Anti integrin αv

Manufactured by Cell Signaling Technology

Sourced in United States

Anti-integrin αv is a laboratory reagent that binds to and detects the integrin αv subunit. Integrins are cell surface receptors that mediate cell-cell and cell-extracellular matrix interactions. The integrin αv subunit can form heterodimers with various β subunits and is involved in a range of cellular processes.

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Integrin αV

6 protocols using anti integrin αv

Integrin Signaling Pathway Antibodies

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Anti-FKBP10 (PA5-63387, 0.4 µg/mL) was purchased from Invitrogen (Rockford, IL, USA). Anti-AKT (9272,1:1000), anti-p-AKT₃₀₈(4056,1:1000), anti-p-AKT₄₇₃(9271L,1:1000), anti-integrin αV (4711,1:500) and α5 (4705,1:1000), anti-GAPDH (2118,1:1000) were purchased from Cell Signaling Technology (Danvers, MA, USA). Anti-integrin α6 (ab97760,1:500) was purchased from Abcam (Cambridge, MA, USA). Anti-integrin α1 (mab5676, 2µg/mL) and α2 (mab12331,1µg/mL) were purchased from the R&D system (Minneapolis, MN, USA).
Secondary goat anti-rabbit and goat anti-mouse antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Matrigel was purchased from Corning (Corning Life Science, Tewksbury, MA, USA).

Gong L.B., Zhang C., Yu R.X., Li C., Fan Y.B., Liu Y.P, & Qu X.J. (2020). FKBP10 Acts as a New Biomarker for Prognosis and Lymph Node Metastasis of Gastric Cancer by Bioinformatics Analysis and in Vitro Experiments. OncoTargets and therapy, 13, 7399-7409.

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Immunoblot Analysis of Cell Lysate Proteins

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Cell lysate preparation and immunoblot analyses were performed as previously reported [40 (link)]. Filters were probed with the indicated primary antibodies: anti-TIMP-1 and anti-CD99 (R&D Systems, Minneapolis, MN, USA); anti-integrin β1, anti-CD63 and anti-vinculin (Santa Cruz Biotechnology, Dallas, TX, USA); anti-vimentin, anti-integrin αv, anti-PDGFRβ, anti-pAKT, anti-pErk 1/2 and anti-ZO-1 (Cell Signaling Technology Inc., Danvers, MA, USA); anti-ITPRIPL1 (OriGene Technologies, Rockville, MD, USA); anti-NF-kB-p65 (Elabscience, Houston, TX, USA); anti-actin (Sigma-Aldrich); and anti-CD44 (Abcam, Cambridge, UK). Densitometric analysis was performed on at least two different exposures to assure the linearity of each acquisition using ImageJ software (v1.46r).

Agnello L., d’Argenio A., Caliendo A., Nilo R., Zannetti A., Fedele M., Camorani S, & Cerchia L. (2023). Tissue Inhibitor of Metalloproteinases-1 Overexpression Mediates Chemoresistance in Triple-Negative Breast Cancer Cells. Cells, 12(13), 1809.

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Western Blot Analysis of Cell Signaling

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Cells were washed with PBS and lysed with SDS lysis buffer. Frozen tissues were lysed using T-PER Tissue Protein Extraction Reagent (Thermo Fisher Scientific). Protein concentrations were determined using the Bradford assay (Bio-Rad). Equal amounts of protein from each sample were resolved by SDS-PAGE and transferred onto PVDF membranes (Millipore). Immunoblots were blocked by incubation in 5% skim milk in TBS-T (0.1% Tween 20) for 1 h at 25 °C. Membranes were incubated with the following primary antibodies: anti-TINAGL1 (1:1000; 12077-1-AP, Proteintech), anti-pFAK (1:1000; #3283; Cell Signaling Technology), anti-FAK (1:1000; #3285; Cell Signaling Technology), β-actin (1:10,000; sc-47778, Santa Cruz Biotechnology), anti-Twist (1:1000; ab49254, Abcam), anti-E-cadherin (1:500; #13-1700; Invitrogen), anti-N-cadherin (1:1000, ab18203, Abcam), anti-integrin β1 (1:1000; ab30394, Abcam), anti-integrin αv (1:1000; #4711, Cell Signaling Technology), anti-integrin α5 (1:1000; #4705, Cell Signaling Technology), and anti-GAPDH antibodies (1:20,000; Abc-1001, AbClon), followed by their corresponding HRP-conjugated secondary antibodies, anti-mouse (1:5000: #115-035-003, Jackson ImmunoResearch Labs) and anti-rabbit antibodies (1:4000; #Abc-5003, AbClon). Proteins were detected using AbSignal (Abclone).

Lee D., Ham I.H., Oh H.J., Lee D.M., Yoon J.H., Son S.Y., Kim T.M., Kim J.Y., Han S.U, & Hur H. (2024). Tubulointerstitial nephritis antigen-like 1 from cancer-associated fibroblasts contribute to the progression of diffuse-type gastric cancers through the interaction with integrin β1. Journal of Translational Medicine, 22, 154.

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Measuring Cell Surface Integrin Expression

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HCFs were transfected with 150 pmol of either siGLO or siDAAM1, then seeded in DMEM/F12 and 1% serum. 48 hrs post-transfection cells were treated with 10 ug/ml anti-integrin α5β1 (Novus, #2–52680) or anti-integrin αv (Cell Signaling #4711) antibodies in 1 ml of media for 30 min prior to cell surface stripping (0.2 M acetic acid, 0.5 M NaCl) for 30 s. Cell were incubated for 90 min prior to incubation with 2° antibody-488 for 30 min. Live cells were imaged (Zeiss LSM 780 confocal) and analyzed using ImageJ’s Analyze Particles.

Phillips A.T., Boumil E.F., Venkatesan A., Tilstra-Smith C., Castro N., Knox B.E., Henty-Ridilla J.L, & Bernstein A.M. (2023). The formin DAAM1 regulates the deubiquitinase activity of USP10 and integrin homeostasis. European journal of cell biology, 102(4), 151347.

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Protein Expression Analysis Protocol

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Cells were lysed in RIPA buffer (Millipore, Billerica, MA, USA) containing protease inhibitor cocktail (Roche, Basel, Switzerland). The lysates were quantified using a protein assay kit (Bio-Rad, Hercules, CA, USA) and the obtained proteins (20 μg) were separated by SDS-PAGE and transferred to a polyvinylidene difluoride membrane. The proteins were identified using the following antibodies: anti-VGLL1 [2000:1, 10124-2-AP; Proteintech (Rosemont, IL, USA)]; anti-TEAD4 [2000:1, ab58310; Abcam (Cambridge, MA, USA)]; anti-integrin αV (1000:1, 4711S), anti-β-tubulin (3000:1, 2128S), anti-p-ERK (3000:1, 4370S), anti-ERK (3000:1, 4695S), and anti-RSK2 (2000:1, 5528S) (Cell Signaling Technology, Danvers, MA, USA); anti-GAPDH [5000:1, LF-PA0212; AB FRONTIER (Seoul, Korea)]; and anti-β-actin [3000:1, SC-47778; Santa Cruz Biotechnology (Dallas, TX, USA)]; anti-GFP [2000:1, MA5-15256; Thermo Fisher (Waltham, MA, USA)].

Hwang M.A., Won M., Im J.Y., Kang M.J., Kweon D.H, & Kim B.K. (2022). TNF−α Secreted from Macrophages Increases the Expression of Prometastatic Integrin αV in Gastric Cancer. International Journal of Molecular Sciences, 24(1), 376.

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Western Blot Analysis of EMT Markers

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Protein was extracted from the cells and quantified as described previously [18, 19] . Equal amounts of protein were separated by electrophoresis on sodium dodecyl sulfate polyacrylamide gel electrophoresis gels, then transferred to polyvinylidene fluoride membranes. The membranes were blocked with 5% nonfat milk in TTBS (10 mM Tris-HCl pH 7.4, 100 mM NaCl, 0.5% Tween-20) for 40 min at room temperature and incubated overnight at 4 °C with primary antibodies. The following primary antibodies were used: anti-LBH, anti-ZEB1, anti-ZEB2, anti-SNAIL, and anti-SLUG (Abcam); anti-integrin-α1, anti-integrin-α2, anti-integrin-α4, anti-integrin-αv, anti-integrin-β1, anti-integrin-β3, anti-integrin-β4, anti-integrin-β5, anti-E-cadherin, anti-vimentin, and anti-actin (Cell Signaling Technology, Boston, MA, USA). The membranes were washed in TTBS and incubated with secondary antibodies for 40 min. After extensive washing, the membranes were visualized using the enhanced chemiluminescence reagent. Final images were analyzed using ImageJ software.

Deng M., Yu R., Wang S., Zhang Y., Li Z., Song H., Liu B., Xu L., Wang X., Zhang Z., Lv Q., Wang X., Che X., Qu X., Liu Y, & Hu X. (2018). Limb-Bud and Heart Attenuates Growth and Invasion of Human Lung Adenocarcinoma Cells and Predicts Survival Outcome. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 47(1).

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