Rabbit anti integrin β1

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit anti‐integrin β1 is a primary antibody that specifically recognizes the integrin β1 subunit. Integrins are cell surface receptors that mediate cell-cell and cell-extracellular matrix interactions. The integrin β1 subunit associates with multiple α subunits to form diverse integrin heterodimers.

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Integrin β1 (53 citations) Anti-Integrin β1 (19 citations)

5 protocols using rabbit anti integrin β1

Sac2 Protein Purification and Enzymatic Assay

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HEK293T cells grown to ∼80% confluence were cotransfected with appropriate plasmids using PEI reagent. After ∼18-h transfection, cells were lysed in RIPA buffer. Soluble fractions were collected by centrifugation at 18,000 rpm for 15 min at 4°C. Immunoprecipitates were prepared by 2-h binding at 4°C, followed by washing with 50 mM Tris-HCl, pH 8.0, and 150 mM NaCl. To prepare Sac2 proteins for enzymatic assays, endogenous mouse Sac2 proteins from N2A cells were immunopurified using 1 µg of anti-Sac2 antibodies and 15 µl of protein A beads. GFP-Sac2 and Flag-Sac2 proteins were purified using GFP-Trap beads (ChromoTek) and anti-Flag M2 affinity gel (Sigma-Aldrich), respectively. Final beads were resuspended in reaction buffer (50 mM Tris-HCl, pH 8.0, and 150 mM NaCl). Endogenous β1 integrin was detected using rabbit anti–β1 integrin (Cell Signaling Technology).

Hsu F., Hu F, & Mao Y. (2015). Spatiotemporal control of phosphatidylinositol 4-phosphate by Sac2 regulates endocytic recycling. The Journal of Cell Biology, 209(1), 97-110.

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Western Blot Analysis of Cellular Proteins

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Lysates from whole-cell extracts, cell-surface proteins, or intracellular proteins were subjected to gel electrophoresis. Proteins were then transferred to PVDF membranes (Bio-Rad, Burlington, ON). The membranes were blocked in a solution of TBS-T containing 4% BSA or 3% milk for 30 minutes at room temperature and then incubated at room temperature with the primary antibody for 1h. Rabbit anti-CD71 (1:1000), rabbit anti-Glut1 (1:1000), and rabbit anti-EGFR (1:1000) were purchased from GeneTex (Irvine, CA), goat anti-EGFR, mouse anti-TfR
(1:400, 1:1000), and mouse anti-CHC (1:1000) were purchased from Santa Cruz Biotechnology (Santa Cruz, CA). Rabbit anti-β1 integrin (1:1000), rabbit anti-pAMPK (1:500), rabbit anti-pACC (1:500), rabbit anti-pan-actin (1:1000), and rabbit anti-total ERK (1:1000) were purchased from Cell Signaling Technology (Danvers, MA). Mouse anti-β1-integrin (1:400) was purchased from Calbiochem (Billerica, MA). Secondary antibodies were goat anti-rabbit, goat anti-mouse, (Jackson Immunoresearch, West Grove, PA). Streptavidin-POD (1:1000) was purchased from Roche.

Ross E. (2021). The regulation of the cell surface proteome by amp-activated protein kinase.

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Integrin Subunit Immunoprecipitation and Blotting

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The following antibodies were used for immunoprecipitation and Western blot studies (Bicker et al, 2017): mouse anti‐tubulin alpha Ab‐2 (MS‐581‐P1, 1:6,000, Thermo), goat anti‐EGFL7 (R‐12, sc‐34416, 1:1,000, Santa Cruz Biotechnology, Dallas, TX, USA), rabbit anti‐integrin β₁ (#4706, 1:1,000, Cell Signaling Technology, Danvers, MA, USA), rabbit anti‐integrin β₃ (H‐96, sc‐14009, 1:1,000, Santa Cruz), mouse anti‐CD49e (610634, 1:1,000, BD Transduction Laboratories, San Jose, CA, USA), mouse anti‐integrin α_V (P2W7, sc‐9969, 1:1,000, Santa Cruz), IRDye 680RD‐conjugated streptavidin, fluorescently labeled goat‐anti‐rabbit (1:15,000, LI‐COR Biosciences, Lincoln, NV, USA), fluorescently labeled goat‐anti‐mouse (1:15,000, LI‐COR Biosciences), and fluorescently labeled donkey‐anti‐goat (1:15,000, LI‐COR).

Dudvarski Stanković N., Bicker F., Keller S., Jones D.T., Harter P.N., Kienzle A., Gillmann C., Arnold P., Golebiewska A., Keunen O., Giese A., von Deimling A., Bäuerle T., Niclou S.P., Mittelbronn M., Ye W., Pfister S.M, & Schmidt M.H. (2018). EGFL7 enhances surface expression of integrin α5β1 to promote angiogenesis in malignant brain tumors. EMBO Molecular Medicine, 10(9), e8420.

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Immunoprecipitation and Western Blot Analysis of MUC16, Integrin α4, and Integrin β1

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T3M4 and Capan-2 (WT and SC) cells were lysed in non-denaturing RIPA buffer (Thermo scientific, Lenexa, KS, USA) containing protease inhibitor (Roche Diagnostics GmbH, Mannheim, Germany). A total of 500 µg of proteins were incubated with either mouse anti-MUC16 (5 µg/mL) or mouse IgG (5 µg/mL; Jackson ImmunoResearch Laboratories, Inc., PN, USA) overnight at 4 °C. Lysates were then incubated with protein G Sepharose beads (GenScript, Piscataway, NJ, USA) for 2 h at room temperature. Beads were collected, washed three times with RIPA buffer without a protease inhibitor, and boiled in SDS loading buffer (1X). Samples were subjected to 4–20% gradient (Bio-Rad, CA, USA) SDS-PAGE gel electrophoresis and transferred to the PVDF membrane. The membranes were blocked with 5% skimmed milk and incubated with primary antibodies rabbit anti-integrin α4 (Cell Signaling Technology, Danvers, MA, USA, 1:1000) and rabbit anti- integrin β1 (Cell Signaling technology, Danvers, MA, USA, 1:1000) overnight. After incubating with the respective secondary antibodies, the protein–antibody complex was detected using enhanced chemiluminescence (Bio-Rad, CA, USA).

Rajesh C., Sagar S., Rathinavel A.K., Chemparathy D.T., Peng X.L., Yeh J.J., Hollingsworth M.A, & Radhakrishnan P. (2022). Truncated O-Glycan-Bearing MUC16 Enhances Pancreatic Cancer Cells Aggressiveness via α4β1 Integrin Complexes and FAK Signaling. International Journal of Molecular Sciences, 23(10), 5459.

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Integrin Signaling Pathway Analysis

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Total protein of A549 and H1650 cells was collected and extracted using RIPA lysis buffer (Jinkelong Biotechnology Co., Ltd., Beijing, China), containing protease inhibitor cocktail and a protein phosphatase inhibitor (Beyotime Institute of Biotechnology, Haimen, China), followed by centrifugation at 10,000 g for 10 min at 4 °C. Following electrophoresis, the samples were then transferred to PVDF membranes, and the membranes were incubated with rabbit anti-integrin α5, rabbit anti-integrin β1, rabbit anti-FAK and rabbit anti-p-FAK primary antibodies (Cell Signaling Technology, Inc.) overnight at 4 °C. The membranes were then incubated with the indicated secondary antibodies (Santa Cruz Biotechnology, Inc., SC-2005) for 1 h at room temperature. Detection was performed using an electrochemiluminescence kit (Pierce; Thermo Fisher Scienti c, Inc.). β-actin (Santa Cruz Biotechnology, Inc.) was used as an internal control.

Shen D., Zeng Y., Zhang W., Li Y., Zhu J., Liu Z., Yan Z., & Huang J. (2021). CDCA attenuates LUAD pathogenesis progression via integrin α5β1/FAK/p53 signalling pathway.

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