µg/ml of soluble gC1q added to the culture medium for 24 h. The percentage of mean values (±SD) of the number of BrdU-positive cells per field of three independent experiments is reported. *, P < 0.05. (B) FACS analysis of α4 and α9 integrin subunit expression levels in HT1080, RD, CaCo-2, HeLa, and HaCaT cells. (C) Cell adhesion of HT1080 and CaCo-2 cells to gC1q. The cells were preincubated with anti–α4 integrin subunit mAb (P1H4), anti–α9 integrin subunit mAb (Y9A2), or anti–β integrin subunit mAb (4B4; final concentration, 10 µg/ml) for 15 min at 37°C and were then allowed to adhere at 37°C for 20 min. Data are expressed as the means ± SD of three independent experiments with six replicates. *, P < 0.05; **, P < 0.001. (D–F) Proliferation inhibition of HT1080, CaCo-2, and HaCaT cells expressed as the percentage versus the respective control (ctrl). The gC1q domain was used at a concentration of 5 µg/ml; the monoclonal antibody anti-gC1q (1H2) and the function blocking monoclonal antibodies anti–α4 integrin subunit (P1H4) and anti–α9 integrin subunit (Y9A2) were used at 10 µg/ml. Data are expressed as the means ± SD of three independent experiments. *, P < 0.05; **, P < 0.001. (G) Effect of gC1q and the mutants E933A, G945A, and the deleted form on CaCo-2 cell proliferation monitored using the XCELLigence system. The cell index after 48 h of dynamic monitoring calculated as the mean ± SD from n = 3 experiments with n = 6 replicates is reported. *, P < 0.001. (H) Representative immunofluorescence images of skin cryostat sections of 7-wk-old WT mice stained for EMILIN1 and for the α9 integrin subunit. Bars, 25 µm.
Integrin α9β1, supplied by McLane Research Laboratories, 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/result/integrin α9β1/product/McLane Research Laboratories
Average 90 stars, based on 1 article reviews
integrin α9β1 - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


The EMILIN1 gC1q domain inhibits cell proliferation through the interaction with the α4 and α9 integrin subunit. (A) Proliferation of sarcoma (HT1080 and RD), carcinoma (HeLa and CaCo-2), and immortal keratinocyte (HaCaT) cell lines in the presence or in the absence of 50 µg/ml of soluble gC1q added to the culture medium for 24 h. The percentage of mean values (±SD) of the number of BrdU-positive cells per field of three independent experiments is reported. *, P < 0.05. (B) FACS analysis of α4 and α9 integrin subunit expression levels in HT1080, RD, CaCo-2, HeLa, and HaCaT cells. (C) Cell adhesion of HT1080 and CaCo-2 cells to gC1q. The cells were preincubated with anti–α4 integrin subunit mAb (P1H4), anti–α9 integrin subunit mAb (Y9A2), or anti–β integrin subunit mAb (4B4; final concentration, 10 µg/ml) for 15 min at 37°C and were then allowed to adhere at 37°C for 20 min. Data are expressed as the means ± SD of three independent experiments with six replicates. *, P < 0.05; **, P < 0.001. (D–F) Proliferation inhibition of HT1080, CaCo-2, and HaCaT cells expressed as the percentage versus the respective control (ctrl). The gC1q domain was used at a concentration of 5 µg/ml; the monoclonal antibody anti-gC1q (1H2) and the function blocking monoclonal antibodies anti–α4 integrin subunit (P1H4) and anti–α9 integrin subunit (Y9A2) were used at 10 µg/ml. Data are expressed as the means ± SD of three independent experiments. *, P < 0.05; **, P < 0.001. (G) Effect of gC1q and the mutants E933A, G945A, and the deleted form on CaCo-2 cell proliferation monitored using the XCELLigence system. The cell index after 48 h of dynamic monitoring calculated as the mean ± SD from n = 3 experiments with n = 6 replicates is reported. *, P < 0.001. (H) Representative immunofluorescence images of skin cryostat sections of 7-wk-old WT mice stained for EMILIN1 and for the α9 integrin subunit. Bars, 25 µm.

Journal: The Journal of Cell Biology

Article Title: EMILIN1–α4/α9 integrin interaction inhibits dermal fibroblast and keratinocyte proliferation

doi: 10.1083/jcb.201008013

Figure Lengend Snippet: The EMILIN1 gC1q domain inhibits cell proliferation through the interaction with the α4 and α9 integrin subunit. (A) Proliferation of sarcoma (HT1080 and RD), carcinoma (HeLa and CaCo-2), and immortal keratinocyte (HaCaT) cell lines in the presence or in the absence of 50 µg/ml of soluble gC1q added to the culture medium for 24 h. The percentage of mean values (±SD) of the number of BrdU-positive cells per field of three independent experiments is reported. *, P < 0.05. (B) FACS analysis of α4 and α9 integrin subunit expression levels in HT1080, RD, CaCo-2, HeLa, and HaCaT cells. (C) Cell adhesion of HT1080 and CaCo-2 cells to gC1q. The cells were preincubated with anti–α4 integrin subunit mAb (P1H4), anti–α9 integrin subunit mAb (Y9A2), or anti–β integrin subunit mAb (4B4; final concentration, 10 µg/ml) for 15 min at 37°C and were then allowed to adhere at 37°C for 20 min. Data are expressed as the means ± SD of three independent experiments with six replicates. *, P < 0.05; **, P < 0.001. (D–F) Proliferation inhibition of HT1080, CaCo-2, and HaCaT cells expressed as the percentage versus the respective control (ctrl). The gC1q domain was used at a concentration of 5 µg/ml; the monoclonal antibody anti-gC1q (1H2) and the function blocking monoclonal antibodies anti–α4 integrin subunit (P1H4) and anti–α9 integrin subunit (Y9A2) were used at 10 µg/ml. Data are expressed as the means ± SD of three independent experiments. *, P < 0.05; **, P < 0.001. (G) Effect of gC1q and the mutants E933A, G945A, and the deleted form on CaCo-2 cell proliferation monitored using the XCELLigence system. The cell index after 48 h of dynamic monitoring calculated as the mean ± SD from n = 3 experiments with n = 6 replicates is reported. *, P < 0.001. (H) Representative immunofluorescence images of skin cryostat sections of 7-wk-old WT mice stained for EMILIN1 and for the α9 integrin subunit. Bars, 25 µm.

Article Snippet: Moreover, mouse anti-CdK2 (BD), mouse anti–Cyclin D1/2 (Millipore), rabbit anti–mature TGF-β1 (BioVision Research Products), rabbit anti–pan-CK antibody (Dako), mouse anti–integrin α9β1 (clone Y9A2) and anti–integrin α4 (clone P1H4; Millipore), goat anti–mouse integrin α9β1 (LifeSpan BioSciences), and mouse anti–β1 integrin subunit (clone 4B4; Beckman Coulter) antibodies were used.

Techniques: Expressing, Concentration Assay, Inhibition, Blocking Assay, Immunofluorescence, Staining

Proposed model for the regulatory role of EMILIN1 in skin homeostasis. The illustration summarizes the proposed molecular mechanism underlying the regulatory role of EMILIN1 in skin proliferation. (A) TGF-β triggers cytostatic signal pathways mainly through pSmad2 (Ser465/467) activation and modulates PI3K/Akt signaling by regulating PTEN expression. showed that EMILIN1 inhibits TGF-β processing by binding specifically to the pro–TGF-β precursor and by preventing its maturation in the extracellular space. Here, we demonstrated that EMILIN1 binding to dermal fibroblast and basal keratinocytes α4β1/α9β1 integrins empowers the down-regulation of proliferative cues induced by TGF-β. This effect is mediated by α4/α9β1-dependent PTEN activation and inhibition of pErk1/2 proproliferative activity. (B) The increased levels of mature TGF-β and the lack of α4/α9β1 integrin–specific engagement by the lack of EMILIN1 result in PTEN down-regulation and, hence, reduced activity. This determines the activation of proliferative pathways such as pAkt and pErk1/2 that in turn lead to a reduction of TGF-β signaling via increased Erk1/2-dependent phosphorylation of Smad2 at inhibitory Ser245/250/255. In conclusion, we provide the first evidence for the central role of PTEN in the cross talk between α4/α9β1 integrin and TGF-β signal pathways.

Journal: The Journal of Cell Biology

Article Title: EMILIN1–α4/α9 integrin interaction inhibits dermal fibroblast and keratinocyte proliferation

doi: 10.1083/jcb.201008013

Figure Lengend Snippet: Proposed model for the regulatory role of EMILIN1 in skin homeostasis. The illustration summarizes the proposed molecular mechanism underlying the regulatory role of EMILIN1 in skin proliferation. (A) TGF-β triggers cytostatic signal pathways mainly through pSmad2 (Ser465/467) activation and modulates PI3K/Akt signaling by regulating PTEN expression. showed that EMILIN1 inhibits TGF-β processing by binding specifically to the pro–TGF-β precursor and by preventing its maturation in the extracellular space. Here, we demonstrated that EMILIN1 binding to dermal fibroblast and basal keratinocytes α4β1/α9β1 integrins empowers the down-regulation of proliferative cues induced by TGF-β. This effect is mediated by α4/α9β1-dependent PTEN activation and inhibition of pErk1/2 proproliferative activity. (B) The increased levels of mature TGF-β and the lack of α4/α9β1 integrin–specific engagement by the lack of EMILIN1 result in PTEN down-regulation and, hence, reduced activity. This determines the activation of proliferative pathways such as pAkt and pErk1/2 that in turn lead to a reduction of TGF-β signaling via increased Erk1/2-dependent phosphorylation of Smad2 at inhibitory Ser245/250/255. In conclusion, we provide the first evidence for the central role of PTEN in the cross talk between α4/α9β1 integrin and TGF-β signal pathways.

Article Snippet: Moreover, mouse anti-CdK2 (BD), mouse anti–Cyclin D1/2 (Millipore), rabbit anti–mature TGF-β1 (BioVision Research Products), rabbit anti–pan-CK antibody (Dako), mouse anti–integrin α9β1 (clone Y9A2) and anti–integrin α4 (clone P1H4; Millipore), goat anti–mouse integrin α9β1 (LifeSpan BioSciences), and mouse anti–β1 integrin subunit (clone 4B4; Beckman Coulter) antibodies were used.

Techniques: Activation Assay, Expressing, Binding Assay, Inhibition, Activity Assay