β1 integrin

Manufactured by BD

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β1 integrin is a cell surface receptor that belongs to the integrin family of proteins. It plays a fundamental role in mediating cell-cell and cell-extracellular matrix interactions. β1 integrin is involved in a variety of cellular processes, including adhesion, migration, and signal transduction.

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Anti-β1 integrin (10 citations) β1 integrin antibody (8 citations) Integrin β1 (CD29, (4 citations) Mouse anti-integrin β1 (3 citations) Rat anti-active β1-Integrin 9EG7 (2 citations) Anti-β1 integrin (clone Ha2/5), (2 citations) Integrin β1-blocking antibody (2 citations) Active integrin β1 (2 citations) Total integrin β1 (2 citations) Active β1-integrin (clone 9EG7, (2 citations)

28 protocols using β1 integrin

Immunofluorescence and immunoblotting protocols for cellular protein detection

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The following monoclonal antibodies were used for immunofluorescence: anti-CHC17 (2 μg ml⁻¹; X22 (ref. 54 (link))), cortactin (1:500; Millipore, number 05–180), paxillin (1:500; Millipore, number 05–417), anti-HA (1:100; Covance, number MMS-101P). Rat anti-CD29 mAb13 against inactive β1-integrin (5 μg ml⁻¹; BD biosciences, number BDB552828), rabbit polyclonal antisera against the conserved region of CLCs55 (link), and Hip1R (1:100; Millipore, number AB9882) were also used. Secondary labelling was done with Alexafluor-488 (1:500; Life Technologies, number A-11001) or 555-conjugated secondary antibodies (1:500; Life Technologies, number A-21422). Alexafluor 647-phalloidin (1:100; Life Technologies, number A-22287) was used to stain F-actin. The following antibodies were used for immunoblotting: anti-CHC17 (1:1,000; TD.1 (ref. 56 (link))), Hip1R (1:500; Millipore, number AB9882), β1-integrin (1:1,000; BD Biosciences, number 610467), TfR (1:1,000; BD Biosciences, number 612124), HA (1:1,000; Covance, number MMS-101P), Hip1 (1:500; Sigma, number HPA013606), anti-β-actin (1:2,000; Sigma, number A5441) and α-tubulin (1:5,000; Sigma, number T6199).

Majeed S.R., Vasudevan L., Chen C.Y., Luo Y., Torres J.A., Evans T.M., Sharkey A., Foraker A.B., Wong N.M., Esk C., Freeman T.A., Moffett A., Keen J.H, & Brodsky F.M. (2014). Clathrin light chains are required for the gyrating-clathrin recycling pathway and thereby promote cell migration. Nature Communications, 5, 3891.

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Immunoblotting Analysis of Cellular Signaling

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Cells were lysed in RIPA buffer supplemented with leupeptin, aprotinin, phenylmethylsulfonyl fluoride, sodium vanadate, and a phosphatase inhibitor cocktail (Roche 04906845001). Lysates were quantified using the Pierce BCA assay (ThermoFisherScientific). 50ug of protein lysate was separated on 4–12 % Bis-Tri gels (Life Technology, Noverx) and samples were transferred to nitrocellulose membranes and immunoblotted with the following antibodies. HER3 (Santa Cruz sc81455), phospho-HER3 (Cell Signaling 4791), AKT (BD 610837), phospho-AKT (Cell Signaling 9271), β1 Integrin (BD 610467), and β-Actin (Sigma A5441).

Campbell M.R., Zhang H., Ziaee S., Ruiz-Saenz A., Gulizia N., Oeffinger J., Amin D.N., Ahuja D., Moasser M.M, & Park C.C. (2016). Effective treatment of HER2-amplified breast cancer by targeting HER3 and β1 integrin. Breast cancer research and treatment, 155(3), 431-440.

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Cell Lysis and Immunoblotting Protocol

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Cell lysis was performed with RLN-T buffer (RLN buffer plus 0.5% Triton X-100 and the complete protease inhibitors cocktail EDTA-free; Roche) at 20 × 10⁶ cells/ml for 5 min on ice. Extracts were centrifuged at 11,000 × g for 15 min at 4°C. The primary antibodies used were as follows: anti-IF1 (1:200) (22 (link)), e-cadherin (1:250, BD Biosciences), β1 integrin (1:2, kindly provided by Carlos Cabañas, CBMSO), β-catenin (1:500, BD Biosciences), vimentin (1:1,000, Cell Signaling), NF-κB p65 (1:1,000, Abcam), pIKBα (1:500, Cell Signaling), IKBα (1:1,000, Cell Signaling), α-tubulin (1:3,000, Sigma-Aldrich), β-F1-ATPase (1:25,000) and Hsp60 (1:2,000) from Ref. (35 (link)), SDH-B (1:500, Invitrogen),α-F1-ATPase (1:1,000, Molecular Probes), Core 2 of complex III (1:500, Abcam), MTCO2 (1:500, Abcam), VDAC (1:500, Abcam), and PYGM (1:1,000, Abcam).

García-Ledo L., Nuevo-Tapioles C., Cuevas-Martín C., Martínez-Reyes I., Soldevilla B., González-Llorente L, & Cuezva J.M. (2017). Overexpression of the ATPase Inhibitory Factor 1 Favors a Non-metastatic Phenotype in Breast Cancer. Frontiers in Oncology, 7, 69.

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Characterization of Mechanotransductive Pathways in Fibroblasts

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Antibodies specific for the following proteins were used: α-SMA (1:5000) and collagen-1 (1:1000, Sigma Aldrich); TRPV4 (1:500, Alomone Labs); p-AKT (Ser⁴⁷³) (1:1000) and total AKT (1:1000, Cell Signaling Technology); PI3Kα (1:250), PI3Kγ (1:250), and GRK2 (1:500, Santa Cruz); GAPDH (1:10,000, Fitzgerald); β1 integrin (1:1000) and flotillin-1 (1:1000, BD Biosciences); TRPV2 (1:500, Boster); and 6-His (1:1000, Roche). Purified TGF-β1 was purchased from R&D Systems and used at 2 ng/ml in all experiments. The TRPV4 agonist GSK1016790A as well as the TRPV4 antagonist (RN-1734, 50 μM) were purchased from Sigma-Aldrich. Alexa Fluor-phalloidin, ProLong Gold Antifade Reagent, and Alexa-Fluor conjugated secondary antibodies were obtained from Invitrogen. Ni-NTA beads were purchased from Qiagen. Polyacrylamide gels of varying stiffness and the polyacrylamide substrates (shear moduli 25 kPa) embedded with 0.2 μm yellow/green fluorospheres used for traction force microscopy were purchased from Matrigen. All other chemicals were purchased from Sigma-Aldrich and Fisher Scientific.

Grove L.M., Mohan M.L., Abraham S., Scheraga R.G., Southern B.D., Crish J.F., Prasad S.V, & Olman M.A. (2019). Translocation of TRPV4-PI3Kγ complexes to the plasma membrane drives myofibroblast transdifferentiation. Science signaling, 12(607), eaau1533.

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Hydrogel Culture and Immunostaining of hMSCs

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hMSCs on hydrogels were fixed with 4% PFA for 10 min and permeabilised with 0.2% Triton-X100 for 10 min. Following blocking with 10% BSA solution in PBS for 1 h, substrates were incubated with primary antibodies (vinculin (Abcam, ab18058), YAP/TAZ (Cell signalling, D24E4), β1 integrin (BD Biosciences, 550531), MyoD (BD Biosciences, 554130) and Alexa633-conjugated phalloidin (Sigma Aldrich) and subsequently with Alexa488 or -546-conjugated secondary antibodies (Life Technologies) and DAPI. For proliferation studies, EdU labelling was performed following the manufacturer’s protocol (Click-iT EdU Alexa Fluor-488 HCS Aaasy, Thermo fisher scientific). Quantification of nuclear localisation was performed manually. Cells were considered to have nuclear localisation when the level of fluorescence in the nucleus was higher than the level in the cytosol.

Bruekers S.M., Bao M., Hendriks J.M., Mulder K.W, & Huck W.T. (2017). Adaptation trajectories during adhesion and spreading affect future cell states. Scientific Reports, 7, 12308.

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Quantifying Cell Surface β1-Integrin Levels

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For quantitation of surface β1-integrin levels, cells were washed twice with PBS, trypsinised, centrifuged at 1,500 RPM then re-suspended in 500 μl of FACS buffer (PBS+0.1% heat inactivated BSA) and kept on ice. For primary antibody labelling with β1-integrin (BD Biosciences, 610467), cells were centrifuged and re-suspended in 100 μl of FACS buffer containing a 1:200 dilution of primary antibody and incubated on ice for 30 min. Cells were washed twice by sequential addition of 1 ml FACS buffer followed by centrifugation as above. Alexa 488 secondary antibody (Thermo Scientific) was added according to the antibody staining as above. Two rounds of washing were performed before surface integrin levels were measured using a FACS Aria 2 (BD).

Datta A., Sandilands E., Mostov K.E, & Bryant D.M. (2017). Fibroblast-derived HGF drives acinar lung cancer cell polarization through integrin-dependent RhoA-ROCK1 inhibition. Cellular signalling, 40, 91-98.

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Cellular Compartment Purification and Analysis

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Purification of each cellular compartment was tested by Western blot with antibodies for glyceraldehyde-3-phosphate dehydrogenase (cat. G8795; Sigma), High Mobility Group AT-Hook 1 (Hmga1) (cat. ab129153; Abcam), β1 integrin (cat. 610467; BD Bioscience), β-actin (cat. ab6276; Abcam), and collagen 1 (cat. PA5-95137; Invitrogen). One fifth of the extracellular protein pellet was dissolved in 30 uL of 4× sodium dodecyl sulfate (SDS) buffer supplemented with 100 mmol/L dithiothreitol (DTT). For other compartments, 10 uL sample was mixed with 10× lithium dodecyl sulfate (LDS) and 4× SDS.

Moutin E.B., Bons J., Giavara G., Lourenco F., Pan D., Burton J.B., Shah S., Colombé M., Gascard P., Tlsty T., Schilling B, & Winton D.J. (2024). Extracellular Matrix Orchestration of Tissue Remodeling in the Chronically Inflamed Mouse Colon. Cellular and Molecular Gastroenterology and Hepatology, 17(4), 639-656.

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Immunofluorescence and Immunoblotting Protocol

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Experiments were performed according to protocols previously described [31 (link)]. Samples were incubated overnight at 4⁰C with different dilutions for immunofluorescence with primary antibodies against ClC-3 (1:50, Abcam), β1 integrin (1:100, BD Pharmingen), α-tubulin (1:50, Abcam), vimentin (1:100, Boster), K18 (1:100, Boster) and K18 pS52 (1:50, Abcam). All antibodies were diluted to 1:1000 for immunoblotting.

Xu B., Jin X., Min L., Li Q., Deng L., Wu H., Lin G., Chen L., Zhang H., Li C., Wang L., Zhu J., Wang W., Chu F., Shen J., Li H, & Mao J. (2014). Chloride channel-3 promotes tumor metastasis by regulating membrane ruffling and is associated with poor survival. Oncotarget, 6(4), 2434-2450.

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Immunohistochemical Analysis of Tumor Tissues

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Sections (4 μm) of 20 tumor blocks were used for immunohistochemical analysis. The slides were placed in boiling citric acid buffer (10 mM sodium citrate and citric acid) for 10 minutes. Sections were treated with primary antibodies β1-integrin (#610467, BD Bioscience), EP1 receptor, p65, and FoxC2, applied at a 1:100 or 1:200 dilution and incubated overnight at 4°C. Bound antibody was detected using EnVision polymer technology. After a complete wash in PBS, the slides were developed in freshly prepared diaminobenzedine solution (DAB) for 8 min, and then counterstained with hematoxylin. PBS substituted for the primary antibody as a negative control. The sections were photographed by LeiCa microscopy and Image analyse system. 4 low power views (400×) were randomly selected from each samples in a blind manner.

Bai X., Wang J., Guo Y., Pan J., Yang Q., Zhang M., Li H., Zhang L., Ma J., Shi F., Shu W., Wang Y, & Leng J. (2014). Prostaglandin E2 stimulates β1-integrin expression in hepatocellular carcinoma through the EP1 receptor/PKC/NF-κB pathway. Scientific Reports, 4, 6538.

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Integrin and TGF-β Signaling Assay

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Antibodies included: β1 integrin (#610167), β4 integrin (#553745), α6 integrin (#555734) (all from BD Biosciences); Smad2 (#3103), phospho-Smad2 (S465/467, #3101), NF-κB p65 (#4764), phospho-NF-κB p65 (S536, #3033), E-cadherin (#4065), β-actin (#4967), Caspase-3 (#9662), Cleaved Caspase-3 (#9661), Cleaved Caspase-9 (#9509), cleaved PARP (#9544) (all from Cell Signaling), α-tubulin (#T5168, Sigma-Aldrich), ZO-1 (#sc-33725, Santa Cruz), and Alexa-Fluor®-conjugated secondary antibodies (Molecular Probes®, Life Technologies). Growth factors/hormones included: rhTGFβ1 (Invitrogen) and insulin (Sigma-Aldrich). The TβRI inhibitor SB-431542 was from InvivoGen.

Avery-Cooper G., Doerr M., Gilbert R.W., Youssef M., Richard A., Huether P, & Viloria-Petit A.M. (2014). Par6 is an essential mediator of apoptotic response to transforming growth factor beta in NMuMG immortalized mammary cells. Cancer Cell International, 14, 19.

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