Talin t3287

Manufactured by Merck Group

Sourced in United States

Talin (T3287) is a lab equipment product manufactured by Merck Group. It is a core component used in various scientific research applications. The product's function is to provide a stable and reliable platform for conducting experiments and analyses.

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Lab products found in correlation

Fibronectin f3648, by Merck Group (3 mentions) Anti rabbit secondary antibody, by Jackson ImmunoResearch (2 mentions) Rhodamine phalloidin, by Thermo Fisher Scientific (2 mentions) Lamp1 bs 1970r, by Bioss Antibodies (2 mentions) Acti stain 670, by Cytoskeleton (2 mentions) Hic 5 611164, by BD (2 mentions) β1 integrin clone 9eg7 553715, by BD (2 mentions) Cd29 610467, by BD (2 mentions) Ilk 611803, by BD (2 mentions) Tensin1 nbp1 84129, by Novus Biologicals (2 mentions) Phosphotyrosine clone 4g10 05 321, by Merck Group (2 mentions) α actinin a5044, by Merck Group (2 mentions) Tensin1 sab200283, by Merck Group (2 mentions) Phosphotyrosine clone p tyr 100 9411, by Cell Signaling Technology (2 mentions) β1 integrin clone 12g10 ab30394, by Abcam (2 mentions) α tubulin clone dm1a t9026, by Merck Group (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Merck Group (2 mentions) Normal goat serum (ngs), by Thermo Fisher Scientific (1 mentions) Paxillin, by BD (1 mentions) Te fm epi fluorescence system, by Olympus (1 mentions)

Spelling variants of this product

Talin (9 citations) T3287 (6 citations) Anti-talin antibody (clone 8D4; T3287) (3 citations)

6 protocols using talin t3287

Integrin and Cytoskeletal Protein Analysis

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Antibodies used in this analysis were: Hic-5 611164, β1 integrin clone 9EG7 553715, CD29 610467, ILK 611803 (BD Biosciences, Franklin Lakes, NJ USA); tensin1 NBP1-84129 (Novus Biologicals, Littleton, CO, USA); phosphotyrosine clone 4G10 05-321 (Millipore); talin T3287, fibronectin F3648, α-tubulin clone DM1A T9026, α-actinin A5044, tensin1 SAB200283 (Sigma-Aldrich, St. Louis, MO, USA); phosphotyrosine clone P-Tyr-100 9411 (Cell Signaling, Danvers, MA, USA); β1 integrin clone 12G10 ab30394 (Abcam, Cambridge, MA, USA); LAMP1 bs-1970R (Bioss, Woburn, MA, USA); Epcam G8.8 was deposited to the DSHB by Farr, A.G.
F-actin was visualized using Rhodamine phalloidin (Thermo-Fisher, Carlsbad, CA, USA) or Actistain 670 (Cytoskeleton, Denver, CO, USA). Fluorescently conjugated secondary antibodies used were: Dylight 488, 550 and 633 conjugated anti-mouse and anti-rabbit were purchased from Thermo-Fisher. FITC anti-rat, Alexa-fluor 488 anti-mouse, HRP-conjugated anti-mouse and anti-rabbit secondary antibodies were purchased from Jackson ImmunoResearch. The polydimethylsiloxane (PDMS) substrates were prepared as previously described(52 (link)).

Goreczny G.J., Forsythe I.J, & Turner C.E. (2018). Hic-5 Regulates Fibrillar Adhesion Formation to Control Tumor Extracellular Matrix Remodeling through Interaction with Tensin1. Oncogene, 37(13), 1699-1713.

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Integrin and Cytoskeletal Protein Analysis

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Immunofluorescence Imaging of Focal Adhesions

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HUVECs were fixed with 2% PFA after treatment for 24 h with DMSO or KCH-1521, and blocked with 5% normal goat serum (NGS; #16210, Gibco) in 1× PBS + 0.1% Tween 20 (PBST) for 1 h. The cells were incubated for 1 h at room temperature (RT) with the following primary antibodies: talin (T3287), vinculin (V9131, both from Sigma-Aldrich), and paxillin (610051, BD Biosciences, San Jose, CA, USA). After washing, the cells were incubated for 1 h at RT with Alexa Fluor 594-conjugated anti-mouse IgG (A11005) and Alexa Fluor 488-conjugated Phalloidin (A12379, both from Molecular Probes, Eugene, OR, USA). Nuclei were stained with 4′,6-diamidino-2-phenylindole (DAPI; D9542, Sigma-Aldrich). Negative controls for immunofluorescence staining were used to evaluate the specificity of primary antibodies and to exclude the possibility of non-specific staining of secondary antibodies by omitting the incubation of primary antibodies [37 (link)]. All immunofluorescent images were obtained using the TE-FM Epi-fluorescence system attached to an inverted microscope (BX61, Olympus, Tokyo, Japan).

Lim I.R., Joo H.J., Jeong M., Kim J.H., Choi S.C., Kim C., Jung J.W, & Hong S.J. (2017). Talin Modulation by a Synthetic N-Acylurea Derivative Reduces Angiogenesis in Human Endothelial Cells. International Journal of Molecular Sciences, 18(1), 221.

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Integrin-Mediated Cell Adhesion and Signaling

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Rabbit anti-human α5 integrin (ab25251) and β1 integrin (ab52971) monoclonal antibodies were purchased from Abcam (Cambridge, UK). Talin (T3287) was purchased from Sigma-Aldrich (Shanghai, China). HMGN2 (9437P), phospho-FAK (3284), FAK (3285); phospho-Src (6943) and Src (2109) were purchased from Cell Signaling Technology (Danvers, MA, USA). Rhodamine-conjugated phalloidin, DAPI and FITC were purchased from Sigma-Aldrich. RBITC-conjugated secondary antibody was purchased from Beyotime (Shanghai, China). Cytochalasin B and fibronectin peptide were acquired from Sigma-Aldrich. TRIzol reagent was obtained from Invitrogen (Carlsbad, CA, USA). RevertAid First Strand cDNA Synthesis kit and Maxima^® SYBR-Green were obtained from Thermo Fisher Scientific (Vilnius, Lithuania). The PCR primers were obtained from Sangon Biotech Co., Ltd. (Shanghai, China). RPMI-1640 medium was purchased from HyClone, Thermo Scientific (Beijing, China). Fetal bovine serum (FBS) was obtained from FuMeng Gene Co., Ltd. (Shanghai, China). Penicillin-streptomycin was purchased from Beijing Solarbio Science and Technology Co., Ltd. (Beijing, China). Other chemical reagents were all analytical grade.

Wang X., Li J., Chen S., Shen X., Yang X., Teng Y., Deng L., Wang Y., Chen J., Wang X, & Huang N. (2016). Knockdown of HMGN2 increases the internalization of Klebsiella pneumoniae by respiratory epithelial cells through the regulation of α5β1 integrin expression. International Journal of Molecular Medicine, 38(3), 737-746.

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Western Blot Analysis of Protein Signaling

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Antibodies to hnRNPA1 (ab5832, ab50492), hnRNPA3 (ab50949), hnRNPA₂/B₁ (ab64800), hnRNPL (ab6106, ab65049) and GAPDH (ab8245) or β-actin (ab8227) as loading controls, were from Abcam. Antibodies against acetyl-Lys (9441), pAKT (40665) and AKT (9272) were from Cell Signaling Technology. Other antibodies used were: ERK (sc-93) and pERK (sc-7383) from Santa Cruz Biotechnology; KRAS (05–516) from Millipore and Talin (T3287) from Sigma-Aldrich.
Epidermal growth factor (EGF 20ng/ml), trichostatin (TSA, 0.5μM) and sodium butyrate were from Sigma-Aldrich, UO126 (10μM) from Promega, LY294002 (10μM) from Calbiochem and Fibronectin from BD Biosciences.

Roda D., Castillo J., Telechea-Fernández M., Gil A., López-Rodas G., Franco L., González-Rodríguez P., Roselló S., Pérez-Fidalgo J.A., García-Trevijano E.R., Cervantes A, & Zaragozá R. (2015). EGF-Induced Acetylation of Heterogeneous Nuclear Ribonucleoproteins Is Dependent on KRAS Mutational Status in Colorectal Cancer Cells. PLoS ONE, 10(6), e0130543.

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Western Blot Analysis of Cytoskeletal Proteins

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Whole cell lysates were used for Western blotting following routine protocols for gel electrophoresis and trans-blotting, as described earlier [31, 33] . Equal amounts of 10 µL lysate containing 2 µg/µL protein were loaded on precast TGX stain-free gels (Bio-Rad, Munich, Germany). Transturbo blot PVDF membranes (Bio-Rad) were used for blotting. Each Western blot contained 5 samples for each group: 4 h 1g, 4 h RPM-AD cells, 24 h 1g, 24 h RPM AD cells and 24 h RPM MCS.
The following primary antibodies were used at a dilution of 1:1000: fibronectin (F3648), laminin (L9393) and talin (T3287) (all Sigma-Aldrich) and vascular endothelial growth factor (VEGFA; ab46154, Abcam, Cambridge, United Kingdom). The corresponding secondary antibodies were used at a dilution of 1:3000: HRP-linked anti-mouse IgG (#7076) and anti-rabbit IgG (#7074, both Cell Signaling Technology, Massachusetts, USA). The analysis was performed in ChemiDoc XRS+ (Bio-Rad), and the densitometric quantification was performed using ImageLab (BioRad).

Warnke E., Pietsch J., Kopp S., Bauer J., Sahana J., Wehland M., Krüger M., Hemmersbach R., Infanger M., Lützenberg R, & Grimm D. (2017). Cytokine Release and Focal Adhesion Proteins in Normal Thyroid Cells Cultured on the Random Positioning Machine. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 43(1).

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