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Anti axl c89e7

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Anti-AXL (C89E7) is a rabbit monoclonal antibody that recognizes the AXL receptor tyrosine kinase. AXL is a member of the TAM (Tyro3, AXL, MerTK) family of receptor tyrosine kinases and is involved in various cellular processes such as cell survival, proliferation, and migration.

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Lab products found in correlation

Mouse anti β actin mab, by Merck Group (1 mentions) Hrp conjugated goat anti rabbit igg secondary antibody, by Jackson ImmunoResearch (1 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (1 mentions) Bradford assay, by Thermo Fisher Scientific (1 mentions) Cd14 positive selection kit, by Miltenyi Biotec (1 mentions) Recombinant gm csf, by Miltenyi Biotec (1 mentions) Chemiluminescence assay, by Bio-Rad (1 mentions) Protease inhibitor cocktail, by Thermo Fisher Scientific (1 mentions) P atm ser1981, by Cell Signaling Technology (1 mentions) Lamin b m20, by Santa Cruz Biotechnology (1 mentions) Anti β actin, by Abcam (1 mentions) Alexa fluor 568 phalloidin, by Thermo Fisher Scientific (1 mentions) Anti β actin, by Merck Group (1 mentions) Anti phospho stat3 tyr705, by Cell Signaling Technology (1 mentions) Anti vimentin, by Merck Group (1 mentions) Anti e cadherin, by Cell Signaling Technology (1 mentions) Anti gapdh, by Santa Cruz Biotechnology (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Irdye 800 labeled goat anti mouse igg, by LI COR (1 mentions) Irdye 680 labeled goat anti rabbit igg, by LI COR (1 mentions)

Spelling variants of this product

Anti-AXL (11 citations) Rabbit anti-AXL (C89E7, (2 citations) Anti-AXL C89E7 rabbit mAb (2 citations)

4 protocols using anti axl c89e7

1

Quantifying Dendritic Cell Protein Expression

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5x106 cells were lysed in RIPA buffer in the presence of a protease inhibitor cocktail (ThermoFisher) for 30 min at 4°C. Protein concentration was determined by Bradford assay (ThermoFisher). Dendritic cells (DC) were derived from CD14pos peripheral blood monocytes (CD14 positive selection kit, Miltenyi) that were cultured for five days with 20 ng/ml recombinant GM-CSF (Miltenyi) and 50 ng/ml IL-13 (Sanofi-Aventis donation). Equal amounts of protein were resolved on 4-20% Mini Protean gradient gels (Bio-Rad Laboratories) then transferred to nitrocellulose membranes (ThermoFisher). Protein expression was analyzed using anti-AXL (C89E7, Cell Signaling Technology) or anti-DC-SIGN (D7F5C, Cell Signaling Technology) rabbit mAbs followed by HRP-conjugated Goat Anti-Rabbit IgG secondary antibody (Jackson ImmunoResearch). Blots were developed by chemiluminescence assay (Bio-Rad Laboratories). Anti-β-actin (mouse mAb, Sigma Aldrich) was used to confirm protein loading.
Espino A., Gouilly J., Chen Q., Colin P., Guerby P., Izopet J., Amara A., Tabiasco J., Al-Daccak R., El Costa H, & Jabrane-Ferrat N. (2022). The mechanisms underlying the immune control of Zika virus infection at the maternal-fetal interface. Frontiers in Immunology, 13, 1000861.
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2

Multimodal Protein Detection Protocol

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Anti-AXL (C89E7, Cell Signaling, Danvers, MA, USA), anti-β-actin (8226, Abcam, Cambridge, MA, USA) antibodies were used in western blot assays. Lamin B (M-20,Santa Cruz Biotechnology, Dallas, TX, USA), Alexa Fluor 568 Phalloidin (A12380, Thermo Fisher, Waltham, MA, USA), 53BP1 (4937S, Cell Signaling, Danvers, MA, USA), and p-ATM Ser-1981 (D25E5, Cell Signaling, Danvers, MA, USA) were used in immunofluorescence, and PE-conjugated anti-human AXL antibody (FAB154P, R&D Systems, Minneapolis, MN, USA) was used in the flow cytometry.
Batur T., Argundogan A., Keles U., Mutlu Z., Alotaibi H., Senturk S, & Ozturk M. (2021). AXL Knock-Out in SNU475 Hepatocellular Carcinoma Cells Provides Evidence for Lethal Effect Associated with G2 Arrest and Polyploidization. International Journal of Molecular Sciences, 22(24), 13247.
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3

Quantitative Immunoblotting of Signaling Proteins

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Antibodies used were anti-phospho-Stat3 (Tyr705) (Cell signaling Technology, Cat # 9145), anti-E-cadherin (Cell signaling Technology, Cat # 3195), anti-Occludin (BD Transduction Laboratories, Cat # 611091), anti-Vimentin (Millipore, Cat #CS207806), anti-β-Actin (Sigma, Cat #A1978), anti-GAPDH (Santacruz Biotechnology, Cat # Sc-365062), anti-phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (Cell signaling Technology, Cat #4370), anti-Axl (C89E7) (Cell signaling Technology, Cat #8661). Briefly, cells were rinsed in phosphate buffered saline (PBS) and lysed in lysis buffer (20 mM Tris-HCl, 150 mM NaCl, 1% Triton X-100 (v/v), 2 mM EDTA, pH 7.8 supplemented with 1 mM sodium orthovanadate, 1 mM phenylmethylsulfonyl fluoride (PMSF), 10 μg/ml aprotinin, and 10 μg/ml leupeptin). Protein concentrations were determined using the BCA protein assay (Pierce, Rockford, IL) and immunoblotting experiments were performed using standard procedures. For quantitative immunoblots, primary antibodies were detected with IRDye 680-labeled goat-anti-rabbit IgG or IRDye 800-labeled goat-anti-mouse IgG (LI-COR Biosciences, Lincoln, NE) at 1:5000 dilution. Bands were visualized and quantified using an Odyssey Infrared Imaging System (LI-COR Biosciences).
Golkowski M., Lau H.T., Chan M., Kenerson H., Vidadala V.N., Shoemaker A., Maly D.J., Yeung R.S., Gujral T.S, & Ong S.E. (2020). Pharmacoproteomics identifies kinase pathways that drive the epithelial-mesenchymal transition and drug resistance in hepatocellular carcinoma. Cell systems, 11(2), 196-207.e7.
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4

Cell Lysis and Western Blotting

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Cells were lysed at 4 °C using ice cold lysis buffer containing 30 mM Tris/HCl pH 6.7, 5% glycerol, 2.5% β-mercaptoethanol, and 1% SDS. Protein extracts were analyzed by SDS-PAGE and western blotting. Enhanced chemiluminescence (ECL) signals were detected as described before [38 (link)]. The following antibodies were used for western blot: anti-AXL C89E7 (Cell Signaling Technology, Boston, MA, USA), anti-CD68 (Cell Signaling Technology, Boston, MA, USA), anti-DICER1 clone D38E7 (Cell Signaling Technology, Boston, MA, USA), anti-SPRY4 (GeneTex, Irvine, CA, USA), pan-AGO clone 2A8 (Millipore, Overijse, Belgium), anti-vinculin E1E9V XP (Cell Signalling Technology, Boston, MA, USA), anti-alpha-tubulin (Santa Cruz, Heidelberg, Germany). HRP-labelled secondary antibodies were purchased from Cell Signaling Technology (Boston, MA, USA).
Kozar I., Philippidou D., Margue C., Gay L.A., Renne R, & Kreis S. (2021). Cross-Linking Ligation and Sequencing of Hybrids (qCLASH) Reveals an Unpredicted miRNA Targetome in Melanoma Cells. Cancers, 13(5), 1096.
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