Pdgfrβ

Manufactured by Cell Signaling Technology

Sourced in United States, United Kingdom, China

PDGFRβ is a tyrosine kinase receptor that plays a key role in cell signaling pathways. It is involved in the regulation of various cellular processes, including cell growth, proliferation, and differentiation. PDGFRβ is commonly used in research applications to study its function and role in different biological systems.

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Lab products found in correlation

Close spelling variants of this product

Anti-PDGFRβ (40 citations) P-PDGFRβ (17 citations) Rabbit anti-PDGFRβ (8 citations) PDGFRβ (28E1) (6 citations) Anti-phospho-PDGFRβ (5 citations) Anti-p-PDGFRβ (4 citations) Anti-PDGFRβ antibody (3 citations) PDGFRΒ antibody (2 citations) Total PDGFRβ (2 citations) PDGFRβ kinase (2 citations)

64 protocols using pdgfrβ

Quantitative Fluorescent Immunostaining of Pericytes

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A fluorescent double staining kit (G1235; Servicebio, Wuhan, China) based on tyramide signal amplification was performed in accordance with the manufacturer’s instructions. Primary antibodies for histological staining included CD31 (dilution 1 : 5000; GB13428; Servicebio) and PDGFR‐β (dilution 1 : 500; #3169; Cell Signaling, Danvers, MA, USA).
Purified pericytes were fixed, permeabilized, and subsequently blocked with BSA for 1 h. Cells were then incubated with antibodies against α‐SMA (dilution 1 : 100; ab7817; Abcam, Cambridge, UK), PDGFR‐β (dilution 1 : 100; #3169; Cell Signaling), neuron‐glial antigen 2 (NG2) (dilution 1 : 100; sc‐53389; Santa Cruz Biotechnology, Dallas, TX, USA), and CD13 (dilution 1 : 100; sc‐13536; Santa Cruz Biotechnology) overnight at 4 °C. The next day, the cells were washed and incubated with secondary Alexa Fluor 488 anti‐rabbit antibody (dilution 1 : 1000; 4412; Cell Signaling) or Alexa Fluor 594 anti‐mouse antibody (dilution 1 : 1000; 8890; Cell Signaling) for 1 h when protected from light. Nuclear staining was performed with 4′,6‐diamidino‐2‐phenylindole. The images were captured by high‐content analysis (Operetta; PerkinElmer, Waltham, MA, USA). Image analysis and fluorescence quantification were performed using columbus (PerkinElmer) and imagej (NIH, Bethesda, USA).

Tang L., Shi J., Yu M., Shan Y., Zhao J, & Sheng M. (2022). Isolation and characterization of peritoneal microvascular pericytes. FEBS Open Bio, 12(4), 784-797.

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Immunohistochemical Analysis of Mouse Lungs

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Mouse lungs were inflated and fixed in 2% paraformaldehyde, dehydrated in a series of increasing ethanol concentration washes, embedded in paraffin and sectioned. Antibodies used were anti-SM22α (goat anti-SM22α 1:200 Abcam), GFP (goat anti-GFP 1:100 Abcam, rabbit anti-GFP 1:100 Molecular Probe), Scgb1a1 (goat anti-Scgb1a1 1:20 Santa Cruz), SPC (rabbit-anti SPC 1:500 Chemicon), Pdgfrα (rabbit anti-Pdgfrα 1:50 Cell Signaling), Pdgfrβ (rabbit anti-Pdgfrβ 1:100 Cell Signaling), vimentin (rabbit anti-vimentin 1:100 Santa Crux), collagen type1 (rabbit anti-Col1 1:500 Abcam), Ki67 (rabbit anti-Ki67 1:50 Abcam), PCNA (mouse anti-PCNA 1:50 Biocare), PO4-Histone H3 (mouse anti-PO4-Histone H3 1:200 Cell Signaling), TubbIV (mouse anti-TubbIV 1:20 Biogenex), S100A4 (rabbit anti-S100A4 1:200 Abcam). LacZ staining of lungs was performed as previously described^{8 (link)}. The slide was imaged on a Zeiss LSM 710 confocal microscope and analyzed in ImageJ software.

Peng T., Frank D.B., Kadzik R.S., Morley M.P., Rathi K.S., Wang T., Zhou S., Cheng L., Lu M.M, & Morrisey E.E. (2015). Hedgehog actively maintains adult lung quiescence and regulates repair and regeneration. Nature, 526(7574), 578-582.

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Immunohistochemical Analysis of Mouse Lungs

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Western Blot Analysis of CCM3 Signaling

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Tissue or cells were lysed in 2x Laemmli buffer and boiled for 5 min at 100 °C followed by centrifugation at 20,000 × g for 15 min at 4 °C. The protein extracts were subjected to standard Western blot analysis which was performed. The following antibodies were used for western blotting: Rabbit polyclonal antibody against CCM3 was generated (Invitrogen) against full-length recombinant human CCM3 protein expressed and purified from Escherichia coli. β-actin (mouse, A1978) and β-actin (mouse, A5441) were from Sigma; p-Caveolin-1 (rabbit, 611339) was from BD Pharmingen; Abl (rabbit, 2862s), p-Akt (rabbit, 9271), Akt (rabbit, 9272), p-MLC2 (rabbit, 3674), PDGFR-β (rabbit, 3168), p-Tie2 (rabbit, 4221), p-Tie2 (rabbit, 4226), Tie2 (rabbit, 4224), and VEGFR2 (rabbit, 2479) were from Cell Signaling Technology. Caveolin-1 (rabbit, sc894) was from Santa Cruz. Angpt2 (rabbit, ab8452), p-Abl (rabbit, ab4717), and N-Cadherin (rabbit, ab76057) were from Abcam; Angpt2 (AF7186) was from R&D Systems. All primary antibodies were diluted 1:1000. For data presented in the same figure panel, the samples were derived from the same experiment and that gels/blots were processed in parallel. Uncropped blots and gel images were provided in the Source data file.

Zhou H.J., Qin L., Jiang Q., Murray K.N., Zhang H., Li B., Lin Q., Graham M., Liu X., Grutzendler J, & Min W. (2021). Caveolae-mediated Tie2 signaling contributes to CCM pathogenesis in a brain endothelial cell-specific Pdcd10-deficient mouse model. Nature Communications, 12, 504.

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Antibody Panel for Receptor Tyrosine Kinases

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Mouse monoclonal antibodies: anti-phospho-FAK(Tyr397) from BD Transduction (Lexington, KY); anti-EGFR and anti-phosphotyrosine clone 4G10, from Upstate Biotechnology (Lake Placid, NY); anti-β tubulin and anti-ERBB3 from Sigma-Aldrich (St. Louis MO); anti IGF-IRβ from Santa Cruz Biotechnology (Santa Cruz, CA). Rabbit polyclonal antibodies: anti-actin and anti-ERBB4 from Sigma; anti-phospho-FGFR (Tyr653/654), anti-phospho-HER2/ERBB2 (Tyr877), anti-phospho-HER4/ERBB4 (Tyr984) and anti-FAK from Cell Signaling (Beverly, MA); anti-PDGFR β and anti-PDGFRα from Upstate Biotechnology; anti-FGFR3 and anti-FGFR4 from Santa Cruz Biotechnology. Rabbit monoclonal antibodies: anti-phospho-PDGFRα (Tyr849)/PDGFRβ (Tyr857), anti-phospho-IGF-IRβ (Tyr1135/1136)/InsulinRβ (Tyr1150/1151), anti-phospho-HER3/ErbB3 (Tyr1289), anti-PDGFRβ and anti-HER2/ERBB2 from Cell Signaling.

Cassinelli G., Favini E., Dal Bo L., Tortoreto M., De Maglie M., Dagrada G., Pilotti S., Zunino F., Zaffaroni N, & Lanzi C. (2016). Antitumor efficacy of the heparan sulfate mimic roneparstat (SST0001) against sarcoma models involves multi-target inhibition of receptor tyrosine kinases. Oncotarget, 7(30), 47848-47863.

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Lung Tissue Histology and Immunophenotyping

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Lungs were inflated with 2% paraformaldehyde under constant pressure of 30 cm water and allowed to fix overnight. Tissue was embedded in paraffin and sectioned. Hematoxylin and eosin staining was performed to examine tissue morphology. Immunohistochemistry was used to detect protein expression using the following antibodies on paraffin sections: GFP (chicken, Aves, 1:500), GFP (goat, Abcam, 1:100), RFP (rabbit, Rockland, 1:250), Nkx2.1 (rabbit, Santa Cruz, 1:50), Sox2 (rabbit, Seven Hills, 1:500), Sox9 (rabbit, Santa Cruz, 1:100), Pecam (rat, HistoBioTec, 1:20), SM22α (goat, Abcam, 1:100), Pdgfrα (rabbit, Cell Signaling, 1:50), Pdgfrα (goat, R&D Systems, 1:50), Pdgfrβ (rabbit, Cell Signaling, 1:100), Pdgfrβ (goat, R&D Systems, 1:400), Scgb1a1 (goat, Santa Cruz, 1:20), Tubb4 (mouse, BioGenex, 1:20), Sftpc (rabbit, Millipore, 1:250), Sftpc (goat, Santa Cruz, 1:50), Pdpn (mouse, Hybridoma Bank, 1:50), Aqp5 (rabbit, Abcam, 1:100), and Ki67 (rabbit, Abcam, 1:50).

Frank D.B., Peng T., Zepp J., Snitow M., Vincent T., Penkala I.J., Cui Z., Herriges M.J., Morley M.P., Zhou S., Lu M.M, & Morrisey E.E. (2016). Emergence of a wave of Wnt signaling that regulates lung alveologenesis through controlling epithelial self-renewal and differentiation. Cell reports, 17(9), 2312-2325.

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Synthesis and Biological Evaluation of SC-43

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SC-43, or 1-(4-chloro-3-(trifluoromethyl)phenyl)-3-(3-(4-cyanophenoxy)phenyl) urea, was synthesized by Dr. Chung-Wai Shiau at National Yang-Ming University. Sorafenib (Nexavar) was kindly provided by Bayer HealthCare AG (Berlin, Germany). Antibodies for alpha-smooth muscle actin (α-SMA), P-STAT3 (Tyr705), STAT3, cyclin D1, glyceraldehyde-3-phosphate dehydrogenase, P-Smad2 (Ser465/467), P-Smad3 (Ser423/425), Smad2, Smad3, poly (ADP-ribose) polymerase (PARP), platelet-derived growth factor receptor (PDGFR)-β, P-PDGFR-β (Tyr857), and P-Akt (Ser473) were purchased from Cell Signaling (Danvers, MA, USA). Akt was purchased from Santa Cruz Biotechnology (San Diego, CA, USA). Furthermore, sodium vanadate was purchased from Cayman Chemical (Ann Arbor, MI, USA). PTP inhibitor III was purchased from Calbiochem (San Diego, CA, USA). Cremaphor and sodium stibogluconate were obtained from Sigma (Saint Louis, MO, USA).

Su T.H., Shiau C.W., Jao P., Yang N.J., Tai W.T., Liu C.J., Tseng T.C., Yang H.C., Liu C.H., Huang K.W., Hu T.C., Huang Y.J., Wu Y.M., Chen L.J., Chen P.J., Chen D.S., Chen K.F, & Kao J.H. (2017). Src-homology protein tyrosine phosphatase-1 agonist, SC-43, reduces liver fibrosis. Scientific Reports, 7, 1728.

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Immunohistochemical Analysis of Murine Stroke Model

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One day after permanent middle cerebral occlusion, mice were transcardially perfused with PBS followed by 4% paraformaldehyde and sections prepared as previously described.^{8 (link)} The primary antibodies used were rabbit anti-AQP4 (aquaporin 4; 1:1000, Millipore), chicken anti-GFP (green fluorescent protein; 1:1000, Abcam), rabbit anti-claudin 5 (1:1000, Abcam), mouse anti-NeuN (neuronal nuclei; 1:400, Millipore), rabbit anti-neural/glial antigen 2 (NG2; 1:200, Millipore), rabbit anti–platelet-derived growth factor receptor (PDGFR)-β (1:200, Cell Signaling), anti–platatelet endothelial cell adhesion molecule-1 (CD31; 1:400, BD), rabbit antivascular endothelial-cadherin (1:1000, Abcam), rabbit anti–ZO-1 (zonula occludens 1; 1:500, Fisher), and staining revealed using species-specific fluorophore-conjugated (Streptavidin Alexa 488, Molecular Probes; Cy3 or Cy5, Jackson) or biotin-conjugated secondary antibodies (Jackson). Biotinylated secondary antibodies were revealed using the ABC kit (Vector labs). 4’,6-diamidine-2’-phenylindole (1 μg/mL, Sigma) was used for counterstaining.

Özen I., Roth M., Barbariga M., Gaceb A., Deierborg T., Genové G, & Paul G. (2018). Loss of Regulator of G-Protein Signaling 5 Leads to Neurovascular Protection in Stroke. Stroke, 49(9), 2182-2190.

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Western Blot Analysis of Fibrosis Markers

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Cells were washed twice with PBS and scraped from the plates in RIPA buffer (50 mM Tris HCl pH 8, 150 mM NaCl, 1% NP-40, 0.5% sodium deoxycholate, and 0.1% SDS) containing a Protease Inhibitor Cocktail (Thermo Fisher Scientific). Proteins were electrophoresed in sample buffer on acrylamide gels and then transferred to polyvinylidene difluoride membranes (Clear Blot Membrane-P; ATTO Co., Ltd., Tokyo, Japan). Membranes were blocked with 0.5% TBST containing 3% non-fat milk, incubated with the primary antibodies (1:1000) overnight at 4°C, and then incubated with horseradish peroxidase-conjugated anti-rabbit antibodies (1:3000; Sigma-Aldrich, St. Louis, MO, USA). Blots were visualized using the ECL Western Blotting Detection System (GE Healthcare, Buckinghamshire, UK). β-actin was used as a loading control. Antibodies against α-SMA, COL1A1, PDGFRβ, and β-actin were purchased from Cell Signaling Technology (Boston, MA, USA).

Suzuki R., Asama H., Waragai Y., Takagi T., Hikichi T., Sugimoto M., Konno N., Watanabe K., Nakamura J., Kikuchi H., Sato Y., Marubashi S., Masamune A, & Ohira H. (2017). Fibrosis-related miRNAs as serum biomarkers for pancreatic ductal adenocarcinoma. Oncotarget, 9(4), 4451-4460.

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Protein Expression Analysis of PDGF Signaling

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Proteins were isolated from the ventricular homogenate or cells with lysis buffer (Beyotime Institute of Biotechnology, Shanghai, China) with PMSF. Equal amounts of protein were subjected to SDS-PAGE and transferred to PVDF membranes (Milliopore, Billerica, MA, USA). The membranes were blocked and then incubated with GAPDH (Proteintech, Rosemont, IL, USA), MMP-9, α-SMA, p-PDGFRα (Tyr720), PDGFRα (Abcam, Cambridge, MA, USA), p-PDGFRβ (Tyr740), PDGFRβ (Cell Signaling Technology, Danvers, MA, USA), PDGF-A, PDGF-B, PDGF-C and PDGF-D (Bioss, Beijing, China). Subsequently, the membranes were incubated with an HRP-conjugated secondary antibody (Thermo Fisher Scientific, Waltham, MA, USA) at room temperature for 1 h and were visualized using enhanced chemiluminescence reagents (Sigma-Aldrich) according to the manufacturer’s instruction.

Wang L.X., Yang X., Yue Y., Fan T., Hou J., Chen G.X., Liang M.Y, & Wu Z.K. (2017). Imatinib attenuates cardiac fibrosis by inhibiting platelet-derived growth factor receptors activation in isoproterenol induced model. PLoS ONE, 12(6), e0178619.

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