VPAC2 (IHC-grade), VIP Receptor 2 Antibody

Figure 1. Immunohistochemical identification of VIP Receptor 2 in small intestine. Sections were dewaxed, microwaved in citric acid, and incubated with anti-VPAC2 (VIP receptor 2) antibody (7TM0372N-IC) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution.Color was developed by incubation in 3-amino-9-ethylcarbazole (AEC), and sections were counterstained with hematoxylin. Note, VPAC2 receptors were detected at the plasma membrane of neuroendocrine cells in small intestine.

Figure 2. Immunohistochemical identification of VIP Receptor 2 in breast carcinoma. Sections were dewaxed, microwaved in citric acid, and incubated with anti-VPAC2 (VIP receptor 2) antibody (7TM0372N-IC) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution. Sections were then developed in 3,3-diaminobenzidine (DAB)-glucose oxidase and lightly counterstained with hematoxylin. Note, VPAC2 receptors were uniformly detected at the plasma membrane of nearly all tumor cells.

Figure 3. Immunohistochemical identification of VIP Receptor 2 in lung carcinoma. Sections were dewaxed, microwaved in citric acid, and incubated with anti-VPAC2 (VIP receptor 2) antibody (7TM0372N-IC) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution. Sections were then developed in 3,3-diaminobenzidine (DAB)-glucose oxidase and lightly counterstained with hematoxylin. Note, VPAC2 receptors were uniformly detected at the plasma membrane of nearly all tumor cells.

Figure 4. Immunohistochemical identification of VIP Receptor 2 in pancreatic carcinoma. Sections were dewaxed, microwaved in citric acid, and incubated with anti-VPAC2 (VIP receptor 2) antibody (7TM0372N-IC) at a dilution of 1:100. Sections were then sequentially treated with biotinylated anti-rabbit IgG and avidin-biotin solution.Color was developed by incubation in 3-amino-9-ethylcarbazole (AEC), and sections were counterstained with hematoxylin. Note, VPAC2 receptors were uniformly detected at the plasma membrane of nearly all tumor cells.

Figure 5. Validation of the VIP Receptor 2 in transfected HEK293 cells. Native HEK293 cells (MOCK) or HEK293 cells stably expressing the VIP Receptor 2 (VPAC2) were lysed and immunoblotted with the phosphorylation-independent anti-VPAC2 antibody (7TM0372N-IC) at a dilution of 1:1000.

Figure 6. Immunocytochemical identification of VIP Receptor 2 in HEK293 cells. Native HEK293 cells (MOCK) or HEK293 cells stably expressing the VIP receptor 2 (VPAC2) were immunocytochemically stained with anti-VPAC2 (VIP receptor 2) antibody (7TM0372N-IC) at a dilution of 1:200. Note, VPAC2 receptors were confined to the plasma membrane in transfected cells.

Figure 7. Western blot analysis of VIP Receptor 2 in mouse tissues in vivo. Tissues from VPAC2-deficient mice (VPAC2-KO) and their wild-type littermates (VPAC2-WT) were dissected, homogenated and immunoblotted using anti-VPAC2 (VIP receptor 2) antibody (7TM0372N-IC) at a dilution of 1:1000. Note, absence of VPAC2 receptors in stomach and colon in VPAC2-KO but not in VPAC2-WT mice.

Schulz S, Röcken C, Mawrin C, Weise W, Höllt V, Schulz S. Immunocytochemical identification of VPAC1, VPAC2, and PAC1 receptors in normal and neoplastic human tissues with subtype-specific antibodies. Clin Cancer Res. 2004 Dec 15;10(24):8235-42. PubMed PMID: 15623599.

Schulz S, Mann A, Novakhov B, Piggins HD, Lupp A. VPAC2 receptor expression in human normal and neoplastic tissues: evaluation of the novel MAB SP235. Endocr Connect. 2015 Mar;4(1):18-26. doi: 10.1530/EC-14-0051. Epub 2014 Dec 11. PubMed PMID: 25504760; PubMed Central PMCID: PMC4285768.