rat anti β1 integrin function Search Results


93
Alomone Labs polyclonal antibodies
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Becton Dickinson rat anti-β1 integrin
A: Proliferation assay in β3 <t>integrin−/−</t> endothelial cells. MLEC were isolated from wild-type (β3+/+) and β3 integrin−/− (β3−/−) mice as previously described (Maeshima et al., 2002). Proliferation was assessed by [3H]-thymidine incorporation. All groups represent triplicate analyses. The results are shown as the mean ± SEM. ** indicates p < 0.01; compared to control cells.
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Santa Cruz Biotechnology rat anti integrin β1
A: Proliferation assay in β3 <t>integrin−/−</t> endothelial cells. MLEC were isolated from wild-type (β3+/+) and β3 integrin−/− (β3−/−) mice as previously described (Maeshima et al., 2002). Proliferation was assessed by [3H]-thymidine incorporation. All groups represent triplicate analyses. The results are shown as the mean ± SEM. ** indicates p < 0.01; compared to control cells.
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Santa Cruz Biotechnology polyclonal rabbit anti rat tgf β1

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Becton Dickinson rat anti-α5 integrin
Differential effects of loss of contractility. (A,B) Fibroblasts expressing mApple–paxillin show an altered distribution of adhesions on 2D (A) and 1D (B) surfaces after treatment with 25 μM blebbistatin. Kymographs illustrate the formation of NAs (red arrowheads) at the leading edge on 2D surfaces (A) and random formation on 1D surfaces (B). (C,D) Timelapse series showing AF568-labeled <t>9EG7</t> (activated <t>β1</t> <t>integrin)</t> incorporation into adhesions on 2D surfaces in the control (C) or after treatment with 25 μM blebbistatin (D). Note the rearward movement of integrins in the control (purple arrowheads) and the lack of movement after treatment with blebbistatin (cyan arrowheads). The yellow dotted line indicates the original position of the adhesion. (E,F) Activated β1 integrin incorporation on 1D surfaces in the control (E) or after treatment with blebbistatin (F). Kymographs illustrate that integrins remain stationary and stable in either condition. The white dotted lines show the leading edge; the kymograph is shown at the green dotted line. Scale bars: 5 μm.
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93
Alomone Labs β1 adrenergic receptor
No change in autonomic receptor expression at the heart. A, B) Western blot analysis of beta-1 <t>adrenergic</t> receptor (β1AR, n = 7/group) (A) and muscarinic acetylcholine receptor M2 (mAChR-M2, n = 6/group) (B) protein levels in right atria between CTL and STZ-AD. β-actin served as loading control.
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Image Search Results


A: Proliferation assay in β3 integrin−/− endothelial cells. MLEC were isolated from wild-type (β3+/+) and β3 integrin−/− (β3−/−) mice as previously described (Maeshima et al., 2002). Proliferation was assessed by [3H]-thymidine incorporation. All groups represent triplicate analyses. The results are shown as the mean ± SEM. ** indicates p < 0.01; compared to control cells.

Journal:

Article Title: Physiological levels of tumstatin, a fragment of collagen IV ?3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via ?V?3 integrin

doi:

Figure Lengend Snippet: A: Proliferation assay in β3 integrin−/− endothelial cells. MLEC were isolated from wild-type (β3+/+) and β3 integrin−/− (β3−/−) mice as previously described (Maeshima et al., 2002). Proliferation was assessed by [3H]-thymidine incorporation. All groups represent triplicate analyses. The results are shown as the mean ± SEM. ** indicates p < 0.01; compared to control cells.

Article Snippet: They were incubated with various primary antibodies, i.e., rat anti-mouse CD31 (Pharmingen), rabbit anti-von Willebrand Factor (vWF) (Dako), rat anti-β1 integrin (Pharmingen), and hamster anti-β3 integrin (Pharmingen) antibodies at room temperature for 2 hr.

Techniques: Proliferation Assay, Isolation

A: Immunohistochemical staining with anti-β3 integrin (β3) antibody and CD31 or vWF was performed to assess localization of β3 integrin in blood vessels. Anti-CD31 antibody was used for the tumor and skin tissues and anti-vWF antibody was used for the liver tissue. β3 integrin-positive blood vessels (merge) are indicated with arrows. Scale bar: 50 μm.

Journal:

Article Title: Physiological levels of tumstatin, a fragment of collagen IV ?3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via ?V?3 integrin

doi:

Figure Lengend Snippet: A: Immunohistochemical staining with anti-β3 integrin (β3) antibody and CD31 or vWF was performed to assess localization of β3 integrin in blood vessels. Anti-CD31 antibody was used for the tumor and skin tissues and anti-vWF antibody was used for the liver tissue. β3 integrin-positive blood vessels (merge) are indicated with arrows. Scale bar: 50 μm.

Article Snippet: They were incubated with various primary antibodies, i.e., rat anti-mouse CD31 (Pharmingen), rabbit anti-von Willebrand Factor (vWF) (Dako), rat anti-β1 integrin (Pharmingen), and hamster anti-β3 integrin (Pharmingen) antibodies at room temperature for 2 hr.

Techniques: Immunohistochemical staining, Staining

A: Immunohistochemical staining with anti-β3 integrin (β3) antibody and CD31 was performed to assess localization of β3 integrin in the tumor blood vessels with volumes of 0.1, 0.5 and 3.0 cm3 in wild-type mice. β3 integrin-positive blood vessels (merge) are indicated with arrows. Scale bar: 50 μm.

Journal:

Article Title: Physiological levels of tumstatin, a fragment of collagen IV ?3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via ?V?3 integrin

doi:

Figure Lengend Snippet: A: Immunohistochemical staining with anti-β3 integrin (β3) antibody and CD31 was performed to assess localization of β3 integrin in the tumor blood vessels with volumes of 0.1, 0.5 and 3.0 cm3 in wild-type mice. β3 integrin-positive blood vessels (merge) are indicated with arrows. Scale bar: 50 μm.

Article Snippet: They were incubated with various primary antibodies, i.e., rat anti-mouse CD31 (Pharmingen), rabbit anti-von Willebrand Factor (vWF) (Dako), rat anti-β1 integrin (Pharmingen), and hamster anti-β3 integrin (Pharmingen) antibodies at room temperature for 2 hr.

Techniques: Immunohistochemical staining, Staining

Journal: Cell Host & Microbe

Article Title: β1-Integrin Accumulates in Cystic Fibrosis Luminal Airway Epithelial Membranes and Decreases Sphingosine, Promoting Bacterial Infections

doi: 10.1016/j.chom.2017.05.001

Figure Lengend Snippet:

Article Snippet: The samples were stained with a rat anti-mouse β1-integrin (1:100 dilution, clone MB1.2, Merck Millipore), anti-acid ceramidase (1:100 dilution), anti-ceramide (1:100 dilution), anti-sphingosine (1:1000 dilution), anti-mouse β2-integrin antibodies (1:100, clone M1812, 1:100, #557437, BD) or FITC-Annexin (1:200, #11 828 681 001, Roche) in H/S (132 mM NaCl, 20 mM HEPES [pH 7.4], 5 mM KCl, 1 mM CaCl 2 , 0.7 mM MgCl 2 , 0.8 mM MgSO 4 ) plus 1% FCS at room temperature for 45 min.

Techniques: Virus, Isolation, Recombinant, Software

Differential effects of loss of contractility. (A,B) Fibroblasts expressing mApple–paxillin show an altered distribution of adhesions on 2D (A) and 1D (B) surfaces after treatment with 25 μM blebbistatin. Kymographs illustrate the formation of NAs (red arrowheads) at the leading edge on 2D surfaces (A) and random formation on 1D surfaces (B). (C,D) Timelapse series showing AF568-labeled 9EG7 (activated β1 integrin) incorporation into adhesions on 2D surfaces in the control (C) or after treatment with 25 μM blebbistatin (D). Note the rearward movement of integrins in the control (purple arrowheads) and the lack of movement after treatment with blebbistatin (cyan arrowheads). The yellow dotted line indicates the original position of the adhesion. (E,F) Activated β1 integrin incorporation on 1D surfaces in the control (E) or after treatment with blebbistatin (F). Kymographs illustrate that integrins remain stationary and stable in either condition. The white dotted lines show the leading edge; the kymograph is shown at the green dotted line. Scale bars: 5 μm.

Journal: Journal of Cell Science

Article Title: Micro-environmental control of cell migration - myosin IIA is required for efficient migration in fibrillar environments through control of cell adhesion dynamics

doi: 10.1242/jcs.098806

Figure Lengend Snippet: Differential effects of loss of contractility. (A,B) Fibroblasts expressing mApple–paxillin show an altered distribution of adhesions on 2D (A) and 1D (B) surfaces after treatment with 25 μM blebbistatin. Kymographs illustrate the formation of NAs (red arrowheads) at the leading edge on 2D surfaces (A) and random formation on 1D surfaces (B). (C,D) Timelapse series showing AF568-labeled 9EG7 (activated β1 integrin) incorporation into adhesions on 2D surfaces in the control (C) or after treatment with 25 μM blebbistatin (D). Note the rearward movement of integrins in the control (purple arrowheads) and the lack of movement after treatment with blebbistatin (cyan arrowheads). The yellow dotted line indicates the original position of the adhesion. (E,F) Activated β1 integrin incorporation on 1D surfaces in the control (E) or after treatment with blebbistatin (F). Kymographs illustrate that integrins remain stationary and stable in either condition. The white dotted lines show the leading edge; the kymograph is shown at the green dotted line. Scale bars: 5 μm.

Article Snippet: Reagents Sources were: rat anti-activated-β1 integrin 9EG7, rat anti-α5 integrin, and mouse anti-paxillin antibodies (BD Pharmingen); mouse anti-PY antibody (Upstate Biotechnology); rabbit anti-MIIA and rabbit anti-MIIB antibodies (Covance).

Techniques: Expressing, Labeling

No change in autonomic receptor expression at the heart. A, B) Western blot analysis of beta-1 adrenergic receptor (β1AR, n = 7/group) (A) and muscarinic acetylcholine receptor M2 (mAChR-M2, n = 6/group) (B) protein levels in right atria between CTL and STZ-AD. β-actin served as loading control.

Journal: Journal of Alzheimer's disease : JAD

Article Title: Autonomic Dysfunction Impairs Baroreflex Function in an Alzheimer’s Disease Animal Model

doi: 10.3233/JAD-220496

Figure Lengend Snippet: No change in autonomic receptor expression at the heart. A, B) Western blot analysis of beta-1 adrenergic receptor (β1AR, n = 7/group) (A) and muscarinic acetylcholine receptor M2 (mAChR-M2, n = 6/group) (B) protein levels in right atria between CTL and STZ-AD. β-actin served as loading control.

Article Snippet: Next, proteins were transferred onto a PVDF membrane (IPFL00005, Immobilon-FL), and nonspecific binding was blocked with Intercept Protein-Free Blocking Buffer (927–90001, LI-COR) for 1 h. The membrane was then washed in Tris-buffered saline containing 0.1% Tween-20 and incubated with primary antibodies against either β1 adrenergic receptor (1 : 1000, rabbit, #AAR-023, Alomone labs) or muscarinic acetylcholine receptor M2 (1 : 600, rabbit, #AMR-002, Alomone labs) and β-actin (1 : 5000, mouse, #926–42212, LI-COR) overnight at 4°C.

Techniques: Expressing, Western Blot, Control