Rabbit antibodies

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit antibodies are a type of immunoglobulin (Ig) produced by rabbits in response to foreign antigens. They are commonly used in various research and diagnostic applications, such as Western blotting, immunohistochemistry, and ELISA. Rabbit antibodies offer high specificity and sensitivity, making them a valuable tool for the detection and analysis of target proteins.

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Lab products found in correlation

Cftm770 goat anti rabbit igg, by Biotium (2 mentions) Lsm 510, by Zeiss (2 mentions) Chamber slide, by Thermo Fisher Scientific (1 mentions) Dapi containing mounting medium, by Vector Laboratories (1 mentions) Alexaflour 488 secondary antibodies, by Thermo Fisher Scientific (1 mentions) Beclin 1, by Cell Signaling Technology (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Anti–mouse or anti–rabbit IgG HRP‐linked secondary antibodies Rabbit anti-Bcl2 antibodies Rabbit anti-human antibodies Secondary antibodies against rabbit or mouse IgG conjugated to horseradish peroxidase Peroxidase labeled anti‐rabbit or anti‐mouse secondary antibodies HRP-labeled goat-anti-rabbit or goat-anti-mouse secondary antibodies HRP-conjugated goat anti-rabbit and anti-mouse IgG antibodies Rabbit anti-Bax and anti-caspase-3 antibodies HRP-conjugated anti-rabbit and anti-mouse IgG antibodies Alexa 488-conjugated anti-rabbit secondary antibodies

6 protocols using rabbit antibodies

Western Blot Analysis of Cell Markers

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Western blots were performed as previously described according to the manufacturer's instructions (Mees et al, 2010 (link)).
FZD5, E-cadherin and β-catenin were detected with rabbit antibodies (Cell Signaling Technology, Danvers, MA, USA). HNF1B was detected with a mouse antibody (Santa Cruz Biotechnology, Dallas, TX, USA) and TMEM92 was detected with a goat antibody (Santa Cruz Biotechnology). Four exemplary cell lines were used for each group with actin as the reference.

Listing H., Mardin W.A., Wohlfromm S., Mees S.T, & Haier J. (2014). MiR-23a/-24-induced gene silencing results in mesothelial cell integration of pancreatic cancer. British Journal of Cancer, 112(1), 131-139.

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Visualizing Endothelial Cell Junctions

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Immunofluorescence staining of HMEC monolayers was performed using chamber slides (Fisher, Hanover Park, IL). Cells were cultured to monolayer, treated with either vector or 20 ng/ml VEGF or 50 ng/ml Ang-1 and co-treated with either 10 μM Triciribine (TCBN) or 1 μM pp-2 for 24 hours and washed twice with ice-cold PBS, fixed using 2% paraformaldehyde for 30 min, permeabilized with 0.1% Triton X-100 for 15 min, and blocked with 2% BSA in sterile PBS for 1 hour. Cell monolayers were then incubated with antibodies against VE-cadherin (1:100, Rabbit antibodies, Cell Signaling, Danvers, MA) at 4°C overnight. Immunofluorescence was revealed using goat anti-rabbit AlexaFlour-488 secondary antibodies (1:2000, Life Technologies, Grand Island, NY). Cells were mounted on to a glass slide using DAPI containing mounting medium (Vector Laboratories, PA). Images were captured using a confocal microscope equipped with argon and helium/neon lasers (LSM510, Zeiss, Germany). Controls were performed by omitting primary antibodies. All controls gave negative results with no detectable non-specific labeling.

Gao F., Sabbineni H., Artham S, & Somanath P.R. (2017). Modulation of long-term endothelial-barrier integrity is conditional to the cross-talk between Akt and Src signaling. Journal of cellular physiology, 232(10), 2599-2609.

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Cell Autophagy Induction Protocol

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CQ and DDP were purchased from Sigma-Aldrich (St Louis, MO, USA). The human ACC SW13 cell line was obtained from the Chinese Academy of Sciences (Shanghai, People’s Republic of China). The antibodies used in the experiments included the following: rabbit antibodies against Beclin-1, LC3, Bax, and GAPDH (all from Cell Signaling Technology, Danvers, MA, USA), rabbit antibodies against Bcl-2 (Abcam, Cambridge, UK), and rabbit antibodies against p62 (Proteintech, Chicago, IL, USA). Nude BALB/c mice (4 weeks old, male, 16–20 g) were obtained from the Shanghai Experimental Animal Center, Chinese Academy of Sciences (Shanghai, People’s Republic of China).

Qin L., Xu T., Xia L., Wang X., Zhang X., Zhang X., Zhu Z., Zhong S., Wang C, & Shen Z. (2016). Chloroquine enhances the efficacy of cisplatin by suppressing autophagy in human adrenocortical carcinoma treatment. Drug Design, Development and Therapy, 10, 1035-1045.

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Western Blot Analysis of P-STAT3 in A549 Cells

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Proteins in A549 cell lysates were electrophoretically separated on sodium dodecyl sulfate polyacrylamide gels and transferred onto polyvinylidene difluoride membranes. After being blocked with 5% nonfat dry milk in 0.1% Tween 20 in tris-buffered saline, the membranes were incubated with rabbit antibodies (1:1,000 dilution; Cell Signaling Technology, United States) for phospho-signal transducer and activator of transcription 3 (P-STAT3) (Tyr705) or GAPDH at 4°C overnight. The membranes were washed three times with 0.1% Tween 20 in tris-buffered saline and subsequently incubated with horseradish peroxidase conjugated goat anti-rabbit IgG (1:2,000 dilution) for 2 h at room temperature. The membranes were washed three times, and target proteins were visualized with enhanced chemiluminescent solution detection reagents (Bio-Rad, United States) on a GeneGnome HR image capture (Cambridge, UK).

Tang W.D., Tang H.L., Peng H.R., Ren R.W., Zhao P, & Zhao L.J. (2023). Inhibition of tick-borne encephalitis virus in cell cultures by ribavirin. Frontiers in Microbiology, 14, 1182798.

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Phosphorylation of MAPK p38 and JNK in Caco-2 Cells

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Expression of the phosphorylated MAPK p38 and JNK (Jun amino-terminal kinases) was assessed on differentiated Caco-2 cells and jejunal explants by immunoblotting as previously described49 (link)54 (link). Cells differentiated on 24-well inserts or explants were treated with 10 μM of diluent (DMSO) or toxins, DON, deepoxy-DON or 3-epi-DON for 1 hour. Proteins were extracted, quantified and a total of 15 μg of protein was separated by SDS-PAGE. The membranes were probed with rabbit antibodies (Cell Signaling Technology, Danvers, USA) specific for: phospho-SPAK/JNK or phospho-p38 diluted at 1:500 or GAPDH diluted at 1:1000. After washing, the membranes were incubated with 1:10,000 CF^TM770 goat anti-rabbit IgG (Biotium, Hayward, USA) for the detection. Antibody detection was performed using an Odyssey Infrared Imaging Scanner (Li-Cor Science Tec, les Ulis, France) with the 770 nm channel. The expression of the proteins was estimated after normalization with GAPDH signal.

Pierron A., Mimoun S., Murate L.S., Loiseau N., Lippi Y., Bracarense A.P., Schatzmayr G., He J.W., Zhou T., Moll W.D, & Oswald I.P. (2016). Microbial biotransformation of DON: molecular basis for reduced toxicity. Scientific Reports, 6, 29105.

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MAPK Signaling Pathway in Caco2 Cells

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Caco2 cells differentiated on 24-well format (same process that for TEER), were treated with 10 µM of DMSO for control, D3G or DON for 1 hour to analyze the expression of the total and phosphorylated MAPK P38 and JNK. Proteins were extracted from cells as previously described (Pinton et al. 2009 (link)) quantified and 15 µg of total proteins was separated by SDS-PAGE. The membranes were probed with rabbit antibodies (Cell Signaling Technology, Danvers, USA) specific for: SAPK/JNK and phospho-SPAK/JNK or p38 and phospho-p38 diluted at 1:500 or GAPDH diluted at 1:1000. After washing, the membranes were incubated with 1:10,000 CF TM 770 goat anti-rabbit IgG (Biotium, Hayward, USA) for the detection. Antibody detection was performed using an Odyssey Infrared Imaging Scanner (Li-Cor Science Tec, les Ulis, France) with the 770nm channel. The expression of the proteins was estimated after normalization with GAPDH signal. Three independent experiments were proceeding for each cell culture condition.

Pierron A., Mimoun S., Murate L.S., Loiseau N., Lippi Y., Bracarense A.P., Liaubet L., Schatzmayr G., Berthiller F., Moll W.D, & Oswald I.P. (2016). Intestinal toxicity of the masked mycotoxin deoxynivalenol-3-β-D-glucoside. Archives of toxicology, 90(8).

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