- 41-0700 - Invitrogen Antibodies CAV2 antibody

Submitted references Homotrimer cavin1 interacts with caveolin1 to facilitate tumor growth and activate microglia through extracellular vesicles in glioma.

Wang L, Yang C, Wang Q, Liu Q, Wang Y, Zhou J, Li Y, Tan Y, Kang C
Theranostics 2020;10(15):6674-6694

MicroRNA-218 inhibits cell migration and invasion in renal cell carcinoma through targeting caveolin-2 involved in focal adhesion pathway.

Yamasaki T, Seki N, Yoshino H, Itesako T, Hidaka H, Yamada Y, Tatarano S, Yonezawa T, Kinoshita T, Nakagawa M, Enokida H
The Journal of urology 2013 Sep;190(3):1059-68

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Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Western blot analysis of A431 cell lysates using Zymed Ms anti-Caveolin-2 (Product # 41-0700).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Western blot was performed using Caveolin 2 Monoclonal Antibody (ZC013) (Product # 41-0700) and a~18 kDa band corresponding to Caveolin-2 was observed in A431, A549, and HeLa; and was absent in Jurkat and 3T3L1. Whole cell extracts (30 µg lysate) of A431 (Lane 1), A549 (Lane 2), HeLa (Lane 3), Jurkat (Lane 4) and 3T3L1 (Lane 5) were electrophoresed using NuPAGE® 4-12 % Bis-Tris gel (Product # NP0322BOX). Resolved proteins were then transferred onto a nitrocellulose membrane (Product # IB23001) by iBlot® 2 Dry Blotting System (Product # IB21001).The blot was probed with the primary antibody (1:1000 dilution) and detected by chemiluminescence with Goat anti-Mouse IgG (H+L) Superclonal™ Recombinant Secondary Antibody, HRP (Product # A28177, 1:4000 dilution) using the iBright FL 1000 (Product # A32752). Chemiluminescent detection was performed using Novex® ECL Chemiluminescent Substrate Reagent Kit (Product # WP20005).

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
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Experimental details: Figure 3 eGFP-Cavin1 interacts with Caveolin1 and was loaded onto EVs of U87 cells. (A) Schematic diagram of the proposed mechanism showing how Cavin1 and vCavin1 affect EV production. (B) WB analysis showing an equal expression level of eGFP-Cavin1 and eGFP-vCavin1 in U87 cells. In addition, the levels of endogenous Cavin1, Caveolin1 and Caveolin2 were not altered by eGFP-Cavin1 and eGFP-vCavin1 expression. (C) IP-WB analysis showing an obvious association of eGFP-Cavin1 with Caveolin1 but no binding between eGFP-vCavin1 and Caveolin1 in U87. (D) WB analysis showing the overexpression of eGFP-Cavin1 in EVs, whereas no eGFP-vCavin1 was detected. Besides, eGFP-Cavin1 and eGFP-vCavin1 expression did not affect levels of endogenous Cavin1, Caveolin1, and Caveolin2 in EVs. (E) Confocal images showing an evident co-localization of eGFP-Cavin1 with Caveolin1 but little co-localization of eGFP-vCavin1 with Caveolin1. (F) Colocalization was quantified and expressed as a Pearson coefficient value. Colocalization of Caveolin1 with eGFP-Cavin1 was significantly higher than with eGFP-vCavin1 (p < 0.0001). (G) Confocal images showing co-localization of eGFP-vCavin1 with Caveolin2 but only little co-localization of eGFP-Cavin1 with Caveolin2. (H) The colocalization of Caveolin2 with eGFP-vCavin1 was higher than with eGFP-Cavin1 (p < 0.001). (I) Confocal images showing co-localization of eGFP-Cavin1 with EEA1. (J) Colocalization of EEA1 with eGFP-Cavin1 was significantly higher than with eG

Supportive validation

Submitted by: Invitrogen Antibodies (provider)
Main image
Experimental details: Figure 8 eGFP-Cavin1 overexpressing murine glioma cells GL261 secreted EVs leading to recruitment and activation of microglia. (A) WB analysis of the expression of eGFP-Cavin1, endogenous Cavin1, Caveolin1, and Caveolin2 in GL261-eGFP, GL261-C, and GL261-vC cells; eGFP-Cavin1 or eGFP-vCavin1 expression did not alter the expression level of endogenous Cavin1. However, Caveolin1 and Caveolin2 levels increased in cells expressing eGFP-Cavin1. (B) IP-WB analysis showing an obvious association between eGFP-Cavin1 and Caveolin1 but no binding between eGFP-vCavin1 and Caveolin1 in GL261. (C) WB analysis of the expression of eGFP-Cavin1, Caveolin1, Caveolin2, CD63, CD81, and Alix in GL261-EVs, GL261-C-EVs, and GL261-vC-EVs; eGFP-Cavin1 showed a high expression level whereas eGFP-vCavin1 was not detected in EVs. In addition, Caveolin1 and Caveolin2 levels were not affected by eGFP-Cavin1 and eGFP-vCavin1 expression. (D) Representative images of migrated BV2 cells induced by an equal concentration of GL261-EVs, GL261-C-EVs or GL261-vC-EVs in the transwell migration assay. Scale bar, 200 mum. (E) Quantification of the number of migrated BV2 cells. GL261-C-EVs induced an increase in the number of migrated BV2 cells as compared with GL261-EVs and GL261-vC-EVs (p < 0.001; p < 0.001). Compared with the Control group, GL261-EVs and GL261-vC-EVs both increased the migrated cell number (p < 0.05; p < 0.05). (F) Confocal immunofluorescence images of BV2 cells treated for 48 h with an equal conc

41-0700

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