Monoclonal primary antibodies against human α-catenin (Cat#2028-1), β-catenin (Cat#1247-1), and E-cadherin (Cat#1702-1) were purchased from Epitomics (Burlingame, CA, USA). The primary monoclonal antibodies against the HA tag (Cat#ab9134) and human β-actin (Cat#sc-130300) were purchased from Abcam (Cambridge, UK) and Santa Cruz Biotechnology (Santa Cruz, CA, USA), respectively. The pcDNA3.1-HA-p65 and pcDNA3.1 vectors were kindly provided by Dr Jun Cui (Zhongshan School of Medicine, Sun Yat-sen University). The NF-κB inhibitor Bay 11-7082 was obtained from Sigma-Aldrich (St Louis, MO, USA).
Human β actin
Manufactured by Abcam
Sourced in United Kingdom
β-actin is a structural protein that is ubiquitously expressed in eukaryotic cells. It is a key component of the cytoskeleton and is involved in various cellular processes, such as cell motility, cell division, and cell signaling.
Automatically generated - may contain errors
Lab products found in correlation
β catenin, by Abcam (1 mentions)
Bay11 7082, by Merck Group (1 mentions)
E cadherin, by Abcam (1 mentions)
Monoclonal primary antibodies against human α catenin, by Abcam (1 mentions)
Hdac7, by Cell Signaling Technology (1 mentions)
Rapamycin, by Selleck Chemicals (1 mentions)
Hdac8, by Abcam (1 mentions)
Ar420626, by Merck Group (1 mentions)
Phospho mtor ser2448, by Cell Signaling Technology (1 mentions)
Mg132, by Merck Group (1 mentions)
Hnrnp l, by Abcam (1 mentions)
Image lab system, by Bio-Rad (1 mentions)
Pvdf membrane, by Merck Group (1 mentions)
Ripa buffer, by Beyotime (1 mentions)
Bcl 2, by Abcam (1 mentions)
Concanavalin a (cona), by Merck Group (1 mentions)
Human insulin, by Eli Lilly (1 mentions)
Af146, by R&D Systems (1 mentions)
5 protocols using human β actin
1
Evaluating Catenin Protein Expression
2
Proteasome Inhibition and mTOR Regulation
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N-(2,5-Dichlorophenyl)-4-(furan-2-yl)-2-methyl-5-oxo-1,4,5,6,7,8-hexahydro-quinoline-3-carboxamide (AR420626) and MG-132 (Sigma-Aldrich, St. Louis, MO, USA); TNF-α antagonist R-705013 (link) (Calbiochem, Darmstadt, Germany); rapamycin (Selleckchem, Houston, TX, USA); polyclonal rabbit antibodies against human β-actin (Abcam, Cambridge, UK), acetyl-histone H3 (Lys9/Lys14), cleaved caspase-3 (Asp175), cleaved caspase-9, phospho-mTOR (Ser2448) (Cell Signaling Technology, Boston, MA, USA); monoclonal rabbit antibodies against HDAC1, HDAC2, HDAC4, HDAC5, HDAC6, HDAC7, mTOR (Cell Signaling Technology) and HDAC8 (Abcam); monoclonal mouse antibodies against HDAC3, caspase-8 (Cell Signaling Technology) and 20S Proteasome β5 (Santa Cruz Biotechnology, Dallas, TX, USA); and horseradish peroxidase (HRP)-conjugated antimouse and antirabbit immunoglobulins (Dako, Glostrup, Denmark) were used in the study.
3
Quantitative Analysis of Protein Expression
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Cells were harvested 48 hrs after siRNA transfection, and protein was isolated with RIPA buffer (Beyotime, China). Cellular protein was extracted from each group, and the total protein content was determined according to the instructions provided with the cell protein extraction kit. The total protein samples were separated on SDS-PAGE gels and transferred onto PVDF membranes (Millipore, USA). The membranes were immunoblotted overnight at 4°C with primary antibodies against the following targets: HnRNPL (1:800; Abcam, UK), p53 (1:800; Abcam, UK), Bcl2 (1:1000; Abcam, UK), and human β-actin (1:500; Abcam, UK). The PVDF membranes were washed with TBST and then incubated with secondary HRP-conjugated goat IgG (1:5000; ZSGB-BIO,China) for 1 hr at 37°C. Signals were detected with a Bio-Rad Image Lab system (Bio-Rad, USA). The images were quantified by Image J software, and the relative protein expression levels were normalized to β-actin levels in each sample. All experiments were performed in triplicate.
4
Whole-Blood Immune Response Assay
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The whole-blood sample from each individual was divided into 7 1-ml aliquots. The samples were either treated or untreated, as follows: Tube 1, concanavalin A as positive control (Sigma-Aldrich, Bremen, Germany); Tube 2, untreated sample as negative control; Tube 3, human albumin (Fresenius, Bad Homburg, Germany); Tube 4, human β-actin (Abcam; Cambridge, UK); Tube 5, human glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Sigma-Aldrich, Bremen, Germany); Tube 6, human insulin (Eli Lilly; Bad Homburg, Germany); and Tube 7, untreated sample as negative control. All proteins were used at the same two concentrations (low: 2 µg/ml and high: 2 mg/ml), which were confirmed using the Bradford assay. For incubations at the 2-mg/ml concentration, the proteins were pre-incubated with a BioTrek transfection reagent (Stratagene, La Jolla, CA, USA). For intracellular cytokine assays (IL-2, IFg) and for HLA-DR activation, anti-CD28 and CD49d were used to co-stimulate T cells.
5
Antibody Characterization for Immunoanalysis
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Antibodies were purchased commercially as follows: human IL13RA2 (MAB614 for immunoblotting and AF146 for immunohistochemistry, R&D Systems, Minneapolis, MN), human STAT6, human phospho-STAT6 Y641 (Cell Signaling Technology, Beverly, MA), human ssDNA (IBL, Tokyo, Japan), human β-actin, human N-cadherin and mouse CD31 (Abcam, Cambridge, MA).
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