Immunostaining was performed on 4 μm-thick paraffin sections using rabbit anti-AGR2 antibody (Abcam, 1:30), anti-XBP1s (Monoclonal Antibodies Unit, CNIO, Madrid, Spain 1:100), anti-ATF6 (Abcam, 1:8000), anti-GRP78 (Cell Signalling Technology, Hitchin, UK, 1:200) with DABMap kit, following protocols for the Ventana Discovery System (Illkirch, France). Counterstaining was performed with haematoxylin.
Anti agr2 antibody
Manufactured by Abcam
Sourced in Spain, United Kingdom, United States
The Anti-AGR2 antibody is a laboratory reagent used for the detection and analysis of the AGR2 protein in biological samples. AGR2 is a protein involved in various cellular processes and is often studied in the context of cancer research and other areas of biology. This antibody can be used in techniques such as Western blotting, immunohistochemistry, and immunofluorescence to identify and quantify the presence of AGR2 in cells or tissues.
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Lab products found in correlation
Anti β actin antibody, by Abcam (2 mentions)
Anti atf6, by Abcam (1 mentions)
Anti grp78, by Cell Signaling Technology (1 mentions)
Anti mmp2 antibody, by Abcam (1 mentions)
Anti mmp9 antibody, by Cell Signaling Technology (1 mentions)
Ecl reagent, by GE Healthcare (1 mentions)
Protease inhibitor, by Roche (1 mentions)
Dm6000b, by Leica (1 mentions)
Goat anti rabbit igg fitc, by Santa Cruz Biotechnology (1 mentions)
Rhodamine conjugated goat anti rat igg h l, by Proteintech (1 mentions)
Vegfr2 antibody, by Abcam (1 mentions)
Anti cd31 antibody, by Abcam (1 mentions)
Bca protein assay kit, by Takara Bio (1 mentions)
Hif 1α antibody, by Proteintech (1 mentions)
Ecl kit, by GE Healthcare (1 mentions)
Anti β actin antibody, by Cell Signaling Technology (1 mentions)
Ripa lysis buffer, by Beyotime (1 mentions)
4 protocols using anti agr2 antibody
1
Immunohistochemical Analysis of UPR Markers
2
Western Blot Protocol for Protein Analysis
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After transfection, cells were harvested and lysed in NP-40 lysis buffer (20 mM Tris-HCl, pH 7.5; 150 mM NaCl; and 1% NP-40) supplemented with protease inhibitors (Roche). The clarified cell lysate (usually 50 μg protein) was applied onto 10% SDS-PAGE gels and then transferred to PVDF membranes. The membranes were probed with the primary antibodies followed by incubation with HRP-conjugated secondary antibodies. The proteins were visualized by ECL reagents (GE Healthcare). Monoclonal antibodies used in this study were anti-AGR2 antibody (1:1,000; abcam), anti-α-DG antibody (1:1,000; Cell Signaling), anti-β-DG antibody (1:1,000; Santa Cruz), MANDAG for β-DG (1:200; DSHB, University of Iowa), anti-MMP2 antibody (1:1,000; abcam), anti-MMP9 antibody (1:1,000; Cell Signaling), and anti-β-actin antibody (1:20,000; abcam).
3
Immunohistochemical Analysis of Tumor Vasculature
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Tumor tissue was fixed (4% paraformaldehyde, 24 h), paraffin-embedded, sectioned, dewaxed (Xylene), rehydrated (graded alcohol), and blocked (2% normal goat serum, 1 h). Then the sections were stained with α-smooth muscle actin (SMA) antibody (1:100; Proteintech, Chicago, USA), antivascular endothelial growth factor receptor 2 (VEGFR2), antibody (1:100; Abcam, Cambridge, UK), anti-AGR2 antibody (1:500; Abcam, Cambridge, UK), and anti-CD31 antibody (1:500; Abcam , Cambridge, UK). The sections were washed and incubated with rhodamine-conjugated goat anti-rat IgG (H+L) (1:50; Proteintech, Chicago, USA) or goat anti-rabbit IgG-FITC (1:200; Santa Cruz, Dallas, USA) for 40 min at room temperature. Tissue was visualized using a fluorescence microscope (Leica DM6000B).
4
Tumor and Endothelial Cell Protein Analysis
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Tumors were harvested. Radioimmunoprecipitation assay (RIPA) lysis buffer (Beyotime, Shanghai, China) was used to lyse tumor tissue. Bicinchoninic acid (BCA) protein assay kits (TaKaRa, Dalian, China) were used to detect protein concentrations. Western-blotting assay was conducted for detection of HIF-1α and AGR2 by using HIF-1α antibody (1:100; Proteintech, Chicago, USA) and anti-AGR2 antibody (1:500; Abcam, Cambridge, UK) as primary antibody. Well-grown HUVECs were cultured with 1 µg AGR2. Then HUVECs were treated with rhES (100 µg), AuNPs (100 µg), rhES-AuNPs (100 µg), and saline (5 mM) for 24 h, respectively. Lysates of HUVECs were collected and applied for detection of MMP2, cMyc, VE-cadherin (VE-ca), and phosphorylation of p38 and ERK1/2, by using rabbit monoclonal p44/p42 (ERK1/2) antibody, rabbit monoclonal phos-phop44/42 (ERK1/2) antibody, rabbit monoclonal p38 antibody, mouse monoclonal phosphop38 (Thr180/Tyr182) antibody, and rabbit polyclonal anti-β-actin antibody (Cell Signaling, Boston, USA). The internal control protein was β-actin. It was detected by anti-beta actin antibody (1:1000; Abcam, Cambridge, UK). Detection was performed with the ECL kit (GE Healthcare, Pittsburgh, USA).
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