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Anti tgf β rii

Manufactured by Santa Cruz Biotechnology
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Sourced in Germany, Denmark

Anti TGF-β RII is a lab equipment product that is used for the detection and quantification of the TGF-β RII protein. It functions as an antibody that specifically binds to the TGF-β RII protein, allowing for its identification and measurement in various samples.

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Lab products found in correlation

Anti tgfβri, by Santa Cruz Biotechnology (2 mentions) Anti iβ3, by Santa Cruz Biotechnology (2 mentions) Pd 10 desalting column, by GE Healthcare (2 mentions) Synergy 2 plate reader, by Agilent Technologies (2 mentions) Anti α smooth muscle actin, by Merck Group (1 mentions) Anti smad4, by Santa Cruz Biotechnology (1 mentions) Anti smad3, by Abcam (1 mentions) Anti p smad3, by Merck Group (1 mentions) Anti smad2, by BD (1 mentions) Anti snail, by Cell Signaling Technology (1 mentions) Anti p smad2, by Cell Signaling Technology (1 mentions) Anti β actin, by Merck Group (1 mentions) Anti n cadherin, by BD (1 mentions) Ep568y, by Abcam (1 mentions) Sds page gel, by Bio-Rad (1 mentions) In vivo ms fx pro, by Bruker (1 mentions) Anti rabbit or anti mouse igg, by Santa Cruz Biotechnology (1 mentions) Lsm 510 inverted confocal microscope, by Zeiss (1 mentions) Alexafluor 546 carboxylic acid succinimidyl ester, by Thermo Fisher Scientific (1 mentions)

5 protocols using anti tgf β rii

1

Investigating TGF-βRII Protein Interactions

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To investigate association of membrane proteins, cells were lysed using a 1% Nonidet-P40 buffer containing a cocktail of protease and phosphatase inhibitors (Pierce). 400μg total protein lysate per tube was incubated overnight at 4°C under gentle end-over-end mixing with anti-TGF-βRII (1 μg, Santa Cruz). Subsequently, the immune complex was captured with protein A/G agarose resin, thoroughly washed with lysis buffer and eluted with non-reducing sample buffer. Proteins were then separated on a 10% SDS-PAGE gel (BioRad) and transferred to a PVDF membrane. Following blocking with 5% milk in TBS with 0.1% Tween-20, membranes were incubated with anti-Iβ3 (Santa Cruz, 1:1000) or anti-TGF-β RII (Santa Cruz, 1:1000) at 4°C overnight. After washing, membranes were blotted with anti-rabbit or anti-mouse IgG (1:5000 Santa Cruz), and bands were detected by enhanced chemiluminescence using an In Vivo MS FX Pro (Bruker). The Iβ3 and TGF-βRII co-precipitation was quantified by normalizing the band intensity of Iβ3 pulled down with TGF-βRII to total protein (anti-TGF-βRII). Analysis was performed using Image J software.
Page J.M., Merkel A.R., Ruppender N.S., Guo R., Dadwal U.C., Cannonier S., Basu S., Guelcher S.A, & Sterling J.A. (2015). Matrix Rigidity Regulates the Transition of Tumor Cells to a Bone-Destructive Phenotype through Integrin β3 and TGF-β Receptor Type II. Biomaterials, 64, 33-44.
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2

Western Blotting of EMT Markers

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Western blotting was carried out as previously described [27 (link)]. The primary antibodies used were anti-N-Cadherin (BD Biosciences, Breda, Netherlands #610920), anti-α-Smooth Muscle Actin (Sigma, Zwijndrecht, Netherlands #A2547), anti-Snail (Cell Signaling, Leiden, Netherlands #3879), anti-Smad2 (BD Biosciences, Breda, Netherlands #610842), anti-p-Smad2 (Cell Signaling, Leiden, Netherlands #3108), anti-Smad4 (Santa Cruz #sc7966), anti-TGFβRI (Santa Cruz, Heidelberg, Germany #sc 398), anti-TGFβRII (Santa Cruz, Heidelberg, Germany #sc-400), anti-Smad3 (Epitomics, Duiven, Netherlands #1735–1), anti-p-Smad3 (a kind gift from Dr Edward B Leof, Mayo Clinic, Rochester, Minnesota) and anti-β-actin (Sigma, Zwijndrecht, Netherlands #A5441). All the secondary antibodies were from Sigma, Zwijndrecht, Netherlands. Western quantification was performed using image J software.
Li Y., Drabsch Y., Pujuguet P., Ren J., van Laar T., Zhang L., van Dam H., Clément-Lacroix P, & ten Dijke P. (2015). Genetic depletion and pharmacological targeting of αv integrin in breast cancer cells impairs metastasis in zebrafish and mouse xenograft models. Breast Cancer Research : BCR, 17(1), 28.
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3

Quantifying Phosphorylated SMAD3 Signaling

Cited 1 time
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After isolation, content determination and electrophoresis, proteins were electroblotted [31 (link)] and incubated with a monoclonal rabbit anti-phosphorylated SMAD3 (1:1000; S423 + S425, EP823Y; Abcam), anti-SMAD3 (1:1000; EP568Y; Abcam), polyclonal rabbit anti-TGFβ-RI (1:200; Santa Cruz Biotechnology), anti-TGFβ-RII (1:200; Santa Cruz Biotechnology), mouse anti-VDR (1:100, D-6; Santa Cruz Biotechnology), anti-α-smooth muscle actin (α-SMA, 1:000 Dako Cytomatic, Glostrup, Denmark), anti-total tubulin and anti-GAPDH antibodies (Sigma Aldrich) following horseradish peroxidase conjugate goat anti-rabbit or anti-mouse IgGs (Pierce, Rockford, IL, USA). Specific complexes were revealed and quantified and densitometric blot analysis performed in three independent experiments [32 (link)].
Campione E., Di Prete M., Costanza G., Saggini A., Agostinelli S., Terrinoni A., Centofanti F., Rapanotti M.C., Bianchi L., Ferlosio A., Scioli M.G, & Orlandi A. (2023). Increased Occurrence of Cutaneous Leiomyomas and Dermatofibromas in Patients with Uterine Leiomyomas without Fumarate Hydratase Gene Mutations. Dermatopathology, 10(3), 231-243.
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4

Investigating TGF-β RII and Iβ3 Interaction

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To investigate the association of TGF-β RII and Iβ3, we performed Förster Resonance Energy Transfer (FRET) and confocal microscopy. Briefly, the donor antibody (anti Iβ3 (SantaCruz)) was labeled with Alexa Fluor® 488 Carboxylic Acid, Succinimidyl Ester (Life Technologies) (Iβ3-488) and the acceptor antibody (anti TGF-β RII (SantaCruz)) was labeled with Alexa Fluor® 546 Carboxylic Acid, Succinimidyl Ester (Life Technologies) (TGF-β RII-546) in a 2.25:1 molar ratio of antibody:dye overnight at 4°. Labelled antibody was purified with size exclusion chromatography using PD-10 Desalting Columns (GE Healthcare). MDA-MB-231, RWGT2, and PC3 cells were grown on discs of rigid and compliant 2D PURs. After 24 hours of culture, cells were fixed with 10% Formaldehyde in PBS and stained overnight at 4° with Iβ3-488, TGF-β RII-546, Iβ3-488 + TGF-β RII-546 or IgG control (1ug/1×106 cells). FRET experiments were performed on a BioTek Synergy 2 plate reader using excitation filter 485/20 and emission filter 590/35. Data were subtracted from the fluorescence of IgG control. Representative images of MDA-MB-231 cells grown on glass coverslips were taken with a Zeiss LSM 510 inverted confocal microscope. Images were obtained for Iβ3-488 (ex: 488, em: BP 505-550), TGF-β RII-546 (ex: 543, em: BP 560-615), colocalization (merge) and FRET (ex: 488, em: LP 585).
Page J.M., Merkel A.R., Ruppender N.S., Guo R., Dadwal U.C., Cannonier S., Basu S., Guelcher S.A, & Sterling J.A. (2015). Matrix Rigidity Regulates the Transition of Tumor Cells to a Bone-Destructive Phenotype through Integrin β3 and TGF-β Receptor Type II. Biomaterials, 64, 33-44.
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5

FRET Characterization of BMPR1 and Iβ1 Interaction

Cited 2 times
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To investigate the association of BMPR1 and Iβ1, we performed Förster Resonance Energy Transfer (FRET)23 (link), 27 (link). Briefly, the donor antibody (anti Iβ1 (SantaCruz)) was labeled with Alexa Fluor® 488 Carboxylic Acid, Succinimidyl Ester (Life Technologies) (Iβ1-488) and the acceptor antibody (anti TGF-β RII (SantaCruz)) was labeled with Alexa Fluor® 546 Carboxylic Acid, Succinimidyl Ester (Life Technologies) (BMPRI-546) in a 2.25:1 molar ratio of antibody:dye overnight at 4°C. Labelled antibody was purified with size exclusion chromatography using PD-10 Desalting Columns (GE Healthcare). Rat MSCs were plated on pre-soaked compliant (5 MPa) and rigid (266 MPa) PUR films. After 24 hours of culture, cells were fixed with 10% Formaldehyde in PBS and stained overnight at 4° with Iβ1-488 and Iβ1-488 + BMPRI-546 (1 ug/1×106 cells). FRET experiments were performed on a BioTek Synergy 2 plate reader using excitation filter 485/20 and emission filter 530/35.
Guo R., Lu S., Merkel A.R., Sterling J.A, & Guelcher S.A. (2016). Substrate Modulus Regulates Osteogenic Differentiation of Rat Mesenchymal Stem Cells through Integrin β1 and BMP Receptor Type IA. Journal of materials chemistry. B, Materials for biology and medicine, 4(20), 3584-3593.
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