Clone 6f 3d

Manufactured by Agilent Technologies

Sourced in Denmark

The Clone 6F/3D is a laboratory instrument designed for cell culture applications. It is used for the automated cloning and expansion of cell lines. The device facilitates the isolation, propagation, and maintenance of individual cell colonies, enabling efficient cell line development.

Automatically generated - may contain errors

Lab products found in correlation

Em 109, by Zeiss (1 mentions) Nanozoomer 2.0 ht, by Hamamatsu Photonics (1 mentions) Anti p62, by BD (1 mentions) Anti aβ, by Agilent Technologies (1 mentions) Anti phospho tdp 43 ps409 410, by Cosmo Bio (1 mentions) Anti tau at8 ps202 pt205, by Thermo Fisher Scientific (1 mentions) Discovery xt, by Roche (1 mentions) Dab map kit, by Roche (1 mentions) Envision flex hrp, by Agilent Technologies (1 mentions) Clone at8, by Thermo Fisher Scientific (1 mentions) Alexa fluor 488 anti chicken, by Thermo Fisher Scientific (1 mentions) Mouse anti smi312, by BioLegend (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Southern Biotech (1 mentions) Mouse anti gfap cy3, by Merck Group (1 mentions) Anti mouse cy3, by Thermo Fisher Scientific (1 mentions) Anti rabbit alexa fluor 647, by Thermo Fisher Scientific (1 mentions) Axiovert, by Zeiss (1 mentions)

9 protocols using clone 6f 3d

Cortical Brain Biopsy and Tau-Amyloid Staining

Check if the same lab product or an alternative is used in the 5 most similar protocols

A cortical brain biopsy was performed at the entry point of one of four implants (at a cortical gyrus of the frontal lobe, 20 mm anterior to the coronary suture and 30–50 mm lateral to midline) in each patient. Tissue was immediately fixed in 4 % paraformaldehyde solution, and 5-μm-thick paraffin sections were cut and stained with antibodies against hyperphosphorylated tau (clone AT-8, 1:500 dilution; Fujirebio Europe, Zwijnaarde, Belgium) and β-amyloid (clone 6F/3D, 1:400 dilution; DakoCytomation, Glostrup, Denmark). The product was visualized using the Zymed Lab-SA detection system (Life Technologies).

Eyjolfsdottir H., Eriksdotter M., Linderoth B., Lind G., Juliusson B., Kusk P., Almkvist O., Andreasen N., Blennow K., Ferreira D., Westman E., Nennesmo I., Karami A., Darreh-Shori T., Kadir A., Nordberg A., Sundström E., Wahlund L.O., Wall A., Wiberg M., Winblad B., Seiger Å., Wahlberg L, & Almqvist P. (2016). Targeted delivery of nerve growth factor to the cholinergic basal forebrain of Alzheimer’s disease patients: application of a second-generation encapsulated cell biodelivery device. Alzheimer's Research & Therapy, 8, 30.

+ Open protocol

+ Expand

Histologic and Ultrastructural Assessment of Amyloid

Check if the same lab product or an alternative is used in the 5 most similar protocols

Histologic assessment was based on conventional Hematoxylin Eosin and Congo red stainings as well as immunohistochemistry for beta A4-amyloid (1:400, clone 6 F/3D, Dako, Glostrup, Denmark). Slides were assessed using a Nikon Eclipse 80i microscope (camera: Jenoptik ProgRes C5) comprising bright field and polarization contrast microscopy. For electron microscopy small areas of temporal cortex were postfixed in 1% osmium tetroxide for 1–2 hours, dehydrated through a series of graded ethanols and propylene oxide, and then embedded in Embed 812 resin. Ultrathin sections were stained with lead citrate and uranyl acetate. Specimens were examined using a transmission electron microscope (Carl Zeiss EM 109).

Baumann B., Woehrer A., Ricken G., Augustin M., Mitter C., Pircher M., Kovacs G.G, & Hitzenberger C.K. (2017). Visualization of neuritic plaques in Alzheimer’s disease by polarization-sensitive optical coherence microscopy. Scientific Reports, 7, 43477.

+ Open protocol

+ Expand

Quantitative Analysis of Amyloid-Beta Plaques in Mouse Brain

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

The mouse brains were sagittally cut into two hemispheres, and one hemisphere was prepared for histopathological workup. The samples were fixed in 4% formalin and processed through graded alcohols and xylene into paraffin. Sagittal brain sections with a thickness of

2.5 μ m

were cut on a microtome, deparaffinized, rehydrated, and stained immunohistochemically using an anti-

A β

antibody (clone 6F/3D, diluted 1:100, Dako). The sections were evaluated using a slide scanner (Hamamatsu NanoZoomer 2.0 HT) and saved for digital pathology. The images were analyzed using Fiji.⁷⁴ (link) First, the cortex was manually selected and the “ColSeg” tool⁷⁵ (link) was utilized to segment the plaques by their brown color. The “analyze particle” tool was then used to count the plaque number and calculate the plaque load in plaques per

{mm}^{2}

. The plaque load was then plotted as a function of mouse age, and a linear regression analysis was performed on the data.

Harper D.J., Augustin M., Lichtenegger A., Gesperger J., Himmel T., Muck M., Merkle C.W., Eugui P., Kummer S., Woehrer A., Glösmann M, & Baumann B. (2020). Retinal analysis of a mouse model of Alzheimer’s disease with multicontrast optical coherence tomography. Neurophotonics, 7(1), 015006.

+ Open protocol

+ Expand

Comprehensive Neurodegeneration Immunohistochemistry

Check if the same lab product or an alternative is used in the 5 most similar protocols

Formalin fixed, paraffin-embedded tissue blocks from neocortical areas, basal ganglia, thalamus, hippocampus, brainstem and cerebellum were evaluated. In addition to Hematoxylin and Eosin staining, the following monoclonal (mouse) antibodies were used for immunohistochemistry: monoclonal anti-p62 (1:1,000, BD Transduction, Lexington KY, USA), anti-tau AT8 (pS202/pT205, 1:200, Pierce Biotechnology, Rockford, IL, USA), anti-phospho-TDP-43 (pS409/410, 1:2,000, Cosmo Bio, Tokyo, Japan), anti-α-synuclein (1:2,000, clone 5G4, Roboscreen, Leipzig, Germany; specific for disease-associated form), anti-Aβ (1:50, clone 6F/3D, Dako, Glostrup, Denmark). The DAKO EnVision© detection kit, peroxidase/DAB, rabbit/mouse (Dako, Glostrup, Denmark) was used for visualization of the antibody reactions.

van der Zee J., Van Langenhove T., Kovacs G.G., Dillen L., Deschamps W., Engelborghs S., Matěj R., Vandenbulcke M., Sieben A., Dermaut B., Smets K., Van Damme P., Merlin C., Laureys A., Van Den Broeck M., Mattheijssens M., Peeters K., Benussi L., Binetti G., Ghidoni R., Borroni B., Padovani A., Archetti S., Pastor P., Razquin C., Ortega-Cubero S., Hernández I., Boada M., Ruiz A., de Mendonça A., Miltenberger-Miltényi G., do Couto F.S., Sorbi S., Nacmias B., Bagnoli S., Graff C., Chiang H.H., Thonberg H., Perneczky R., Diehl-Schmid J., Alexopoulos P., Frisoni G.B., Bonvicini C., Synofzik M., Maetzler W., vom Hagen J.M., Schöls L., Haack T.B., Strom T.M., Prokisch H., Dols-Icardo O., Clarimón J., Lleó A., Santana I., Almeida M.R., Santiago B., Heneka M.T., Jessen F., Ramirez A., Sanchez-Valle R., Llado A., Gelpi E., Sarafov S., Tournev I., Jordanova A., Parobkova E., Fabrizi G.M., Testi S., Salmon E., Ströbel T., Santens P., Robberecht W., De Jonghe P., Martin J.J., Cras P., Vandenberghe R., De Deyn P.P., Cruts M., Sleegers K, & Van Broeckhoven C. (2014). Rare mutations in SQSTM1 modify susceptibility to frontotemporal lobar degeneration. Acta Neuropathologica, 128(3), 397-410.

+ Open protocol

+ Expand

Immunocytochemical Analysis of Amyloid-Beta Plaques

Check if the same lab product or an alternative is used in the 5 most similar protocols

Immunocytochemical assays were run as described before [16 (link)]. Animals were deeply anesthetized with pentobarbital (50 mg/kg) and perfused transcardially with 4% paraformaldehyde in 0.1 M phosphate buffer, pH 7.4 (PB). Coronal 50-μm-thick brain sections were cut in a vibratome and collected in PBS. Sections were incubated with 100% methanol and 0.03% H₂O₂ to eliminate endogenous peroxidase followed by incubation overnight at 4°C with primary antibody in PB- 1% bovine albumin- 1% Triton X-100. For immunocytochemistry of Aß plaques, a pre-treatment of 70% formic acid was used before incubation with anti-human Aß antibody (1:50, Dako clone 6F/3D). After several washes in PB, sections were incubated with a biotin-coupled secondary antibody (1:500, Pierce) followed by ABC amplification system (1:250, Pierce) using diaminobenzidine as chromogen. Sections were dehydrated and mounted with DEPEX. Omission of primary antibody was used as control. Panoramic pictures were obtained with a Leica (Germany) microscope using the stitching tool.

Miki Stein A., Munive V., Fernandez A.M., Nuñez A, & Torres Aleman I. (2017). Acute exercise does not modify brain activity and memory performance in APP/PS1 mice. PLoS ONE, 12(5), e0178247.

+ Open protocol

+ Expand

Immunohistochemical Detection of Amyloid-Beta and SAP

Check if the same lab product or an alternative is used in the 5 most similar protocols

Immunoperoxidase histochemistry was performed on a Ventana Discovery XT staining platform using the Ventana DAB Map Kit. Wax sections of formalin fixed tissue were pretreated with formic acid (for Aβ staining) or with Ventana Protease 3 (for SAP staining) and blocked for 8 min using Superblock (Medite). A mouse monoclonal primary antibody was used for detection of Aβ (Dako, clone 6F-3D), and an in-house monospecific polyclonal rabbit antiserum was used to detect human SAP, and counterstained with haematoxylin. Immunofluorescence histochemistry was performed on 14 µm frozen sections of unfixed frozen mouse brains. Sections were dried at room temperature and stored at −20°C before use. Non-specific binding was blocked with 2% w/v BSA, 0.1% Triton X-100 in PBS, and SAP was then detected with the monospecific rabbit anti-human SAP antibody followed by Alexa-488 labelled anti-rabbit IgG antibody, followed by counterstaining with bisbenzimide.

Al-Shawi R., Tennent G.A., Millar D.J., Richard-Londt A., Brandner S., Werring D.J., Simons J.P, & Pepys M.B. (2016). Pharmacological removal of serum amyloid P component from intracerebral plaques and cerebrovascular Aβ amyloid deposits in vivo. Open Biology, 6(2), 150202.

+ Open protocol

+ Expand

Immunohistochemical Profiling of Neurodegenerative Markers

Check if the same lab product or an alternative is used in the 5 most similar protocols

Paraffin-embedded tissue sections (4 μm) from different regions (Table 2) were examined using routine hematoxylin-eosin and luxol-eosin stains. Immunohistochemistry was performed using antibodies against hyperphosphorylated tau protein (clone AT8, 1:500, Thermo Scientific), 4R-tau isoform (RD4, clone 1E1/AG, 1:200, Upstate), 3R-tau isoform (RD3, clone 8E6/C11, 1:500, Upstate), p62 (clone GP62, 1:4000, PROGEN), and ubiquitin (polyclonal, 1:500, Dako) with low-pH citrate buffer epitope retrieval. Moreover, antibodies against amyloid-beta (clone 6F/3D, 1:100, Dako), alpha-synuclein (4D6, 1:10000, Signet), and phospho-TDP-43 (clone 11/9, 1:4000, CosmoBio), were used in the context of a differential diagnostic workup. Subsequent visualization of all antibodies was performed using a horseradish peroxidase–diaminobenzidine system (Envision FLEX/HRP, polyclonal rabbit-anti-guinea pig; Dako).

Stejskalova Z., Rohan Z., Rusina R., Tesar A., Kukal J., Kovacs G.G., Bartos A, & Matej R. (2019). Pyramidal system involvement in progressive supranuclear palsy – a clinicopathological correlation. BMC Neurology, 19, 42.

+ Open protocol

+ Expand

Multimodal Neuron and Glia Imaging

Check if the same lab product or an alternative is used in the 5 most similar protocols

For immunofluorescent labeling of transduced neurons, glia cells, and Aβ plaques, floating brain sections were rinsed in PBS, permeabilized with 0.2% Triton X-100/TBS for 20 min at room temperature, blocked in 3 to 5% normal goat serum (NGS) in PBS for 1 hour at room temperature, and then incubated with primary antibodies diluted in 3% NGS/PBS overnight at 4°C: chicken anti-GFP (1:1000; Aves, #GFP-1020), mouse anti-GFAP-cy3 (astrocytes; 1:1000; Sigma-Aldrich, #C9205), rabbit anti-Iba1 (microglia; 1:500; Wako, #019-19741), rabbit anti-Olig2 (oligodendrocytes; 1:500; Abcam, #ab136253), mouse anti-SMI312 (1:500; BioLegend, #837904), and mouse anti–Aβ (amyloid plaques; 1:200; clone 6F/3D, Dako). After washing three times with PBS, secondary antibodies diluted 1:1000 in 3% NGS/PBS were applied for 1.5 hours at room temperature: Alexa Fluor 488 anti-chicken, Cy3 anti-mouse, Alexa Fluor 647 anti-rabbit, and Alexa Fluor 450 anti-mouse (Thermo Fisher Scientific). After three washes in PBS, sections were mounted on microscope glass slides with mounting media containing DAPI (4′,6-diamidino-2-phenylindole; SouthernBiotech). Imaging of immunolabeled sections was done on a Zeiss Axiovert equipped with a QuickSnap camera or on an Olympus BX5.

Wegmann S., DeVos S.L., Zeitler B., Marlen K., Bennett R.E., Perez-Rando M., MacKenzie D., Yu Q., Commins C., Bannon R.N., Corjuc B.T., Chase A., Diez L., Nguyen H.O., Hinkley S., Zhang L., Goodwin A., Ledeboer A., Lam S., Ankoudinova I., Tran H., Scarlott N., Amora R., Surosky R., Miller J.C., Robbins A.B., Rebar E.J., Urnov F.D., Holmes M.C., Pooler A.M., Riley B., Zhang H.S, & Hyman B.T. (2021). Persistent repression of tau in the brain using engineered zinc finger protein transcription factors. Science Advances, 7(12), eabe1611.

+ Open protocol

+ Expand

Characterization of Proteinase K-Resistant α-Synuclein in Parkinson's Disease

Check if the same lab product or an alternative is used in the 5 most similar protocols

To evaluate proteinase K–resistant α-syn contained in noLB and LB fractions derived from PD brains, we subjected each fraction to digestion with proteinase K (1 μg/ml) for 0, 15, 30, 45, and 60 min. The reaction was stopped by boiling for 5 min before dot blotting with syn211 antibody. To analyze their stability, we treated noLB and LB fractions with increasing concentrations of urea (7 and 8 M) or SDS (0.5, 1, and 2%) for 6 hours at room temperature. α-Syn was visualized as described above.
Filter retardation assay of noLB and LB fractions was probed with antibodies against phosphorylated α-syn (Abcam, EP1536Y; 1:1000), ubiquitin (Sigma-Aldrich, U5379; 1:1000), p62 (Progen, GR62-C; 1:1000), hyperphosphorylated tau (AT8, Thermo Fisher Scientific, MN1020), or Aβ (clone 6F/3D, DAKO; 1:1000).

Bourdenx M., Nioche A., Dovero S., Arotcarena M.L., Camus S., Porras G., Thiolat M.L., Rougier N.P., Prigent A., Aubert P., Bohic S., Sandt C., Laferrière F., Doudnikoff E., Kruse N., Mollenhauer B., Novello S., Morari M., Leste-Lasserre T., Trigo-Damas I., Goillandeau M., Perier C., Estrada C., Garcia-Carrillo N., Recasens A., Vaikath N.N., El-Agnaf O.M., Herrero M.T., Derkinderen P., Vila M., Obeso J.A., Dehay B, & Bezard E. (2020). Identification of distinct pathological signatures induced by patient-derived α-synuclein structures in nonhuman primates. Science Advances, 6(20), eaaz9165.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!