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Mouse anti futsch

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Mouse anti-Futsch is a laboratory reagent used in research applications. It is an antibody that specifically binds to the Futsch protein, which is a microtubule-associated protein found in Drosophila. The antibody can be used to detect and study the localization and function of Futsch in experimental models.

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Lab products found in correlation

Anti mouse alexa fluor 488, by Thermo Fisher Scientific (1 mentions) Anti rat cy5, by Jackson ImmunoResearch (1 mentions) Rabbit anti dsred, by Takara Bio (1 mentions) Anti rabbit cy3, by Jackson ImmunoResearch (1 mentions) Anti mouse cy3, by Jackson ImmunoResearch (1 mentions) H 1000, by Vector Laboratories (1 mentions) Planapo objectives, by Zeiss (1 mentions) Lsm 510 inverted confocal microscope, by Zeiss (1 mentions) Alexa 488 conjugated goat anti mouse igg, by Jackson ImmunoResearch (1 mentions) Mouse anti th, by Merck Group (1 mentions) Goat anti rat cy3, by Jackson ImmunoResearch (1 mentions) Rabbit anti ha, by Cell Signaling Technology (1 mentions) Mouse anti ha f7, by Santa Cruz Biotechnology (1 mentions) Mouse anti gfp, by Developmental Studies Hybridoma Bank (1 mentions) Mouse anti brp, by Developmental Studies Hybridoma Bank (1 mentions) Alexa 488, by Thermo Fisher Scientific (1 mentions) Rabbit anti gfp, by Thermo Fisher Scientific (1 mentions) Lsm 510 meta microscope, by Zeiss (1 mentions) Rabbit anti ha, by Abcam (1 mentions)

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Mouse anti-Futsch (22C10; (5 citations) Anti-Futsch (3 citations)

6 protocols using mouse anti futsch

1

Antibody Staining of Drosophila Neuronal Markers

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We used rat anti-Drosophila N-Cadherin (1:10) and mouse anti-Futsch (22C10; 1:10) (Developmental Studies Hybridoma Bank). Other primary antibodies included rabbit anti-Plp (Martinez-Campos et al., 2004 (link); 1:500), rabbit anti-Asl (Varmark et al., 2007 (link); Novak et al., 2014 (link); 1:500)(all three antibodies generously gifted by Dr. J. Raff), mouse anti-Rh6 (Chou et al., 1999 (link);1:40; generously gifted by Dr. S. Britt), and rabbit anti-DsRed (1:100, Clontech # 632496). Secondary antibodies were anti-Rabbit Cy-3 (1:330) (Jackson ImmunoResearch), anti-Mouse Alexa Fluor 488 (1:1000) (Life Technologies), and anti-Rat Cy-5 (1:500) (Jackson ImmunoResearch), and anti-Mouse Cy-3 (1:300) (Jackson ImmunoResearch).
Hartenstein V., Yuan M., Younossi-Hartenstein A., Karandikar A., Bernardo-Garcia F.J., Sprecher S, & Knust E. (2019). Serial Electron Microscopic Reconstruction of the Drosophila Larval Eye: Photoreceptors with a Rudimentary Rhabdomere of Microvillar-Like Processes. Developmental biology, 453(1), 56-67.
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2

Larval Neuromuscular Junction Imaging

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Third-instar WCS and homozygous spastin5.75 or trans-heterozygous flowerDB25/DB56 larvae were filleted, dissected and immunostained using standard methods (e.g. Ozdowski et al., 2011 (link)). Briefly, larvae were dissected in room temperature PBS and fixed for 30 minutes in 4% paraformaldehyde, immunostained at 4°C overnight using the neuronal membrane marker rabbit anti-HRP (1:100; Jackson ImmunoResearch, PA, 323-005-021) alone or with mAb 22C10 to label microtubules (mouse anti-Futsch, 1:50; Developmental Studies Hybridoma Bank, University of Iowa, Iowa City, IA). Secondary antibodies (Alexa Fluor 488 goat anti-rabbit A-11070 and Alexa Fluor 568 goat anti-mouse A-11031; 1:400; Life Technologies, Grand Island, NY) were incubated for 2–3 hours at room temperature. Fillets were mounted in H-1000 (Vector Laboratories, Burlingame, CA) and z-series images of muscle 4 synapses from larval segments 2–4 acquired on a Zeiss LSM 510 inverted confocal microscope using 63× 1.4 N.A. or 100× 1.2 N.A. PlanApo objectives (Oberkochen, Germany).
Baxter S.L., Allard D.E., Crowl C, & Sherwood N.T. (2014). Cold temperature improves mobility and survival in Drosophila models of autosomal-dominant hereditary spastic paraplegia (AD-HSP). Disease Models & Mechanisms, 7(8), 1005-1012.
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3

Immunostaining and Confocal Imaging of Larval and Adult Brains

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Third instar wandering larvae or adult brains were dissected in PBS or PBT (0.3% Tween 20 in PBS), and incubated with fixative solution (4% formaldehyde in PBT) for 20 min, and immunostained with mouse anti-Futsch (Developmental Studies Hybridoma Bank) at 1:100 or mouse anti-TH (EMD Millipore Corporation) at 1:200 and Alexa 488-conjugated-goat anti-mouse IgG (Jackson ImmunoResearch Laboratories) at 1:500, or TRITC-conjugated-rabbit anti-HRP (Jackson ImmunoResearch Laboratories) at 1:100. Samples were imaged at room temperature (22°C) with a 20×/N.A.0.60 or a 63×/N.A.1.30 oil Plan-Apochromat objective on a Leica SPE laser scanning confocal microscope (JH Technologies), with identical imaging parameters among different genotypes in a blind fashion. For Figures 2C and 5B, the area of muscle 4 or 6/7 was measured and calculated under a Leica DFC365 FX CCD camera with brightfield 20× magnification. Images were processed with Photoshop CS4 using only linear adjustments of contrast and color.
Tsai P.I., Course M.M., Lovas J.R., Hsieh C.H., Babic M., Zinsmaier K.E, & Wang X. (2014). PINK1-mediated Phosphorylation of Miro Inhibits Synaptic Growth and Protects Dopaminergic Neurons in Drosophila. Scientific Reports, 4, 6962.
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4

Visualizing Larval Body Wall Anatomy

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Third instar larvae were dissected to generate body wall filets, and then fixed in 4% paraformaldehyde. Staining was performed as described (Koch et al. 2008 (link)) using rabbit anti-Ank2XL at 1:1000. Microtubules were stained with the 22C10 primary antibody (1:100 mouse anti-futsch, from the Developmental Studies Hybridoma Bank). Goat secondary antibodies were obtained from Jackson ImmunoResearch.
Weiner A.T., Lanz M.C., Goetschius D.J., Hancock W.O, & Rolls M.M. (2016). Kinesin-2 and Apc function at dendrite branch points to resolve microtubule collisions. Cytoskeleton (Hoboken, N.J.), 73(1), 35-44.
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5

Immunohistochemistry and TEM of Larval Neurons

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The wandering larvae were dissected and prepared for immunohistochemistry as described previously (Shrestha and Grueber, 2011 (link)). Primary antibodies used in immunostaining included rat anti-CCT1 (1:50, Abcam), mouse anti-Futsch (1:200, Developmental Studies Hybridoma Bank), rabbit anti-GFP-Alexa488 (1:500, Life Technologies), and rabbit anti-HA (1:400; Cell Signaling Technology). Goat anti-rat Cy3 and anti-mouse Cy3 secondary antibodies were obtained from Jackson ImmunoResearch Laboratories Inc. Wandering larvae were dissected and prepared for TEM experiments as described previously (Yang et al., 2019 (link)).
Wang Y.H., Ding Z.Y., Cheng Y.J., Chien C.T, & Huang M.L. (2020). An Efficient Screen for Cell-Intrinsic Factors Identifies the Chaperonin CCT and Multiple Conserved Mechanisms as Mediating Dendrite Morphogenesis. Frontiers in Cellular Neuroscience, 14, 577315.
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6

Dissection and Immunolabeling of Larval Nervous System

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Larvae were dissected as filets preparations to preserve the fine structure of the whole nervous system and fixed for 20 min in 4% paraformaldehyde (PFA) or for 3 min in Bouins’s solution (Sigma-Aldrich) followed by standard immuno-labeling procedures. The following antibodies were used: rabbit anti-GFP (1:1000, LifeTechnologies), mouse anti-repo (1D48D12, 1:100), mouse anti-GFP (12A6,1:500), mouse anti-Brp (nc82,1:250), mouse anti-Futsch (22C10,1:250) all from Developmental Studies Hybridoma Bank; rabbit anti-p24-1 (kind gift from G. Carnery; Texas A&M University, US), mouse anti-HA (F7, 1:100, Santa Cruz) and rabbit anti-HA (#9110,1:250, Abcam), and anti-HRP-Alexa637 (1:300, Jackson Immuno Research). Secondary antibodies with Alexa 488, Alexa555 or Alexa647 conjugate (LifeTechnologies) were used in a dilution of 1:1000. Samples were mounted in VectaShield anti fade reagent (H-1000, Vector Laboratories). Confocal images were taken with Zeiss LSM 510 Meta microscope.
Mukherjee C., Kling T., Russo B., Miebach K., Kess E., Schifferer M., Pedro L.D., Weikert U., Fard M.K., Kannaiyan N., Rossner M., Aicher M.L., Goebbels S., Nave K.A., Krämer-Albers E.M., Schneider A, & Simons M. (2020). Oligodendrocytes Provide Antioxidant Defense Function for Neurons by Secreting Ferritin Heavy Chain. Cell metabolism, 32(2), 259-272.e10.
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