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Anti rab11

Manufactured by Cell Signaling Technology
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Anti-Rab11 is an antibody that specifically binds to the Rab11 protein, a member of the Ras superfamily of small GTPases. Rab11 is involved in the regulation of endocytic recycling pathways. The Anti-Rab11 antibody can be used to detect and study the localization and expression of Rab11 in various cellular and experimental contexts.

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Lab products found in correlation

Anti rab8a, by Cell Signaling Technology (3 mentions) Anti rab7, by Cell Signaling Technology (3 mentions) Anti rab5, by Cell Signaling Technology (3 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (3 mentions) Cellevent caspase 3 7 green detection reagent, by Thermo Fisher Scientific (3 mentions) Anti gja1, by Thermo Fisher Scientific (2 mentions) Anti ha, by Santa Cruz Biotechnology (2 mentions) Anti lamp1, by Abcam (2 mentions) Anti eea1, by BD (1 mentions) Anti calnexin, by Enzo Life Sciences (1 mentions) Anti giantin, by Abcam (1 mentions) Anti tgn46, by Merck Group (1 mentions) Anti lamp1, by BD (1 mentions) Anti rab7, by Santa Cruz Biotechnology (1 mentions) Anti β1 integrin, by R&D Systems (1 mentions) Ibright imaging system, by Thermo Fisher Scientific (1 mentions) Anti α actin, by Thermo Fisher Scientific (1 mentions) Horseradish peroxidase conjugated anti mouse or anti rabbit igg antibodies, by Thermo Fisher Scientific (1 mentions) Supersignal west dura extended duration substrate, by Thermo Fisher Scientific (1 mentions) Polyvinylidene fluoride membrane, by Merck Group (1 mentions)

Close spelling variants of this product

Anti-Rab11 (D4F5) (2 citations) Rabbit anti-Rab11 (7 citations) Rab11 (24 citations)

14 protocols using anti rab11

1

Immunofluorescence Assay for Organelle Markers

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Immunofluorescence studies were carried out as previously described [24] (link). Briefly, cells grown overnight on 24-well cover glasses (Menzel, 12 mm) were treated with Cy2/Cy3-labeled MOA in FCS-containing medium and fixed in 4% paraformaldehyde (PFA) at 4 °C for 10 min. Cells were washed and incubated with NH4Cl at room temperature for 15 min before being permeabilized with PBS containing 0.02% saponin and 0.2% bovine serum albumin (BSA). Cells were stained with either anti-EEA1 (1:50, BD Transduction Laboratories), anti-Calnexin (1:100, Enzo Life Science), anti-CTR 433 (1:100, kind gift of Michel Bornens, Curie Institut), anti-Giantin (1:100, Abcam), anti-TGN46 (1:100, Sigma Aldrich), anti-Transferrin receptor (TfR, 1:100, Life Technologies), anti-Rab11 (1:100, Cell Signaling), anti-Lamp1 (1:200, BD PharMingen), anti-Rab7 (1:100, Santa Cruz Biotech) or anti-β1 integrin (1:100, R&D Systems) antibodies diluted in permeabilization buffer, followed by either donkey anti-mouse Cy3-labeled secondary antibody (1:100, Jackson ImmunoResearch), donkey anti-rabbit Cy3-labeled secondary antibody (1:100, Jackson ImmunoResearch) or donkey anti-goat Cy3-labeled secondary antibody (1:100, Jackson ImmunoResearch) diluted in permeabilization buffer. Nuclei were stained using DAPI (300 nM, Life Technologies).
Juillot S., Cott C., Madl J., Claudinon J., van der Velden N.S., Künzler M., Thuenauer R, & Römer W. (2016). Uptake of Marasmius oreades agglutinin disrupts integrin-dependent cell adhesion. Biochimica et Biophysica Acta, 1860(2), 392-401.
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2

Immunoblotting of Cell Lysates

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Xenopus or human RPE1 immunoblotting samples were prepared with modified lysis buffer (TBS, 1% Triton X-100, and 10% glycerol with protease inhibitor). After removing fat and cellular debris, a sodium dodecyl sulfate (SDS) sample buffer with dithiothreitol (DTT) was added. Samples were loaded on SDS-polyacrylamide gels and transferred to polyvinylidene fluoride membranes (Merck Millipore, MA, USA). Membranes were incubated in blocking solution (TBS, 0.05% Tween-20 with non-fat powdered milk) for 30 min at room temperature to block non-specific binding. Immunoblotting was performed with the following antibodies at 1:2,500–3,000 dilutions for either 1 hr at room temperature or overnight at 4°C: anti-DDDD-K (Abcam, ab1162), anti-α-actin (ThermoFisher Scientific, MA1-744), anti-α-tubulin (Abcam, ab15246), anti-GJA1 (ThermoFisher Scientific, PA1-25098), anti-HA (Santa Cruz, sc-7392), anti-Rab8a (Cell Signaling, #6975), and anti-Rab11 (Cell Signaling, #5589). Secondary labeling was performed using horseradish peroxidase-conjugated anti-mouse or anti-rabbit IgG antibodies (1:3000, both ThermoFisher Scientific, 31430, 31460) for 1 hr at room temperature. Chemiluminescence was performed with SuperSignal West Dura Extended Duration Substrate (ThermoFisher Scientific, 34076), and the membranes were imaged with an iBright imaging system (FL1000, ThermoFisher Scientific).
Jang D.G., Kwon K.Y., Kweon Y.C., Kim B.G., Myung K., Lee H.S., Young Park C., Kwon T, & Park T.J. (2022). GJA1 depletion causes ciliary defects by affecting Rab11 trafficking to the ciliary base. eLife, 11, e81016.
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3

Western Blot and Flow Cytometry Analysis of Hepatitis B Virus Antigen and ER Proteins

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For western blot analysis, HBs antigen and calnexin were detected with goat anti-HBV polyclonal antibody (Murex, DiaSorin) coupled to horseradish peroxidase (HRP) and rabbit calnexin polyclonal antibody (Enzo), respectively. The rabbit anti-ERp46 (Abcam), mouse anti-ERp57 (Abcam), and mouse anti-ERp72 (Santa Cruz Biotechnology) antibodies were used for detecting PDI proteins by flow cytometry and western blot. NTCP was detected with polyclonal NTCP/SLC10A1 antibody (Bioss Antibodies) coupled to Phycoerythrin (PE) for flow cytometry. mouse anti-ERp57 (Abcam), Rabbit anti-Rab5, anti-Rab7, anti-Rab11, and anti-Lamp1 (Cell Signaling Technology), and Donkey anti-Rabbit-Alexa-Fluor-488 and Donkey anti-Mouse-Alexa-Fluor-568 (Thermo Fisher) antibodies were used for immunofluorescence (IF) studies.
Pérez-Vargas J., Teppa E., Amirache F., Boson B., Pereira de Oliveira R., Combet C., Böckmann A., Fusil F., Freitas N., Carbone A, & Cosset F.L. (2021). A fusion peptide in preS1 and the human protein disulfide isomerase ERp57 are involved in hepatitis B virus membrane fusion process. eLife, 10, e64507.
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4

Endocytic Trafficking Mechanisms Study

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Dynasore was obtained from Sigma-Aldrich. AlexaFluor 488-albumin from bovine serum conjugate, TexasRed-dextran (70,000 MW) lysine fixable, and AlexaFluor594-transferrin were from ThermoFisher Scientific. AlexaFluor594-phalloidin was obtained from ThermoFisher Scientific. The following antibodies and reagents were used: rabbit anti-prosurfactant protein C (Abcam, Cambridge, UK), rat anti-RAGE (R&D Systems, Minneapolis, MN, USA), rabbit anti-EEA1, anti-Rab11, and anti-clathrin from Cell Signaling (Cell Signaling, Danvers, MA, USA).
Kryvenko V., Alberro-Brage A., Fysikopoulos A., Wessendorf M., Tello K., Morty R.E., Herold S., Seeger W., Samakovlis C, & Vadász I. (2023). Clathrin-Mediated Albumin Clearance in Alveolar Epithelial Cells of Murine Precision-Cut Lung Slices. International Journal of Molecular Sciences, 24(3), 2644.
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5

Analyzing Membrane Trafficking Pathways

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The chemicals used in this study were: MBCD (Sigma, C4555), cholesterol-water soluble (Sigma, C4951), Baf A1 (Santa Cruz, CAS 88899-55-2), Wort (Santa Cruz, CAS 19545-26-7), cholera toxin subunit B conjugated with Alexa Fluor 594 (CTxB, Invitrogen, C34777), DAB (Dako, K401011), NEM (Sigma, E3876), DTT (Sigma, D9779), human transferrin peroxidase (Rockland antibodies and assays, 009-0334). The antibodies used were: anti-MAP1LC3B/LC3B (Sigma, L7543), anti-ACTB/β-actin (Sigma, A5441), anti-TFRC/TFRC (Invitrogen, 136,800), anti-VAMP3 (Santa Cruz, sc-514843), anti-CAV1/caveolin-1 (BD Pharmingen, 610,060), anti-ATG9A (Abcam, ab108338), anti-RAB11 (Cell Signaling Technology, 5589), mouse anti-STX6 (Invitrogen, 701,823), WIPI2 (Abcam, ab105459), and ATG16L1 (Cell Signaling Technology, 8089).
Shi Y., Ye Z., Lu G., Yang N., Zhang J., Wang L., Cui J., del Pozo M.A., Wu Y., Xia D, & Shen H.M. (2021). Cholesterol-enriched membrane micro-domaindeficiency induces doxorubicin resistancevia promoting autophagy in breast cancer. Molecular Therapy Oncolytics, 23, 311-329.
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6

Comprehensive Western Blot Analysis

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Tissue and cell lysates were analyzed by western blot using the following antibodies: anti-SorCS2 (R&D Systems, AF4237, 1:1000), anti-EAAT3 (Cell Signaling, #14501, 1:1000), anti-p-ERK (Cell Signaling, #4370, 1:2000), anti-tubulin (EMD Millipore, CP06, 1:5000), anti-mGlur2/3 (Novus Biologicals, NB300-124, 1:1000), anti-actin (Abcam, ab8227, 1:2000), anti-JWA (Trans Genic, KR057, 1:250), anti-N-cadherin (Cell Signaling, #14215, 1:1000), anti-GFP (MBL International, MBL598, 1:2000), anti-Rab11 (Cell Signaling, #5589, 1:1000), anti-synaptophysin (Synaptic Systems, 101011, 1:5000), anti-GluA1 (EMD Millipore, MAB2263, 1:1000), anti-GluA2 (EMD Millipore, MABN71, 1:1000), anti-PSD95 (Cell Signaling, #3409, 1:1000), anti-HO-1 (Cell Signaling, #70081, 1:1000). After incubation with secondary antibodies coupled to HRP, chemiluminescent signal was registered with use of digital LI-COR imaging system.
Malik A.R., Szydlowska K., Nizinska K., Asaro A., van Vliet E.A., Popp O., Dittmar G., Fritsche-Guenther R., Kirwan J.A., Nykjaer A., Lukasiuk K., Aronica E, & Willnow T.E. (2019). SorCS2 Controls Functional Expression of Amino Acid Transporter EAAT3 and Protects Neurons from Oxidative Stress and Epilepsy-Induced Pathology. Cell Reports, 26(10), 2792-2804.e6.
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7

Antibody and Lectin Toolkit for Cell Biology

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The following antibodies and lectins were used: anti-GnT-V (mouse, clone 706824, R&D Systems), anti-α1 sodium potassium ATPase (mouse, clone 464.6, Abcam), anti-LAMP1 (rabbit, Abcam), anti-GAPDH (mouse, clone 6C5, Merck Millipore), anti-GRP78 (BiP) (rabbit, Abcam), anti-GM130 (rabbit, clone D6B1) (Cell Signaling Technology), anti-Golgin97 (rabbit, clone D8P2K, Cell Signaling Technology), anti-Rab5 (rabbit, clone C8B1, Cell Signaling Technology), anti-Rab7 (rabbit, Cell Signaling Technology), anti-Rab11 (rabbit, Cell Signaling Technology), horseradish peroxidase (HRP)-conjugated anti-mouse IgG (GE Healthcare), HRP-conjugated anti-rabbit IgG (GE Healthcare), unconjugated-L4-PHA (J-Chemical), biotinylated-SSA (J-Chemical), biotinylated-RCA (Vector Laboratories), FITC-conjugated L4-PHA (J-Oil Mills), Rhodamine-conjugated L4-PHA (Vector Laboratories), Alexa546-conjugated anti-mouse IgG (Invitrogen), Alexa488-conjugated anti-rabbit IgG (Invitrogen). L4-PHA was conjugated to HRP using a Peroxidase Labeling Kit-NH2 (Dojindo) as described previously (22 (link)).
Osuka R.F., Hirata T., Nagae M., Nakano M., Shibata H., Okamoto R, & Kizuka Y. (2022). N-acetylglucosaminyltransferase-V requires a specific noncatalytic luminal domain for its activity toward glycoprotein substrates. The Journal of Biological Chemistry, 298(3), 101666.
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8

Immunoassays for Cellular Organelle Analysis

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Anti-B7-H3 (ThermoFisher, Loughborough, UK (IP), AF1027 BD Bioscience, Wokingham, UK (WB), and MAB1027 Santa Cruz, Heidelberg, Germany (IF)), anti-EEA1 (Cell Signaling, Leiden, The Netherlands), anti-HSC70 (Santa Cruz), anti-IMPDH2 (Proteintech), anti-Rab10 (Abcam, Cambridge, UK), anti-Rab11 (Cell Signaling), and HTII-280 AT2 (terrace Biotech, San Francisco, USA) were used. IgG negative control was used for IP and obtained from DAKO. DAPI (Sigma-Aldrich, Gillingham, UK) was used as nuclear stain for immunofluorescence. LysoTracker™ Deep Red was used to stain lysosomes (ThermoFisher). Anti-mouse-HRP, anti-rabbit-HRP, and anti-goat-HRP were from DAKO; anti-mouse-568, anti-rabbit-568, anti-rabbbit-488, and phalloidin-488 and -647 were all obtained from Invitrogen. Other reagents used were CellROX™ Deep Red Reagent (for oxidative stress detection) (ThermoFisher). CellEvent™ Caspase-3/7 Green Detection Reagent (ThermoFisher), Cisplatin (Cambridge Bioscience, Cambridge, UK), and Mycophenolic acid (MPA; IMPDH inhibitor) (Sigma-Aldrich).
Alhamad S., Elmasry Y., Uwagboe I., Chekmeneva E., Sands C., Cooper B.W., Camuzeaux S., Salam A, & Parsons M. (2023). B7-H3 Associates with IMPDH2 and Regulates Cancer Cell Survival. Cancers, 15(13), 3530.
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9

Bead-based TLR2 and TLR4 Activation Assay

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The TLR2 ligand Pam3CSK4-biotin and the TLR4 ligand LPS-biotin (InvivoGen) were resuspended to a concentration of 1 mg/ml in endotoxin-free water. Streptavidin-coated 2.8 μm magnetic beads (Dynabeads M-270) were incubated with 1 mg/ml of Pam3CSK4-biotin for 1 h at 4 °C. Beads were spun down and washed in Dulbecco’s modified Eagle medium (DMEM) containing 10% fetal bovine serum (FBS) two times before resuspending to a concentration of 1 × 105 beads/μl.
Immunoblot and confocal microscopy studies were performed using the indicated antibodies: anti-Rab5a 1:100 (Cell Signaling Technology, #2143S), anti-LAMP1 1:1000 (Abcam, #208943), anti-Rab8a 1:100 (Cell Signaling Technology, #6975S), anti-Rab11 1:100 (Cell Signaling Technology, #5589S), anti-β-actin 1:1000 (Cell Signaling Technology, #4970S), anti-MyD88 1:100 (R&D Systems), anti-TRAM (TICAM-2) 1:100 (Abcam), anti-TAK1 1:100 (Cell Signaling Technology, #5206S) anti-B. burgdorferi-FITC 1:1000 (Abcam). Lysotracker Red DND-99 (Invitrogen) was added to a final concentration of 50 nM as per the manufacturer’s instructions.
Petnicki-Ocwieja T., Sharma B., Powale U., Pathak D., Tan S, & Hu L.T. (2022). An AP-3-dependent pathway directs phagosome fusion with Rab8 and Rab11 vesicles involved in TLR2 signaling. Traffic (Copenhagen, Denmark), 23(12), 558-567.
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10

Immunofluorescence Staining of Cellular Proteins

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The primary antibodies used in this study are as follows: anti-RASSF1A (eB114-10H1) from eBioscience, anti-α-tubulin from Sigma Aldrich (St. Louis, MO) and anti-β-actin (8H10D10), anti-cofilin (D3F9), anti-GEF-H1, anti-HIF-1α, and anti-Rab11 from Cell Signaling Technology (Danvers, MA). Briefly, cells were seeded on coverslips at a density of 2 × 104 per well. After treatment, coverslips were washed with phosphate-buffered saline PBS and fixed with 4% paraformaldehyde for 20 min at 37 °C. Cells were permeabilized using ice-cold methanol for 10 min at − 20 °C to preserve microtubules. After extensive washes with PBS, cells were blocked overnight with 5% bovine serum albumin and then stained with primary antibodies and counterstained with appropriate Alexa Fluor 488-, and 555-conjugated secondary antibodies (Thermo Fisher Scientific, Rockford, IL). Coverslips were mounted with DAPI (Santa Cruz Biotechnology), and image captured with high-throughput confocal microscopy (FluoView FV1000, Olympus).
Dubois F., Jean-Jacques B., Roberge H., Bénard M., Galas L., Schapman D., Elie N., Goux D., Keller M., Maille E., Bergot E., Zalcman G, & Levallet G. (2018). A role for RASSF1A in tunneling nanotube formation between cells through GEFH1/Rab11 pathway control. Cell Communication and Signaling : CCS, 16, 66.
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