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Rabbit anti mitofusin 2

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Rabbit-anti-Mitofusin-2 is a primary antibody used in immunochemical applications to detect the Mitofusin-2 protein. Mitofusin-2 is a protein involved in the fusion of mitochondrial outer membranes. This antibody can be used to identify and quantify Mitofusin-2 expression in various cell and tissue samples.

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Lab products found in correlation

Rabbit anti tom20, by Santa Cruz Biotechnology (3 mentions) Ar a014418, by Abcam (3 mentions) Ct99021, by Abcam (3 mentions) Mouse pdi rl77, by Thermo Fisher Scientific (2 mentions) Antibodies to total and ser9 phosphorylated inactive gsk3β, by BD (2 mentions) Rabbit anti gfp and mouse anti βactin, by Abcam (2 mentions) Rabbit anti tdp 43 12892 1 ap, by Proteintech (2 mentions) Mouse anti α tubulin dm1a, by Merck Group (2 mentions) Mouse 610201, by Cell Signaling Technology (2 mentions) Rabbit anti actin, by Abcam (1 mentions) Rabbit anti calreticulin, by Abcam (1 mentions) Rabbit anti gapdh, by Santa Cruz Biotechnology (1 mentions) Odyssey system, by LI COR (1 mentions) Semi dry transfer apparatus, by Bio-Rad (1 mentions) Rabbit anti glyceraldehyde 3 phosphate dehydrogenase gapdh, by Cell Signaling Technology (1 mentions) Rabbit anti gfp ab290, by Abcam (1 mentions) Mouse anti myc 9b11, by Cell Signaling Technology (1 mentions) Rabbit anti egfp, by Abcam (1 mentions) Rabbit anti ha, by Merck Group (1 mentions) Mouse anti calnexin, by BD (1 mentions)

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Rabbit anti- (2 citations)

5 protocols using rabbit anti mitofusin 2

1

Western Blot Analysis of Cellular Proteins

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Whole-cell lysates and cell fraction lysates were prepared as described above, and protein concentrations were determined by the Bradford method (Bradford, 1976 (link)). Samples were diluted in a reducing sample buffer, and subjected to SDS-PAGE using Peirce pre-cast Tris-HEPES gels. A BioRad SemiDry Transfer apparatus was used for gel transfer to PVDF. The resulting Western blots were probed using the following primary antibodies: PRK8 mouse-anti-Parkin (1:200; Santa Cruz), rabbit-anti-Mitofusin-2 (1:2000; Sigma, cat# 110M4842), mouse-anti-HSP60 (1:1200; Stressgen, cat# SPA-806), rabbit-anti-calreticulin (1:1000; Abcam, cat# ab92516), rabbit-anti-GAPDH (1:1200; Santa Cruz, cat# sc25778), rabbit-anti-actin (1:12,000; Abcam, cat# ab8227), rabbit-anti-FACL4 (1:5000; Abcam, cat# ab137525). For secondaries, corresponding Li-Cor Odyssey compatible IR680- and IR800-conjugated antibodies were used for detection, and blots were imaged and analyzed using a Li-Cor Odyssey system (Li-Cor).
Van Laar V.S., Roy N., Liu A., Rajprohat S., Arnold B., Dukes A.A., Holbein C.D, & Berman S.B. (2014). Glutamate excitotoxicity in neurons triggers mitochondrial and endoplasmic reticulum accumulation of Parkin, and, in the presence of N-acetyl cysteine, mitophagy. Neurobiology of disease, 74, 180-193.
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2

Generation of Rat and Rabbit Antibodies to VAPB and PTPIP51

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Rat and rabbit antibodies to VAPB and PTPIP51 were generated by immunisation with GST-VAPB(1-220) and GST-PTPIP51(36-470) respectively20 (link). Rabbit anti-PTPIP51 was from Atlas, rabbit anti-hemagglutin (HA), mouse anti-α-tubulin (DM1A) and rabbit anti-Mitofusin2 were from Sigma. Rabbit anti-TOM20 was from Santa Cruz Biotechnology. Rabbit anti-GFP and mouse anti-βactin were from Abcam. Mouse PDI (RL77) was from Affinity Bioreagents. Rabbit anti-TDP-43 (12892-1-AP) was from Proteintech. Antibodies to total and ser9 phosphorylated (inactive) GSK3β were from BD Transduction Labs (mouse 610201) and Cell Signalling (rabbit 9336) respectively. The concentrations used for the different antibodies are shown in Supplementary Table 1. Secondary antibodies were horseradish peroxidase-coupled goat anti-mouse, anti-rabbit and anti-rat Igs (GE Healthcare), and Alexa fluorophore (350, 488 and 568) coupled goat anti-mouse and anti-rabbit IgGs (Invitrogen). AR-A014418 and CT99021 were from Abcam and Cayman respectively.
Stoica R., De Vos K.J., Paillusson S., Mueller S., Sancho R.M., Lau K.F., Vizcay-Barrena G., Lin W.L., Xu Y.F., Lewis J., Dickson D.W., Petrucelli L., Mitchell J.C., Shaw C.E, & Miller C.C. (2014). ER–mitochondria associations are regulated by the VAPB–PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43. Nature Communications, 5, 3996.
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Antibodies for VAPB and PTPIP51 analysis

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Rat and rabbit antibodies to VAPB and PTPIP51 were generated by immunization with
GST-VAPB(1–220) and GST-PTPIP51(36–470),
respectively20 (link). Rabbit anti-PTPIP51 was from Atlas, rabbit
anti-haemagglutin (HA), mouse anti-α-tubulin (DM1A) and rabbit
anti-Mitofusin-2 were
from Sigma. Rabbit anti-TOM20 was from Santa Cruz Biotechnology. Rabbit anti-GFP
and mouse anti-βactin were from Abcam. Mouse PDI (RL77) was from Affinity
Bioreagents. Rabbit anti-TDP-43 (12892-1-AP) was from Proteintech. Antibodies to
total and ser9-phosphorylated (inactive) GSK-3β were from BD Transduction Labs (mouse
610201) and Cell Signalling (rabbit 9336), respectively. The concentrations used
for the different antibodies are shown in Supplementary Table 1. Secondary antibodies were horseradish
peroxidase-coupled goat anti-mouse, anti-rabbit and anti-rat Igs (GE
Healthcare), and Alexa fluorophore (350, 488 and 568)-coupled goat anti-mouse
and anti-rabbit IgGs (Invitrogen). AR-A014418 and CT99021 were from Abcam and Cayman, respectively.
Stoica R., De Vos K.J., Paillusson S., Mueller S., Sancho R.M., Lau K.F., Vizcay-Barrena G., Lin W.L., Xu Y.F., Lewis J., Dickson D.W., Petrucelli L., Mitchell J.C., Shaw C.E, & Miller C.C. (2014). ER–mitochondria associations are regulated by the VAPB–PTPIP51 interaction and are disrupted by ALS/FTD-associated TDP-43. Nature Communications, 5, 3996.
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4

Antibodies for VAPB and PTPIP51 Proteins

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Rat and rabbit antibodies to VAPB and PTPIP51 have been described previously and were generated by immunization with GST‐VAPB(1–220) and GST‐PTPIP51(36–470) 5. Rabbit PTPIP51 antibody (FAM82A2) was from Atlas Antibodies. Rabbit anti‐haemagglutinin (HA), mouse anti‐α‐tubulin (DM1A) and rabbit anti‐mitofusin‐2 were from Sigma. Mouse anti‐myc (9B11) and rabbit anti‐glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) were from Cell Signaling. Rabbit anti‐FUS (NB100‐565) was from Novus Biologicals. Rabbit anti‐TOM20 was from Santa Cruz Biotechnology and mouse anti‐PDI (RL77) was from Affinity Bioreagents. Antibodies to total and ser9 phosphorylated (inactive) GSK‐3β were from BD Transduction Labs (mouse 610201) and Cell Signalling (rabbit 9336), respectively. Rabbit anti‐GFP (Ab290) was from Abcam. GSK‐3β inhibitors AR‐A014418 and CT99021 were from Abcam and Cayman, respectively, and made up as 1 mM or 100 μM stocks in DMSO; KCN was from Sigma and made up as a 1 M stock in water.
Stoica R., Paillusson S., Gomez‐Suaga P., Mitchell J.C., Lau D.H., Gray E.H., Sancho R.M., Vizcay‐Barrena G., De Vos K.J., Shaw C.E., Hanger D.P., Noble W, & Miller C.C. (2016). ALS/FTD‐associated FUS activates GSK‐3β to disrupt the VAPB–PTPIP51 interaction and ER–mitochondria associations. EMBO Reports, 17(9), 1326-1342.
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5

Antibody Characterization for VAPB and PTPIP51

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Rabbit and rat antibodies to VAPB and PTPIP51 were as described [20 (link)]. Mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH), mouse anti-hemagglutinin (HA), mouse anti-myc 9B11 and rabbit anti-glycogen synthase kinase-3β (GSK3β) phosphorylated on serine-9 (inactive GSK3β) were from Cell Signalling. Rabbit anti-mitofusin-2, rabbit anti-HA, mouse anti-heat shock protein-60 (HSP60) and mouse anti-neurofilament heavy-chain (NFH) (N52) were from Sigma. Rabbit (sc-7011) and mouse (211) anti-α-synuclein, rabbit anti-translocase of the outer mitochondrial membrane protein-20 (TOM20), rabbit anti-fatty acid coenzyme A ligase long-chain 4 (FACL4) and mouse anti-Sigma-1 receptor were from Santa Cruz Biotechnology. Mouse anti-α-synuclein and mouse anti-calnexin were from BD Biosciences. Rabbit anti-EGFP and mouse anti-β-actin were from Abcam. Rabbit anti-PTPIP51 and chicken anti-MAP2 were from Genetex. Mouse anti-protein disulphide isomerase (PDI) was from Affinity Bioreagents, rabbit anti-myc was from Upstate and rabbit anti-GSK3β was from StressGen.
Paillusson S., Gomez-Suaga P., Stoica R., Little D., Gissen P., Devine M.J., Noble W., Hanger D.P, & Miller C.C. (2017). α-Synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production. Acta Neuropathologica, 134(1), 129-149.
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