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Anti integrin β1

Manufactured by Cell Signaling Technology
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Anti-Integrin β1 is a laboratory reagent used to detect and analyze the Integrin β1 protein in biological samples. Integrin β1 is a cell surface receptor that plays a role in cell adhesion and signaling processes. The Anti-Integrin β1 reagent can be used in various research applications, such as western blotting, immunoprecipitation, and flow cytometry, to study the expression, localization, and function of Integrin β1 in cells and tissues.

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Lab products found in correlation

Anti fak, by Cell Signaling Technology (6 mentions) Anti akt, by Cell Signaling Technology (3 mentions) Anti src, by Cell Signaling Technology (3 mentions) Anti β actin, by Merck Group (3 mentions) Anti integrin α5, by Cell Signaling Technology (2 mentions) Anti erk1 2, by Cell Signaling Technology (2 mentions) Anti phospho fak, by Cell Signaling Technology (2 mentions) Anti phospho erk1 2, by Cell Signaling Technology (2 mentions) Anti cd151, by Santa Cruz Biotechnology (2 mentions) Anti integrin α3, by Cell Signaling Technology (2 mentions) Anti integrin β3, by Cell Signaling Technology (2 mentions) Anti β actin, by Cell Signaling Technology (2 mentions) Anti phospho akt, by Cell Signaling Technology (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Anti calnexin, by Cell Signaling Technology (2 mentions) Anti integrin α4, by Cell Signaling Technology (2 mentions) Anti flag, by Merck Group (1 mentions) Anti ki67, by Cell Signaling Technology (1 mentions) Anti α actinin, by Merck Group (1 mentions) Anti α tubulin, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Integrin β1 (53 citations) Rabbit anti‐integrin β1 (5 citations)

19 protocols using anti integrin β1

1

Immunohistochemical Analysis of Tissue Sections

Cited 1 time
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Tissues sections were stained with hematoxylin and eosin (H&E), and IHC was done using anti-FLAG (1:200, Sigma-Aldrich), anti-Ki67 (1:200, Cell Signaling Technology), anti-integrin-β1 (1:300, Cell Signaling Technology) antibodies as described previously [31 (link)].
Jahan R., Macha M.A., Rachagani S., Das S., Smith L.M., Kaur S, & Batra S.K. (2018). Axed MUC4 (MUC4/X) aggravates pancreatic malignant phenotype by activating integrin-β1/FAK/ERK pathway. Biochimica et biophysica acta, 1864(8), 2538-2549.
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2

Immunoblotting Analysis of Cell Signaling

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Tissue samples were snap frozen and stored at − 80 °C or lysed in RIPA-buffer containing protease inhibitors and analyzed by immunoblotting. Primary antibodies used in this study were rabbit anti-zyxin (B71, provided by M. Beckerle, Huntsman Cancer Institute), anti-α-tubulin (#2144, Cell Signaling), anti-α-actinin (#A7811, Sigma-Aldrich), anti-FAK (#3285, Cell Signaling), anti-pFAK (Y397) (#44-624G, Thermo Fisher Scientific), anti-AKT (#9272, Cell Signaling), anti-pAKT (Ser473) (#9271, Cell Signaling), anti-Integrin α5 (#4705, Cell Signaling), anti-Integrin β1 (#9699, Cell Signaling), anti-Col1α2 (#sc-166865, Santa Cruz Biotechnology) and anti-LOX (sc-373995, Santa Cruz Biotechnology). HRP-conjugated anti-mouse (#4416, Sigma-Aldrich) and anti-rabbit (#6154, Sigma-Aldrich) antibodies were used as secondary antibodies and chemiluminescence was detected with the ImageQuant LAS mini system (GE Healthcare). Densitometric analysis was done with ImageJ.
Al-Hasani J., Sens-Albert C., Ghosh S., Trogisch F.A., Nahar T., Friede P.A., Reil J.C, & Hecker M. (2022). Zyxin protects from hypertension-induced cardiac dysfunction. Cellular and Molecular Life Sciences, 79(2), 93.
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3

Comprehensive Antibody Characterization

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The following antibodies were used: mouse IgG1 (MG100) from Life Technologies (Carlsbad, CA), anti-integrin β1 P5D2 (ab24693) from Abcam (Cambridge, UK), anti-tubulin α (T9026) from Sigma-Aldrich, HRP-conjugated polyclonal goat anti-mouse or anti-rabbit antibodies from DAKO Cytomation (Glostrup, DK), and anti-integrin β1 (#4706), anti-MLC2 (#3672), anti-NMHCIIA (#3403), anti-NMHCIIB (#3404), anti-NMHCIIC (#8189), Alexa Fluor® 488-conjugated anti-mouse IgG (H+L) antibodies from Cell Signaling Technologies (Danvers, MA).
Blockhuys S., Liu N., Agarwal N.R., Enejder A., Loitto V, & Sun X.F. (2016). X-radiation enhances the collagen type I strap formation and migration potentials of colon cancer cells. Oncotarget, 7(44), 71390-71399.
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4

Investigating EGFR and Integrin Signaling

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Cetuximab and resveratrol were purchased from Merck KGaA (Darmstadt, Germany). Cell Signaling Technology (Dancers, MA) provided the following antibodies: anti-EGFR (#4267), anti-Phospho-EGFR (#2234), anti-Integrinβ1 (#4706), anti-Src (#2108), anti-Phospho-Src Family (#2101), anti-FAK (#3285), anti-Phospho-FAK (#3283), anti-ERK1/2 (#4695), and anti-Phospho-ERK1/2 (#4370). Santa Cruz Biotechnology, Inc. (Dallas, TX) provided the antibodies against uPAR (sc-10815) and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (sc-3223).
Uzawa K., Amelio A.L., Kasamatsu A., Saito T., Kita A., Fukamachi M., Sawai Y., Toeda Y., Eizuka K., Hayashi F., Kato-Kase I., Sunohara M., Iyoda M., Koike K., Nakashima D., Ogawara K., Endo-Sakamoto Y., Shiiba M., Takiguchi Y., Yamauchi M, & Tanzawa H. (2019). Resveratrol Targets Urokinase-Type Plasminogen Activator Receptor Expression to Overcome Cetuximab-Resistance in Oral Squamous Cell Carcinoma. Scientific Reports, 9, 12179.
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5

Immunostaining of Neurosphere Cells

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Neurosphere cells were collected by cytospin onto glass slides and fixed with 4% paraformaldehyde. Cells were permeabilized by Triton X-100 and immunostained with anti-CD151 (1:50; Santa Cruz Biotechnology, Dallas, TX, www.scbt.com), anti-integrin α3 (1:50), anti-integrin α6 (1:50), and anti-integrin β1 (1:100; Cell Signaling) antibodies following the protocol from Cell Signaling. Secondary antibodies were conjugated with Alexa488 or Cy3 (1:250). Immunofluorescent images were taken and analyzed using the ZEISS AxioImager M2 Imaging System with Axiovision software (Zeiss, Thornwood, NY, www.zeiss.com).
Tilghman J., Schiapparelli P., Lal B., Ying M., Quinones-Hinojosa A., Xia S, & Laterra J. (2016). Regulation of Glioblastoma Tumor-Propagating Cells by the Integrin Partner Tetraspanin CD151. Neoplasia (New York, N.Y.), 18(3), 185-198.
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6

Protein Extraction and Analysis

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Total cellular protein was extracted with radioimmunoprecipitation assay buffer (Sigma-Aldrich) containing protease and phosphatase inhibitors (Calbiochem, Billerica, MA, www.calbiochem.com). The Subcellular Protein Fractionation Kit was used for membrane protein extraction (Thermo Scientific). SDS-PAGE was performed with 50 μg of total proteins using 4% to 12% gradient Tris-glycine gels (LI-COR Biosciences, Lincoln, NE, www.licor.com). Western blot analysis was performed using the Quantitative Western Blot System, with secondary antibodies labeled by IRDye infrared dyes (LI-COR Biosciences). The primary antibodies were anti-CD151, anti-Olig2, anti-FLAG (Santa Cruz), anti-Sox2, anti-S473-pAkt, anti-total-Akt, anti-integrin α3, anti-integrin α6, anti-integrin β1 (Cell Signaling), anti-pan Cadherin (Abcam, Cambridge, MA, www.abcam.com), and anti-β-actin (Sigma-Aldrich).
Tilghman J., Schiapparelli P., Lal B., Ying M., Quinones-Hinojosa A., Xia S, & Laterra J. (2016). Regulation of Glioblastoma Tumor-Propagating Cells by the Integrin Partner Tetraspanin CD151. Neoplasia (New York, N.Y.), 18(3), 185-198.
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7

Western Blot Analysis of DNA Damage Signaling

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Cell seeding, collection of protein and Western blot methods were as previously described[19 (link)] Membranes were probed with the following antibodies: anti-MT1-MMP (EMD Millipore, MA); anti–integrinβ1 (Cell signaling Technology); anti γH2AX (ser139 JBC301, Millipore); anti p-FAKY397 (Abcam); anti-p-ChK1, anti p-ChK2, anti p-RPA32 (Cell Signaling Technology); β-actin, GAPDH (Santa Cruz Biotechnology).
Thakur V., Zhang K., Savadelis A., Zmina P., Aguila B., Welford S.M., Abdul-Karim F., Bonk K.W., Keri R.A, & Bedogni B. (2018). The membrane tethered matrix metalloproteinase MT1-MMP triggers an outside-in DNA Damage Response that impacts chemo- and radiotherapy responses of breast cancer. Cancer letters, 443, 115-124.
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8

Inhibition of Pyk2 and Rac1 Signaling

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NaHS was administered instead of H2S. NaHS and the Pyk2 inhibitor (PF431396) were obtained from Sigma-Aldrich; The FAK specific inhibitor (PF573228), the Src inhibitor (PP2), and the Rac1 inhibitor (NSC23766) were purchased from Selleck Chemicals. CES-siRNA (sc-142618) was obtained from Santa Cruz. Rhodamine was obtain from Cytoskeleton, and DAPI from Beyotime; Following antibodies were used: anti-Rac, anti-Fak, anti-p-FAK397, anti-p-FAK925, anti-Src, anti-p-Src, anti-β-actin, anti-Integrin β1, anti-Integrin β3, anti-Cavenolin-1,anti-p-Pyk2 (Cell Signaling); anti-CSE (Santa Cruz); anti-Integrin β1-FITC, anti-Galectin-3 (eBbioscience); anti-CD68 (Biolegend); Lactate dehydrogenase (LDH) assay from BeyotimeInstitute of Biotechnology.
Miao L., Xin X., Xin H., Shen X, & Zhu Y.Z. (2016). Hydrogen Sulfide Recruits Macrophage Migration by Integrin β1-Src-FAK/Pyk2-Rac Pathway in Myocardial Infarction. Scientific Reports, 6, 22363.
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9

Molecular Signaling in Alzheimer's Disease

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Tissues from 3xTg‐AD mice and AD patients were homogenized with a douncer and sonicated in 200 μl of RIPA with a protease inhibitor cocktail (Complete, Mini EDTA‐free tablets, Roche, Mannheim, Germany). Astrocyte (1×105) and tissue homogenates were centrifuged at 4°C for 10 min at 12,000 × g, and protein content in the supernatant was quantified with the Bio‐Rad Protein Assay (Bio‐Rad, Hercules, CA, USA). Cell and tissue extracts (10 μg) were loaded into gels and blots were developed with rabbit polyclonal anti‐integrin β1, antiphosphoPAK, anti‐PAK, antiphosphoPKC, antiphosphoPKD, antiphosphoAKT, anti‐AKT (1:1000, Cell Signaling Technology, Beverly, MA, USA), rabbit polyclonal anti‐NOX2, anti‐NOX‐1 (1:1000, Novus Biologicals, Littleton, CO, USA), rabbit polyclonal anti‐β actin (1:5000, Sigma, St. Louis, MO, USA), mouse monoclonal anti‐GFAP, anti‐Rac1, anti‐GAPDH (1:2000, Millipore Ibérica, Madrid, Spain), and anti‐beta amyloid 1–16 (1:1000, 6E10 BioLegend, San Diego, CA, USA). For dot blot assay, human tissue extracts (2 μg) were spotted into a nitrocellulose membrane, and rabbit polyclonal anti‐Aβ1‐42 (1:10000, Abcam, Cambridge, UK) was used for chemiluminescence detection.
Wyssenbach A., Quintela T., Llavero F., Zugaza J.L., Matute C, & Alberdi E. (2016). Amyloid β‐induced astrogliosis is mediated by β1‐integrin via NADPH oxidase 2 in Alzheimer's disease. Aging Cell, 15(6), 1140-1152.
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10

Protein Expression Analysis of Signaling Pathways

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Whole cell lysates were prepared in lysis buffer (20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM EDTA, 1% NP40 and 10% Glycerol), resolved by SDS-PAGE and blotted with indicated antibodies. The following antibodies were used in this study: Anti-β-catenin, anti-FAK, anti-phospho-FAK (Tyr397), anti-ERK1/2, anti-SRC and anti-Integrin β1 (Cell Signaling Technology, Danvers, MA); anti-GSK3α/β, anti-phospho-GSK3α/β (Tyr279/216), anti-phospho-ERK1/2, anti-β-Actin and anti-SP1 (Santa Cruz Biotechnology, Dallas, TX). SuperSignal West Pico Chemiluminescent Substrate and SuperSignal Western Blot Enhancer (Thermo Fisher Scientific, Waltham, MA) were used to enhance western signal when needed. Vemurafenib, Dabrafenib, GDC-0879 (8 (link)), Erlotinib, SCH772984 (9 (link)), LY3009120 (10 (link)) and ICG-001(11 (link)) were purchased from Selleck Chemicals (Houston, TX). PF-562271 (12 (link)) was purchased from MedKoo Biosciences (Chapel Hill, NC). PLX7904 (13 (link)) was obtained from Plexxikon (Berkeley, CA). Gelucire is a gift from Gattefosse (Paramus, NJ). NE-PER Nuclear and Cytoplasmic Extraction Reagents from Thermo Fisher Scientific were used for subcellular fractionation according to manufacturer’s protocol.
Chen G., Gao C., Gao X., Zhang D.H., Kuan S.F., Burns T.F, & Hu J. (2017). Wnt/β-catenin pathway activation mediates adaptive resistance to BRAF inhibition in colorectal cancer. Molecular cancer therapeutics, 17(4), 806-813.
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