Isoprenaline (ISO, I5627), formoterol (product no. F9552), ICI118,551 (product no. I127), atenolol (product no. A7655) and 3-methyladenine (3-MA, product no. M9281) were procured from Sigma-Aldrich/Merck. SBI-0206965 was procured from Selleck Chemicals. Antibodies for β1-AR (product no. ab3442), β2-AR (product no. ab182136), N-MYC (product no. ab24193), and Beclin-1 (product no. ab109631 for IHC assay) were obtained from Abcam. Antibodies for LC3B (product no. 3868), Beclin-1 (product no. 3495), CREB (product no. 48H2), p-CREB (product no. 87G3), p-ULK1 (product no. 5869S) and ULK1 (product no. 8054T) were obtained from Cell Signaling Technology. LC3-II (cat. no. A11923) for IHC staining was purchased from Abclonal. ULK1 for the IHC assay was obtained from Zen BioScience.
β2 ar
Manufactured by Abcam
Sourced in United Kingdom
β2-AR is a type of G protein-coupled receptor that binds to and is activated by the neurotransmitter norepinephrine. It plays a role in the regulation of various physiological processes, including cardiovascular function, smooth muscle relaxation, and metabolic processes.
Automatically generated - may contain errors
Lab products found in correlation
β1 ar, by Abcam (2 mentions)
Atenolol, by Merck Group (1 mentions)
P ulk1, by Cell Signaling Technology (1 mentions)
Sbi 0206965, by Selleck Chemicals (1 mentions)
Beclin 1, by Cell Signaling Technology (1 mentions)
3 methyladenine 3 ma, by Merck Group (1 mentions)
Isoprenaline, by Merck Group (1 mentions)
Beclin 1, by Abcam (1 mentions)
Formoterol, by Merck Group (1 mentions)
N myc, by Abcam (1 mentions)
P creb, by Cell Signaling Technology (1 mentions)
Ici 118 551, by Merck Group (1 mentions)
Il 17, by Santa Cruz Biotechnology (1 mentions)
Rorγt, by Abcam (1 mentions)
Il 22, by Santa Cruz Biotechnology (1 mentions)
Odyssey laser scanning system, by LI COR (1 mentions)
Mouse anti β actin antibody, by Merck Group (1 mentions)
Infrared fluorescent dye labeled secondary antibody, by LI COR (1 mentions)
Odyssey infrared scanning system, by LI COR (1 mentions)
β actin, by Proteintech (1 mentions)
6 protocols using β2 ar
1
Molecular Regulation of Autophagy Pathways
2
Quantitative Protein Analysis of Immune Cells
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Total proteins were extracted from the spleens and ankle joints of mice or from in vitro cultured CD4+ T cells and Th17 cells. Briefly, tissues or cells were homogenized in lysis buffer, which contained 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, 1 mM EDTA, 1% NP-40, 0.5% deoxycholic acid, 0.1% SDS, and 10 μl/ml protease inhibitor. By centrifuging at 4°C at 12,000 rpm for 15 min, the supernatants were obtained. The proteins were separated and transferred to membranes according to our previous description [7 (link)]. After blocking nonspecific binding, the membranes were incubated with rabbit antibodies against β2-AR (1: 200; Abcam, UK), ROR-γt (1: 500; Abcam, UK), IL-17 (1: 200; Santa Cruz Biotechnology, USA), IL-22 (1: 200; Santa Cruz Biotechnology, USA), PKA (1: 200; Santa Cruz Biotechnology, USA), or mouse anti-β-actin antibody (1: 5000; Sigma, USA) at 4°C overnight. Following incubation with the corresponding secondary antibodies (1: 5,000; Rockland Immunochemicals, USA), the membranes were visualized using Odyssey laser scanning system (LI-COR Inc, USA), and the protein band intensities were quantified by an image analysis system (Odyssey 3.0 software).
3
Western Blot Analysis of β2-AR Protein
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Total protein was extracted with the procedures as described [41 ]. Briefly, Protein samples (80-100 μg) were separated by 10% acrylamide gel electrophoresis (SDS-PAGE), and then transferred to nitrocellulose membrane. The membranes were blocked with 5% defatted milk for 2-3 h at room temperature on a rocker and then incubated with primary antibodies β2-AR (Abcam, Cambridge, MA, UK) and beta-actin (Proteintech, Wuhan, China) at 4°C overnight. After washing with PBS-T (PBS containing 0.5% Tween 20) for 3 times, the membranes were incubated with infrared fluorescent dye-labeled secondary antibody (LI-COR Biosciences, Lincoln, USA) for 50 min at room temperature away from light. Western blot bands were acquired using Odyssey infrared scanning system (LI-COR Biosciences, Lincoln, USA) and analyzed using Image Studio Ver 4.0 software.
4
Molecular Markers for Neuronal Subregions
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The DG was extracted from the region between -1.55 mm and -2.79 mm posterior to bregma. The dissected tissue samples that were isolated using tissue punches (0.75 mm diameter) were pooled (2 to 3 samples). Subcellular fraction and western blot were described in a previous publication by our group26 (link). Anti-p-ERK1/2 (1:1,000) and anti-TRX-1 (1:1,000) were purchased from Cell Signaling Tech. Inc. (Danvers, MA, USA). β1-AR (1:500) and β2-AR (1:500) were purchased from Abcam (Cambridge, UK). Anti-class III beta-tubulin (anti-Tju1; 1:500), anti-β-catenin (1:500), anti-β-actin, and anti-lamin B were obtained from Sigma-Aldrich (Sigma-Aldrich, St. Louis, MO, USA).
5
Immunohistochemical Analysis of Xenograft Tissues
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Fixed frozen IH tissue sections and IH xenograft tissues were stained as previously described [34 (link)]. The antibodies included β1AR (1:400; Abcam, Cambridge, U.K., http://www.abcam.com ) and β2AR (1:500; Abcam), CD133 (1:50; EMD Millipore, Billerica, MA, http://www.emdmillipore.com ), CD31 (1:50; Dako, Glostrup, Denmark, http://www.dako.com ), and phosphorylated ERK1/2 (pERK1/2) (P-p44/42; 1:100; Cell Signaling Technology, Beverly, MA, http://www.cellsignal.com ) and were detected with either Alexa Fluor 488 or 594 secondary antibodies (Invitrogen, Carlsbad, CA, http://www.invitrogen.com ). From each IH xenograft, the number of activated ERK1/2-positive cells was determined and divided by the total number of cells from three representative high-power fields (HPFs).
6
Protein Expression Analysis in Myocardial Apexes
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Proteins were extracted from myocardial apexes (n = 4 hearts/group), treated with reducing agents, denatured at 100°C, and separated by gel electrophoresis as previously described (Hou et al., 2018 (link)). Next, the proteins were transferred onto polyvinylidene fluoride (PVDF) membranes, blocked with 1% bovine serum albumin, and incubated in the following primary antibodies at 4°C overnight; ANP (1:1,000, Santa Cruz Biotechnology, Dallas, TX, United States; sc-515701), BNP (1:1,000, Santa Cruz Biotechnology; sc-271185), β2AR (1:1,000, Abcam; ab182136), GAPDH (1:4,000, Proteintech, Manchester, United Kingdom; 10494-1-AP). Visualizations of immunoblots were done with enhanced chemiluminescence (Tanon, Shanghai, China). The protein bands were quantified and evaluated by the relative expressions with their GAPDH.
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