recombinant human tgfβ1  (R&D Systems)

 
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    Name:
    Recombinant Human TGF beta 1 Protein
    Description:
    The Recombinant Human TGF beta 1 Protein from R D Systems is derived from CHO The Recombinant Human TGF beta 1 Protein has been validated for the following applications Bioactivity
    Catalog Number:
    240-B-002
    Price:
    259
    Category:
    Proteins and Enzymes
    Source:
    CHO-derived Recombinant Human TGF-beta 1 Protein
    Applications:
    Bioactivity
    Purity:
    >97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie« Blue Staining.
    Conjugate:
    Unconjugated
    Size:
    2 ug
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    Structured Review

    R&D Systems recombinant human tgfβ1
    Recombinant Human TGF beta 1 Protein
    The Recombinant Human TGF beta 1 Protein from R D Systems is derived from CHO The Recombinant Human TGF beta 1 Protein has been validated for the following applications Bioactivity
    https://www.bioz.com/result/recombinant human tgfβ1/product/R&D Systems
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant human tgfβ1 - by Bioz Stars, 2021-05
    99/100 stars

    Images

    1) Product Images from "The Z-cad dual fluorescent sensor detects dynamic changes between the epithelial and mesenchymal cellular states"

    Article Title: The Z-cad dual fluorescent sensor detects dynamic changes between the epithelial and mesenchymal cellular states

    Journal: BMC Biology

    doi: 10.1186/s12915-016-0269-y

    The Z-cad sensor identifies differential plasticity in HMLER EMT subpopulations upon TGFβ1 exposure. a HMLER cells cultured for 24 days with TGFβ1 were sorted into EMT and Bulk –EMT groups and allowed to grow in the absence of TGFβ1 for 13 days. b Parental HMLER cells were grown sorted into EMT and Bulk –EMT groups and allowed to grow for 13 days. c HMLER EMT cells were grown in the presence of the indicated concentrations of decitabine (or vehicle) for 5 days. Medium was changed daily with fresh decitabine. Flow cytometry was performed and the EMT fluorescence signature is indicated ( n = 3 biological replicates for vehicle and 500 nM; n = 2 biological replicates for 100 nM). d qPCR analysis for the indicated genes at different decitabine concentrations is shown. Vehicle treated values were set to 1.0 for each gene. Each concentration was compared to vehicle and analyzed using an unpaired Student’s t test ( n = 3 biological replicates per group). * p value
    Figure Legend Snippet: The Z-cad sensor identifies differential plasticity in HMLER EMT subpopulations upon TGFβ1 exposure. a HMLER cells cultured for 24 days with TGFβ1 were sorted into EMT and Bulk –EMT groups and allowed to grow in the absence of TGFβ1 for 13 days. b Parental HMLER cells were grown sorted into EMT and Bulk –EMT groups and allowed to grow for 13 days. c HMLER EMT cells were grown in the presence of the indicated concentrations of decitabine (or vehicle) for 5 days. Medium was changed daily with fresh decitabine. Flow cytometry was performed and the EMT fluorescence signature is indicated ( n = 3 biological replicates for vehicle and 500 nM; n = 2 biological replicates for 100 nM). d qPCR analysis for the indicated genes at different decitabine concentrations is shown. Vehicle treated values were set to 1.0 for each gene. Each concentration was compared to vehicle and analyzed using an unpaired Student’s t test ( n = 3 biological replicates per group). * p value

    Techniques Used: Cell Culture, Flow Cytometry, Cytometry, Fluorescence, Real-time Polymerase Chain Reaction, Concentration Assay

    The Z-cad sensor identifies EMT induced by TGFβ1 in HMLER cells. a F-actin stress fibers increase during TGFβ1 compared to vehicle treatment (26 days) indicating EMT. Scale bar = 100 μm. b RNA analysis by qRT-PCR at indicated time points during vehicle or TGFβ1 treatment ( n = 3 biological replicates per time point). Vehicle-treated values were set to 1.0 for each gene and analyzed using an unpaired Student’s t test. c Fluorescent confocal microscopy indicating a gain of GFP and loss of RFP at 14 days of TGFβ1 versus vehicle treatment. Mesenchymal-appearing bright GFP cells are indicated by arrows . Scale bar = 20 μm. d Flow cytometric analysis of HMLER cells containing Z-cad sensor showing an increase in cells displaying GFP hi RFP low/neg EMT fluorescence signature during TGFβ1 treatment at the times indicated. e Quantitation of cells displaying the EMT signature in HMLER cells containing Z-cad dual sensor from d . Bar graphs depict the percentage of cells displaying the EMT fluorescence signature in TGFβ1- versus vehicle-treated groups ( n = 3 biological replicates per time point). Data were analyzed using an unpaired Student’s t test. * p value
    Figure Legend Snippet: The Z-cad sensor identifies EMT induced by TGFβ1 in HMLER cells. a F-actin stress fibers increase during TGFβ1 compared to vehicle treatment (26 days) indicating EMT. Scale bar = 100 μm. b RNA analysis by qRT-PCR at indicated time points during vehicle or TGFβ1 treatment ( n = 3 biological replicates per time point). Vehicle-treated values were set to 1.0 for each gene and analyzed using an unpaired Student’s t test. c Fluorescent confocal microscopy indicating a gain of GFP and loss of RFP at 14 days of TGFβ1 versus vehicle treatment. Mesenchymal-appearing bright GFP cells are indicated by arrows . Scale bar = 20 μm. d Flow cytometric analysis of HMLER cells containing Z-cad sensor showing an increase in cells displaying GFP hi RFP low/neg EMT fluorescence signature during TGFβ1 treatment at the times indicated. e Quantitation of cells displaying the EMT signature in HMLER cells containing Z-cad dual sensor from d . Bar graphs depict the percentage of cells displaying the EMT fluorescence signature in TGFβ1- versus vehicle-treated groups ( n = 3 biological replicates per time point). Data were analyzed using an unpaired Student’s t test. * p value

    Techniques Used: Quantitative RT-PCR, Confocal Microscopy, Flow Cytometry, Fluorescence, Quantitation Assay

    2) Product Images from "TFAP2A is a component of the ZEB1/2 network that regulates TGFB1-induced epithelial to mesenchymal transition"

    Article Title: TFAP2A is a component of the ZEB1/2 network that regulates TGFB1-induced epithelial to mesenchymal transition

    Journal: Biology Direct

    doi: 10.1186/s13062-017-0180-7

    TFAP2A overexpression in NMuMG modulates epithelial plasticity. a Expression of either GFP or TFAP2A was induced by 72 h doxycycline treatment in NMuMG cells stably transduced with either pCLX-GFP or pCLX-TFAP2A. Morphological changes and sparse cell arrangement are visible in phase contrast microscopy upon TFAP2A expression. Scale bar: 50 μm. b Gene expression log 2 fold changes of EMT markers (TFs) were calculated from mRNA-seq samples of doxycycline-induced, TGFβ1-treated (72 h, 2 ng/mL) pCLX-GFP (pCLX-GFP + TGF-beta), doxycycline-induced pCLX-TFAP2A (pCLX-TFAP2A), as well as of doxycycline-induced, TGFβ1-treated (72 h, 2 ng/mL) pCLX-TFAP2A (pCLX-TFAP2A + TGF-beta) cell lines relative to doxycycline-induced pCLX-GFP (pCLX-GFP) cell line. Shown are the mean log 2 fold changes (+/- 1 standard deviation) from two experiments. TFAP2A overexpression is apparent in both TFAP2A-induced samples ( dark green and dark blue ) but is not induced in cells treated with TGFβ1 alone ( light blue ). The EMT-inducing TFs have increased expression upon TFAP2A induction. * indicates a p -value ≤ 0.05 and ** a p -value ≤ 0.01 in a two-tailed t -test. c The transcriptional activities of TFAP2{A,C} and SNAI1..3 motifs in different conditions, as inferred with ISMARA from mRNA-seq data as described in ( b ). The two replicates from each condition are plotted next to each other
    Figure Legend Snippet: TFAP2A overexpression in NMuMG modulates epithelial plasticity. a Expression of either GFP or TFAP2A was induced by 72 h doxycycline treatment in NMuMG cells stably transduced with either pCLX-GFP or pCLX-TFAP2A. Morphological changes and sparse cell arrangement are visible in phase contrast microscopy upon TFAP2A expression. Scale bar: 50 μm. b Gene expression log 2 fold changes of EMT markers (TFs) were calculated from mRNA-seq samples of doxycycline-induced, TGFβ1-treated (72 h, 2 ng/mL) pCLX-GFP (pCLX-GFP + TGF-beta), doxycycline-induced pCLX-TFAP2A (pCLX-TFAP2A), as well as of doxycycline-induced, TGFβ1-treated (72 h, 2 ng/mL) pCLX-TFAP2A (pCLX-TFAP2A + TGF-beta) cell lines relative to doxycycline-induced pCLX-GFP (pCLX-GFP) cell line. Shown are the mean log 2 fold changes (+/- 1 standard deviation) from two experiments. TFAP2A overexpression is apparent in both TFAP2A-induced samples ( dark green and dark blue ) but is not induced in cells treated with TGFβ1 alone ( light blue ). The EMT-inducing TFs have increased expression upon TFAP2A induction. * indicates a p -value ≤ 0.05 and ** a p -value ≤ 0.01 in a two-tailed t -test. c The transcriptional activities of TFAP2{A,C} and SNAI1..3 motifs in different conditions, as inferred with ISMARA from mRNA-seq data as described in ( b ). The two replicates from each condition are plotted next to each other

    Techniques Used: Over Expression, Expressing, Stable Transfection, Transduction, Microscopy, Standard Deviation, Two Tailed Test

    TFAP2A expression and activity profile in the NMuMG EMT model. a - b NMuMG cells were treated with 2 ng/mL of TGFβ1 for 72 h and were stained for TFAP2A and F-Actin ( a ) and TFAP2A and E-cadherin ( b ). The merged panels represent colocalization of the imaged markers with the nucleus which was stained with DAPI and compared to controls. Scale bar represents 50 μm. c NMuMG cells were treated for 14 days with 2 ng/mL of TGFβ1. Quantitative RT-PCR of Tfap2a during the time course of this treatment indicates that Tfap2a mRNA levels are reduced upon EMT. The EMT markers E-cadherin (Cdh1), Fibronectin (Fn1), Occludin (Ocln), and Vimentin (Vim) follow the expected trend. d Two mRNA-seq samples from independent wells were prepared from a time course of NMuMG cells treated for 14 days with 2 ng/mL of TGFβ1, and the data was consequently analyzed with ISMARA [ 30 ]. The figure depicts the dynamics of TFAP2A/C transcriptional activity during the time course. The sequence logo of the TFAP2A/C binding motif is also indicated. e - f Lysates from NMuMG/E9 cells treated with 2 ng/mL of TGFβ1 for 72 h were probed for TFAP2A, GAPDH and Lamin B expression by WB and their levels compared with the expression levels of Actin and also to the Ponceau-stained membrane ( e ). The bar plot represents the densitometric quantification of the TFAP2A protein levels upon treatment compared to the control ( f ) ** indicates a p -value
    Figure Legend Snippet: TFAP2A expression and activity profile in the NMuMG EMT model. a - b NMuMG cells were treated with 2 ng/mL of TGFβ1 for 72 h and were stained for TFAP2A and F-Actin ( a ) and TFAP2A and E-cadherin ( b ). The merged panels represent colocalization of the imaged markers with the nucleus which was stained with DAPI and compared to controls. Scale bar represents 50 μm. c NMuMG cells were treated for 14 days with 2 ng/mL of TGFβ1. Quantitative RT-PCR of Tfap2a during the time course of this treatment indicates that Tfap2a mRNA levels are reduced upon EMT. The EMT markers E-cadherin (Cdh1), Fibronectin (Fn1), Occludin (Ocln), and Vimentin (Vim) follow the expected trend. d Two mRNA-seq samples from independent wells were prepared from a time course of NMuMG cells treated for 14 days with 2 ng/mL of TGFβ1, and the data was consequently analyzed with ISMARA [ 30 ]. The figure depicts the dynamics of TFAP2A/C transcriptional activity during the time course. The sequence logo of the TFAP2A/C binding motif is also indicated. e - f Lysates from NMuMG/E9 cells treated with 2 ng/mL of TGFβ1 for 72 h were probed for TFAP2A, GAPDH and Lamin B expression by WB and their levels compared with the expression levels of Actin and also to the Ponceau-stained membrane ( e ). The bar plot represents the densitometric quantification of the TFAP2A protein levels upon treatment compared to the control ( f ) ** indicates a p -value

    Techniques Used: Expressing, Activity Assay, Staining, Quantitative RT-PCR, Sequencing, Binding Assay, Western Blot

    3) Product Images from "Differential Regulation of Transforming Growth Factor ? Signaling Pathways by Notch in Human Endothelial Cells *"

    Article Title: Differential Regulation of Transforming Growth Factor ? Signaling Pathways by Notch in Human Endothelial Cells *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M109.011833

    NICD differentially affects TGFβ/Smad target gene expression. HMEC transduced with empty vector or NICD were left untreated ( UT ) or treated with 2.5 ng/ml of TGFβ1 for 2 h. The mRNA level of target genes of TGFβ/Smad1 ( A ), TGFβ/Smad2
    Figure Legend Snippet: NICD differentially affects TGFβ/Smad target gene expression. HMEC transduced with empty vector or NICD were left untreated ( UT ) or treated with 2.5 ng/ml of TGFβ1 for 2 h. The mRNA level of target genes of TGFβ/Smad1 ( A ), TGFβ/Smad2

    Techniques Used: Expressing, Transduction, Plasmid Preparation

    Smad3 occupancy on SBE and CSL sites in the promoters of Smad3/CSL target genes. HMEC with or without Dll4 co-culture were left untreated or treated with TGFβ1 for 1 h. Smad3 occupancy on SBE and/or CSL sites in PAI1 ( top ), ANKRD1 ( middle ), and
    Figure Legend Snippet: Smad3 occupancy on SBE and CSL sites in the promoters of Smad3/CSL target genes. HMEC with or without Dll4 co-culture were left untreated or treated with TGFβ1 for 1 h. Smad3 occupancy on SBE and/or CSL sites in PAI1 ( top ), ANKRD1 ( middle ), and

    Techniques Used: Co-Culture Assay

    Effects of TGFβ and Dll4-induced Notch activation on histone modification. HMEC with or without Dll4 co-culture were left untreated or treated with TGFβ1 for 2 h. Histone H4 acetylation ( AcH4 ) ( A ) and H3K4Me3 ( B ) were examined by ChIP
    Figure Legend Snippet: Effects of TGFβ and Dll4-induced Notch activation on histone modification. HMEC with or without Dll4 co-culture were left untreated or treated with TGFβ1 for 2 h. Histone H4 acetylation ( AcH4 ) ( A ) and H3K4Me3 ( B ) were examined by ChIP

    Techniques Used: Activation Assay, Modification, Co-Culture Assay, Chromatin Immunoprecipitation

    Effects of Dll4-induced Notch activation on TGFβ signaling. HMEC cocultured with Dll4-expressing HMEC at a 1:1 ratio were left untreated ( UT ) or treated with 2.5 ng/ml TGFβ1 for 1 h ( B and C ) or 2 h ( A , D , E , F , and G ). A , the mRNA level
    Figure Legend Snippet: Effects of Dll4-induced Notch activation on TGFβ signaling. HMEC cocultured with Dll4-expressing HMEC at a 1:1 ratio were left untreated ( UT ) or treated with 2.5 ng/ml TGFβ1 for 1 h ( B and C ) or 2 h ( A , D , E , F , and G ). A , the mRNA level

    Techniques Used: Activation Assay, Expressing

    4) Product Images from "De-repression of the RAC activator ELMO1 in cancer stem cells drives progression of TGFβ-deficient squamous cell carcinoma from transition zones"

    Article Title: De-repression of the RAC activator ELMO1 in cancer stem cells drives progression of TGFβ-deficient squamous cell carcinoma from transition zones

    Journal: eLife

    doi: 10.7554/eLife.22914

    Dock2 is not a direct target of TGFβ signaling via SMAD3. ( A ) Promoter analysis using MatInspector (Genomatrix) revealed five putative SMAD- responsive elements in the Dock2 promoter. The consensus SMAD-binding element (SBE) sequence GTCT was identified 207, 497, 559 and 709 base pairs (bp) upstream of the Dock2 transcriptional start site, and the consensus TGFβ-inhibitory site (TIE) GNNTTGGNGN was identified 266 bp upstream of the D ock2 transcriptional start site. Primers were designed to flank these sites (purple arrows). ( B ) Chromatin immunoprecipitation with an anti-SMAD3 antibody failed to isolate DNA fragments that were amplified by the primers designed to flank any of these sites on the Dock2 promoter, after overexpressing SMAD3 in NIH3T3 cells and treating with TGFβ1 (2 ng/ml) for 24 hr. Non-template (NTC) and no-antibody (no Ab) controls were used to verify the specificity of binding. DOI: http://dx.doi.org/10.7554/eLife.22914.016
    Figure Legend Snippet: Dock2 is not a direct target of TGFβ signaling via SMAD3. ( A ) Promoter analysis using MatInspector (Genomatrix) revealed five putative SMAD- responsive elements in the Dock2 promoter. The consensus SMAD-binding element (SBE) sequence GTCT was identified 207, 497, 559 and 709 base pairs (bp) upstream of the Dock2 transcriptional start site, and the consensus TGFβ-inhibitory site (TIE) GNNTTGGNGN was identified 266 bp upstream of the D ock2 transcriptional start site. Primers were designed to flank these sites (purple arrows). ( B ) Chromatin immunoprecipitation with an anti-SMAD3 antibody failed to isolate DNA fragments that were amplified by the primers designed to flank any of these sites on the Dock2 promoter, after overexpressing SMAD3 in NIH3T3 cells and treating with TGFβ1 (2 ng/ml) for 24 hr. Non-template (NTC) and no-antibody (no Ab) controls were used to verify the specificity of binding. DOI: http://dx.doi.org/10.7554/eLife.22914.016

    Techniques Used: Binding Assay, Sequencing, Chromatin Immunoprecipitation, Amplification

    Related Articles

    Activation Assay:

    Article Title: Nintedanib selectively inhibits the activation and tumour-promoting effects of fibroblasts from lung adenocarcinoma patients
    Article Snippet: All experiments with fibroblasts were carried out on tissue culture plastic substrata coated with 0.1 mg ml−1 collagen-I solution (Millipore, Billerica, MA, USA) overnight at 4 °C. .. To induce either proliferation or activation, fibroblasts were stimulated with 10% FBS (Gibco, Waltham, MA, USA) or 2.5 ng ml−1 human recombinant human TGF-β 1 (R & D Systems, Minneapolis, MN, USA), respectively, concomitantly with increasing doses of nintedanib. .. Nintedanib (BIBF 1120) was provided by Boehringer Ingelheim Pharma GmbH & Co (Vienna, Austria), was diluted in DMSO and used at concentrations 0.5–5 μ M based on previous studies ( ; ; ; ).

    Recombinant:

    Article Title: Nintedanib selectively inhibits the activation and tumour-promoting effects of fibroblasts from lung adenocarcinoma patients
    Article Snippet: All experiments with fibroblasts were carried out on tissue culture plastic substrata coated with 0.1 mg ml−1 collagen-I solution (Millipore, Billerica, MA, USA) overnight at 4 °C. .. To induce either proliferation or activation, fibroblasts were stimulated with 10% FBS (Gibco, Waltham, MA, USA) or 2.5 ng ml−1 human recombinant human TGF-β 1 (R & D Systems, Minneapolis, MN, USA), respectively, concomitantly with increasing doses of nintedanib. .. Nintedanib (BIBF 1120) was provided by Boehringer Ingelheim Pharma GmbH & Co (Vienna, Austria), was diluted in DMSO and used at concentrations 0.5–5 μ M based on previous studies ( ; ; ; ).

    Article Title: 20S-Hydroxyvitamin D3, Noncalcemic Product of CYP11A1 Action on Vitamin D3, Exhibits Potent Antifibrogenic Activity in Vivo
    Article Snippet: Human dermal fibroblasts were isolated from biopsies of a scleroderma patient and from normal donors and were grown as described previously ( , ). .. The confluent fibroblasts were preincubated in serum-free media for 24 hours, and vitamin D hydroxyderivatives (10−9 or 10−10 M) were added to 3 replicate wells 2 hours prior to addition of recombinant human TGF-β1 (R & D Systems, Minneapolis, Minnesota) to a final concentration of 5 ng/mL. ..

    Article Title: Transforming Growth Factor-?1 Downregulates Vascular Endothelial Growth Factor-D Expression in Human Lung Fibroblasts via the Jun NH2-Terminal Kinase Signaling Pathway
    Article Snippet: Both NLF and MRC-5 cells were maintained in Dulbecco’s modified Eagle medium (DMEM) supplemented with 10% fetal bovine serum (FBS), 100 U/mL penicillin and 100 μg/mL streptomycin (Life Technologies, Carlsbad, CA, USA). .. Cells were incubated at 37°C in a humidified 5% CO2 atmosphere and were serum-starved for 24 h before they were stimulated with recombinant human TGF-β1 (5 ng/mL unless otherwise stated) (R & D Systems, Minneapolis, MN, USA) or vehicle for the indicated times. .. To examine the downstream signaling molecules that mediate the effect of TGF-β1 on VEGF-D transcription, MRC-5 cells were pre-treated with selective inhibitors of activin receptor–like kinase (ALK)-5 (SB431542, 10 μmol/L [inhibitors and amounts given in parentheses in this sentence]) (R & D Systems), mitogen-activated protein kinase kinase 1 and 2 (MEK1/2) (UO126, 10 μmol/L) (Cell Signaling Technology, Danvers, MA, USA), phosphatidylinositol 3-kinase (PI3K)/Akt (wortmannin, 100 nmol/L) (Cell Signaling Technology), Jun NH2 -terminal kinase (JNK) (SP600125, 5 μmol/L) (Cell Signaling Technology) or p38 mitogen-activated protein kinase (p38MAPK) (SB203580, 10 μmol/L) (R & D Systems) 1 h before the addition of TGF-β1.

    Article Title: TGF-β1 Alters Esophageal Epithelial Barrier Function by Attenuation of Claudin-7 in Eosinophilic Esophagitis
    Article Snippet: Twenty-four hours after the cells were plated, they were washed and treated with SB431542, a selective inhibitor of TGF-β type 1 receptor (S4317, Sigma Aldrich, St. Louis, MO, 5μm) for 4 hours. .. After 4 hours, the cells were treated with recombinant human TGF-β1 (R & D Systems, Minneapolis, MN, 10 ng/ml) in combination with the selective TGF-β type 1 receptor inhibitor (S4317, Sigma Aldrich, St. Louis, MO, 5μm) for 48 hours. .. Cells were harvested for mRNA analysis using RLT buffer from Qiagen RNeasy kits (Qiagen, Valencia, CA).

    Article Title: TGF-β1 regulates cell fate during epithelial-mesenchymal transition by upregulating survivin
    Article Snippet: .. Antibodies and reagents Human recombinant TGF-β 1 was purchased from R & D Systems (Minneapolis, MN, USA). .. Specific inhibitors of MEK (PD98059), PI3K (LY294002), and Rho (Hydroxyfasudil) were obtained from Calbiochem (La Jolla, CA, USA).

    Article Title: Transdifferentiation of alveolar epithelial type II to type I cells is controlled by opposing TGF-β and BMP signaling
    Article Snippet: Vectorshield mounting medium for fluorescence was purchased from Vector Laboratories (Burlingame, CA). .. Recombinant human TGF-β1 and BMP-4 were obtained from R & D Systems (Minneapolis, MN). .. Mouse ATII cells were isolated from adult C57BL/6 mice using dispase with agarose instillation, filtration, and then immunodepletion of CD16/CD32 and CD45 ( ).

    Article Title: Smad4-dependent TGF-? Signaling Suppresses RON Receptor Tyrosine Kinase-dependent Motility and Invasion of Pancreatic Cancer Cells *
    Article Snippet: BxPC-3 cells were maintained in RPMI 1640 medium, and other cell lines were grown in Dulbecco's modified Eagle's medium; each medium was supplemented with 10% fetal bovine serum. .. Human recombinant TGF-β1 was purchased from R & D Systems (Minneapolis, MN). .. The TGF-β receptor type I kinase inhibitor (RIKI) and the proteasome inhibitor MG132 were purchased from Calbiochem.

    Concentration Assay:

    Article Title: 20S-Hydroxyvitamin D3, Noncalcemic Product of CYP11A1 Action on Vitamin D3, Exhibits Potent Antifibrogenic Activity in Vivo
    Article Snippet: Human dermal fibroblasts were isolated from biopsies of a scleroderma patient and from normal donors and were grown as described previously ( , ). .. The confluent fibroblasts were preincubated in serum-free media for 24 hours, and vitamin D hydroxyderivatives (10−9 or 10−10 M) were added to 3 replicate wells 2 hours prior to addition of recombinant human TGF-β1 (R & D Systems, Minneapolis, Minnesota) to a final concentration of 5 ng/mL. ..

    Incubation:

    Article Title: Transforming Growth Factor-?1 Downregulates Vascular Endothelial Growth Factor-D Expression in Human Lung Fibroblasts via the Jun NH2-Terminal Kinase Signaling Pathway
    Article Snippet: Both NLF and MRC-5 cells were maintained in Dulbecco’s modified Eagle medium (DMEM) supplemented with 10% fetal bovine serum (FBS), 100 U/mL penicillin and 100 μg/mL streptomycin (Life Technologies, Carlsbad, CA, USA). .. Cells were incubated at 37°C in a humidified 5% CO2 atmosphere and were serum-starved for 24 h before they were stimulated with recombinant human TGF-β1 (5 ng/mL unless otherwise stated) (R & D Systems, Minneapolis, MN, USA) or vehicle for the indicated times. .. To examine the downstream signaling molecules that mediate the effect of TGF-β1 on VEGF-D transcription, MRC-5 cells were pre-treated with selective inhibitors of activin receptor–like kinase (ALK)-5 (SB431542, 10 μmol/L [inhibitors and amounts given in parentheses in this sentence]) (R & D Systems), mitogen-activated protein kinase kinase 1 and 2 (MEK1/2) (UO126, 10 μmol/L) (Cell Signaling Technology, Danvers, MA, USA), phosphatidylinositol 3-kinase (PI3K)/Akt (wortmannin, 100 nmol/L) (Cell Signaling Technology), Jun NH2 -terminal kinase (JNK) (SP600125, 5 μmol/L) (Cell Signaling Technology) or p38 mitogen-activated protein kinase (p38MAPK) (SB203580, 10 μmol/L) (R & D Systems) 1 h before the addition of TGF-β1.

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  • 95
    R&D Systems tgf β1
    Expressions of <t>TGF-β1</t> and IL-10 protein
    Tgf β1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tgf β1/product/R&D Systems
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tgf β1 - by Bioz Stars, 2021-05
    95/100 stars
      Buy from Supplier

    99
    R&D Systems recombinant human tgf β1
    The transforming growth factor <t>(TGF)-β</t> pathway is activated during culture of mouse ATII cells. ATII cells were freshly isolated (D0) or cultured for 7 days on tissue culture plastic. The mRNA expression levels of <t>Tgf-β1</t> , Tgf-β2
    Recombinant Human Tgf β1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant human tgf β1/product/R&D Systems
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant human tgf β1 - by Bioz Stars, 2021-05
    99/100 stars
      Buy from Supplier

    N/A
    The ProDots Recombinant Human TGF beta 1 Protein from R D Systems is derived from CHO The ProDots Recombinant Human TGF beta 1 Protein has been validated for the following
      Buy from Supplier

    N/A
    The Recombinant Human TGF beta RIII Protein from R D Systems is derived from NS0 The Recombinant Human TGF beta RIII Protein has been validated for the following applications Bioactivity
      Buy from Supplier

    Image Search Results


    Expressions of TGF-β1 and IL-10 protein

    Journal: Annals of Dermatology

    Article Title: The Expressions of TGF-?1 and IL-10 in Cultured Fibroblasts after ALA-IPL Photodynamic Treatment

    doi: 10.5021/ad.2011.23.1.19

    Figure Lengend Snippet: Expressions of TGF-β1 and IL-10 protein

    Article Snippet: The TGF-β1 and IL-10 ELISA kits and the monoclonal antibodies against these molecules were obtained from R & D systems (USA).

    Techniques:

    Receptor CD36 is required for apoptotic cells induced TGF-β1 mRNA and protein expression. A, CD36 protein expression in RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) for 24 h was analyzed by Western blotting with anti-CD36 (MF3) antibody, and band density was normalized to GAPDH. B, RAWTβRII cells transfected with CD36-target siRNA or control vehicle (Ctr siRNA) for 24 h were stimulated with apoptotic or viable Jurkat cells. C, Apoptotic Jurkat cells were pretreated with annexin V for 45 min and incubated with RAWTβRII transfected with CD36-target siRNA or control siRNA (Ctr siRNA). TGF-β1 mRNA expression or secreted TGF-β1 protein was analyzed as in Figure 1. D, RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) were treated with either LPS (25 ng/ml) or PMA (50 nM). The expression of TGF-β1 mRNA was analyzed as above. Values represent means ± SD of five separate experiments. ns, no significant; *, P

    Journal: PLoS ONE

    Article Title: Induction of TGF-?1 Synthesis by Macrophages in Response to Apoptotic Cells Requires Activation of the Scavenger Receptor CD36

    doi: 10.1371/journal.pone.0072772

    Figure Lengend Snippet: Receptor CD36 is required for apoptotic cells induced TGF-β1 mRNA and protein expression. A, CD36 protein expression in RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) for 24 h was analyzed by Western blotting with anti-CD36 (MF3) antibody, and band density was normalized to GAPDH. B, RAWTβRII cells transfected with CD36-target siRNA or control vehicle (Ctr siRNA) for 24 h were stimulated with apoptotic or viable Jurkat cells. C, Apoptotic Jurkat cells were pretreated with annexin V for 45 min and incubated with RAWTβRII transfected with CD36-target siRNA or control siRNA (Ctr siRNA). TGF-β1 mRNA expression or secreted TGF-β1 protein was analyzed as in Figure 1. D, RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) were treated with either LPS (25 ng/ml) or PMA (50 nM). The expression of TGF-β1 mRNA was analyzed as above. Values represent means ± SD of five separate experiments. ns, no significant; *, P

    Article Snippet: Antibodies and reagents TGF-β1 was from R & D Systems (Minneapolis, MN).

    Techniques: Expressing, Transfection, Western Blot, Incubation

    Both Lyn kinase and ERK1/2 MAPK are required for TGF-β1 synthesis induced by activating anti-CD36 mIgA. A, RAWTβRII cells were stimulated with activating anti-CD36 mIgA (2 µg/ml) for the times indicated. Total cell lysates were immunoblotted for phospho-Lyn kinase and the band density was normalized to total Lyn kinase. B, RAWTβRII cells were pretreated with the src-family kinase inhibitor PP2 (0.001 to 100 µM) for 2 h and then stimulated with anti-CD36 mIgA (2 µg/ml). After 6 h, TGF-β1 mRNA expression was analyzed by real-time PCR and normalized to GAPDH. Total TGF-β1 in the conditioned medium was analyzed by ELISA after 18 h. C, A time course of ERK1/2 phosphorylation was assessed by Western blotting in RAWTβRII cells treated with anti-CD36 mIgA (2 µg/ml). Phospho-ERK1/2 band density was normalized to total ERK1/2. D, RAWTβRII cells were preincubated with MEK kinase inhibitor U0126 or inactive analogue U0124 for 2 h and then stimulated with anti-CD36 mIgA for 6 h to detect TGF-β1 mRNA expression or for 18 h to detect secreted TGF-β1 protein as in Figure 1. Values represent means ± SD of six separate experiments.

    Journal: PLoS ONE

    Article Title: Induction of TGF-?1 Synthesis by Macrophages in Response to Apoptotic Cells Requires Activation of the Scavenger Receptor CD36

    doi: 10.1371/journal.pone.0072772

    Figure Lengend Snippet: Both Lyn kinase and ERK1/2 MAPK are required for TGF-β1 synthesis induced by activating anti-CD36 mIgA. A, RAWTβRII cells were stimulated with activating anti-CD36 mIgA (2 µg/ml) for the times indicated. Total cell lysates were immunoblotted for phospho-Lyn kinase and the band density was normalized to total Lyn kinase. B, RAWTβRII cells were pretreated with the src-family kinase inhibitor PP2 (0.001 to 100 µM) for 2 h and then stimulated with anti-CD36 mIgA (2 µg/ml). After 6 h, TGF-β1 mRNA expression was analyzed by real-time PCR and normalized to GAPDH. Total TGF-β1 in the conditioned medium was analyzed by ELISA after 18 h. C, A time course of ERK1/2 phosphorylation was assessed by Western blotting in RAWTβRII cells treated with anti-CD36 mIgA (2 µg/ml). Phospho-ERK1/2 band density was normalized to total ERK1/2. D, RAWTβRII cells were preincubated with MEK kinase inhibitor U0126 or inactive analogue U0124 for 2 h and then stimulated with anti-CD36 mIgA for 6 h to detect TGF-β1 mRNA expression or for 18 h to detect secreted TGF-β1 protein as in Figure 1. Values represent means ± SD of six separate experiments.

    Article Snippet: Antibodies and reagents TGF-β1 was from R & D Systems (Minneapolis, MN).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Western Blot

    Apoptotic cells induce TGF-β1 production in RAWTβRII macrophages. A, RAW 264.7 macrophages were stably transfected with truncated TGF-β receptor II (RAWTβRII) or empty vector (RAWV). After 48 h, the cells were incubated with TGF-β1 (25 ng/ml) for 6 h. TGF-β1 mRNA expression which was normalized to GAPDH, was measured by real-time PCR and expressed as fold enhancement. B, Human Jurkat T cells were stimulated with UV-irradiation to induce apoptosis. Surface PS exposure was assessed by annexin V staining and cell permeability with propidium iodide as analyzed by flow cytometry (shown as a representative dot plot from five independent experiments). C, Apoptotic or viable Jurkat cells were pretreated with annexin V for 45 min, and incubated with RAWTβRII macrophages for 6 h to measure TGF-β1 mRNA expression. D, Total TGF-β1 in the conditioned medium was analyzed by ELISA after 18 h of co-culture. Values represent means ± SD of five separate experiments. ***, P

    Journal: PLoS ONE

    Article Title: Induction of TGF-?1 Synthesis by Macrophages in Response to Apoptotic Cells Requires Activation of the Scavenger Receptor CD36

    doi: 10.1371/journal.pone.0072772

    Figure Lengend Snippet: Apoptotic cells induce TGF-β1 production in RAWTβRII macrophages. A, RAW 264.7 macrophages were stably transfected with truncated TGF-β receptor II (RAWTβRII) or empty vector (RAWV). After 48 h, the cells were incubated with TGF-β1 (25 ng/ml) for 6 h. TGF-β1 mRNA expression which was normalized to GAPDH, was measured by real-time PCR and expressed as fold enhancement. B, Human Jurkat T cells were stimulated with UV-irradiation to induce apoptosis. Surface PS exposure was assessed by annexin V staining and cell permeability with propidium iodide as analyzed by flow cytometry (shown as a representative dot plot from five independent experiments). C, Apoptotic or viable Jurkat cells were pretreated with annexin V for 45 min, and incubated with RAWTβRII macrophages for 6 h to measure TGF-β1 mRNA expression. D, Total TGF-β1 in the conditioned medium was analyzed by ELISA after 18 h of co-culture. Values represent means ± SD of five separate experiments. ***, P

    Article Snippet: Antibodies and reagents TGF-β1 was from R & D Systems (Minneapolis, MN).

    Techniques: Stable Transfection, Transfection, Plasmid Preparation, Incubation, Expressing, Real-time Polymerase Chain Reaction, Irradiation, Staining, Permeability, Flow Cytometry, Cytometry, Enzyme-linked Immunosorbent Assay, Co-Culture Assay

    Lyn kinase and ERK1/2 MAPK act by separate pathways for activating anti-CD36 mIgA-induced TGF-β1 synthesis. A, RAWTβRII cells were pretreated with inhibitor PP2 (30 µM) for 2 h prior to stimulation with anti-CD36 mIgA (2 µg/ml) for 60 min. Phosphorylation of Lyn and ERK1/2 were analyzed by Western blotting using total cell lysates. B, RAWTβRII cells were pretreated with inhibitor U0126 or analogue U0124 (1.0 µM) for 2 h and then incubated with anti-CD36 mIgA (2 µg/ml) for 90 min. Total cell lysates were used to analyze phosphorylation of Lyn and ERK1/2. Relative values for phosphorylated kinase versus total kinase were determined by densitometry and expressed as means ± SD of five separate experiments. *** P

    Journal: PLoS ONE

    Article Title: Induction of TGF-?1 Synthesis by Macrophages in Response to Apoptotic Cells Requires Activation of the Scavenger Receptor CD36

    doi: 10.1371/journal.pone.0072772

    Figure Lengend Snippet: Lyn kinase and ERK1/2 MAPK act by separate pathways for activating anti-CD36 mIgA-induced TGF-β1 synthesis. A, RAWTβRII cells were pretreated with inhibitor PP2 (30 µM) for 2 h prior to stimulation with anti-CD36 mIgA (2 µg/ml) for 60 min. Phosphorylation of Lyn and ERK1/2 were analyzed by Western blotting using total cell lysates. B, RAWTβRII cells were pretreated with inhibitor U0126 or analogue U0124 (1.0 µM) for 2 h and then incubated with anti-CD36 mIgA (2 µg/ml) for 90 min. Total cell lysates were used to analyze phosphorylation of Lyn and ERK1/2. Relative values for phosphorylated kinase versus total kinase were determined by densitometry and expressed as means ± SD of five separate experiments. *** P

    Article Snippet: Antibodies and reagents TGF-β1 was from R & D Systems (Minneapolis, MN).

    Techniques: Activated Clotting Time Assay, Western Blot, Incubation

    Lyn kinase and ERK1/2 are involved in CD36 mediated TGF-β1 induction by apoptotic cells. A, RAWTβRII cells were cultured in the presence of viable or apoptotic Jurkat cells for the time indicated. Total cell lysates were used for analyzing phosphorylation of ERK1/2 MAPK and Lyn kinase by Western blotting. B, RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) for 24 h were incubated with apoptotic Jurkat cells for 60 or 90 min to analyze phosphorylation of Lyn kinase or ERK1/2, respectively. C, RAWTβRII cells were preincubated with PP2 (30 µM) or U0126 (1 µM) for 2h and then co-cultured with apoptotic Jurkat cells. TGF-β1 mRNA expression or secreted TGF-β1 protein was analyzed as in Figure 1. Values represent means ± SD of six separate experiments. ***, P

    Journal: PLoS ONE

    Article Title: Induction of TGF-?1 Synthesis by Macrophages in Response to Apoptotic Cells Requires Activation of the Scavenger Receptor CD36

    doi: 10.1371/journal.pone.0072772

    Figure Lengend Snippet: Lyn kinase and ERK1/2 are involved in CD36 mediated TGF-β1 induction by apoptotic cells. A, RAWTβRII cells were cultured in the presence of viable or apoptotic Jurkat cells for the time indicated. Total cell lysates were used for analyzing phosphorylation of ERK1/2 MAPK and Lyn kinase by Western blotting. B, RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) for 24 h were incubated with apoptotic Jurkat cells for 60 or 90 min to analyze phosphorylation of Lyn kinase or ERK1/2, respectively. C, RAWTβRII cells were preincubated with PP2 (30 µM) or U0126 (1 µM) for 2h and then co-cultured with apoptotic Jurkat cells. TGF-β1 mRNA expression or secreted TGF-β1 protein was analyzed as in Figure 1. Values represent means ± SD of six separate experiments. ***, P

    Article Snippet: Antibodies and reagents TGF-β1 was from R & D Systems (Minneapolis, MN).

    Techniques: Cell Culture, Western Blot, Transfection, Incubation, Expressing

    Stimulation with activating anti-CD36 mIgA induces TGF-β1 synthesis. A, RAWTβRII cells were cultured with activating anti-CD36 (JC63.1) mIgA or isotype control (2 µg/ml) for the times indicated. TGF-β1 mRNA expression or secreted TGF-β1 protein was analyzed as in Figure 1. B, RAWTβRII cells were pre-treated with the indicated concentrations of actinomycin D or cycloheximide for 1 h, before stimulation for 6 h and TGF-β1 mRNA expression was analyzed as above. C, RAWTβRII cells were cultured in the presence of PMA (50 nM) for 18 h to increase the steady state TGF-β1 mRNA level, and then the cells were incubated with actinomycin D (10 µg/ml) in the presence or absence of anti-CD36 mIgA (2 µg/ml) for the times indicated. D, RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) for 24 h were incubated with anti-CD36 mIgA (2 µg/ml) or isotype control (2 µg/ml) for 6 h or 18 h to analyze TGF-β1 mRNA expression or secreted total TGF-β1 protein respectively, as in Figure 1. Values represent means ± SD of five separate experiments. **, P

    Journal: PLoS ONE

    Article Title: Induction of TGF-?1 Synthesis by Macrophages in Response to Apoptotic Cells Requires Activation of the Scavenger Receptor CD36

    doi: 10.1371/journal.pone.0072772

    Figure Lengend Snippet: Stimulation with activating anti-CD36 mIgA induces TGF-β1 synthesis. A, RAWTβRII cells were cultured with activating anti-CD36 (JC63.1) mIgA or isotype control (2 µg/ml) for the times indicated. TGF-β1 mRNA expression or secreted TGF-β1 protein was analyzed as in Figure 1. B, RAWTβRII cells were pre-treated with the indicated concentrations of actinomycin D or cycloheximide for 1 h, before stimulation for 6 h and TGF-β1 mRNA expression was analyzed as above. C, RAWTβRII cells were cultured in the presence of PMA (50 nM) for 18 h to increase the steady state TGF-β1 mRNA level, and then the cells were incubated with actinomycin D (10 µg/ml) in the presence or absence of anti-CD36 mIgA (2 µg/ml) for the times indicated. D, RAWTβRII cells transfected with CD36-target siRNA or control siRNA (Ctr siRNA) for 24 h were incubated with anti-CD36 mIgA (2 µg/ml) or isotype control (2 µg/ml) for 6 h or 18 h to analyze TGF-β1 mRNA expression or secreted total TGF-β1 protein respectively, as in Figure 1. Values represent means ± SD of five separate experiments. **, P

    Article Snippet: Antibodies and reagents TGF-β1 was from R & D Systems (Minneapolis, MN).

    Techniques: Cell Culture, Expressing, Incubation, Transfection

    The transforming growth factor (TGF)-β pathway is activated during culture of mouse ATII cells. ATII cells were freshly isolated (D0) or cultured for 7 days on tissue culture plastic. The mRNA expression levels of Tgf-β1 , Tgf-β2

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    Article Title: Transdifferentiation of alveolar epithelial type II to type I cells is controlled by opposing TGF-β and BMP signaling

    doi: 10.1152/ajplung.00032.2013

    Figure Lengend Snippet: The transforming growth factor (TGF)-β pathway is activated during culture of mouse ATII cells. ATII cells were freshly isolated (D0) or cultured for 7 days on tissue culture plastic. The mRNA expression levels of Tgf-β1 , Tgf-β2

    Article Snippet: Recombinant human TGF-β1 and BMP-4 were obtained from R & D Systems (Minneapolis, MN).

    Techniques: Isolation, Cell Culture, Expressing

    TGF-β1 treatment promotes ATII transdifferentiation mainly by promoting loss of ATII phenotype. ATII cells were cultured in the absence or presence of human (h) TGF-β1 (4 ng/ml) through 7 days. A : the mRNA expression of Sftpa , Sftpb , and

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    Article Title: Transdifferentiation of alveolar epithelial type II to type I cells is controlled by opposing TGF-β and BMP signaling

    doi: 10.1152/ajplung.00032.2013

    Figure Lengend Snippet: TGF-β1 treatment promotes ATII transdifferentiation mainly by promoting loss of ATII phenotype. ATII cells were cultured in the absence or presence of human (h) TGF-β1 (4 ng/ml) through 7 days. A : the mRNA expression of Sftpa , Sftpb , and

    Article Snippet: Recombinant human TGF-β1 and BMP-4 were obtained from R & D Systems (Minneapolis, MN).

    Techniques: Cell Culture, Expressing

    TGF-β and BMP signaling antagonizes each other during culture. Primary ATII cells were treated with hTGF-β1 (4 ng/ml) ( A ) or hBMP-4 (200 ng/ml) ( B ). Cells treated with TGF-β1 were harvested on days 1 and 3 , whereas cells treated

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    Article Title: Transdifferentiation of alveolar epithelial type II to type I cells is controlled by opposing TGF-β and BMP signaling

    doi: 10.1152/ajplung.00032.2013

    Figure Lengend Snippet: TGF-β and BMP signaling antagonizes each other during culture. Primary ATII cells were treated with hTGF-β1 (4 ng/ml) ( A ) or hBMP-4 (200 ng/ml) ( B ). Cells treated with TGF-β1 were harvested on days 1 and 3 , whereas cells treated

    Article Snippet: Recombinant human TGF-β1 and BMP-4 were obtained from R & D Systems (Minneapolis, MN).

    Techniques:

    Vitamin D hydroxyderivatives down-regulate mRNAs of types I and III collagens and hyaluronan synthase 2 in TGFβ1-stimulated fibroblasts. Expression of COL1A2 mRNA in line Fib1 treated with 10 −10 M vitamin D hydroxy-derivatives (A); COL3A1 mRNA in line Fib1 treated with 10 −8 M vitamin D hydroxy-derivatives (B); and HAS2 in line Z4 treated with 10 −8 M vitamin D hydroxyderivatives (C) are shown. Results are expressed as mean ± SD, with P values of EtOH + TGF-β1 vs different treatments as indicated above connecting lines.

    Journal: The Journal of Clinical Endocrinology and Metabolism

    Article Title: 20S-Hydroxyvitamin D3, Noncalcemic Product of CYP11A1 Action on Vitamin D3, Exhibits Potent Antifibrogenic Activity in Vivo

    doi: 10.1210/jc.2012-3074

    Figure Lengend Snippet: Vitamin D hydroxyderivatives down-regulate mRNAs of types I and III collagens and hyaluronan synthase 2 in TGFβ1-stimulated fibroblasts. Expression of COL1A2 mRNA in line Fib1 treated with 10 −10 M vitamin D hydroxy-derivatives (A); COL3A1 mRNA in line Fib1 treated with 10 −8 M vitamin D hydroxy-derivatives (B); and HAS2 in line Z4 treated with 10 −8 M vitamin D hydroxyderivatives (C) are shown. Results are expressed as mean ± SD, with P values of EtOH + TGF-β1 vs different treatments as indicated above connecting lines.

    Article Snippet: The confluent fibroblasts were preincubated in serum-free media for 24 hours, and vitamin D hydroxyderivatives (10−9 or 10−10 M) were added to 3 replicate wells 2 hours prior to addition of recombinant human TGF-β1 (R & D Systems, Minneapolis, Minnesota) to a final concentration of 5 ng/mL.

    Techniques: Expressing

    Vitamin D hydroxyderivatives inhibit total collagen and hyaluronan production stimulated by TGF-β1. Scleroderma human dermal fibroblast line 08 (A and B) or normal human dermal fibroblasts line 442 (C) were exposed to 20(OH)D 3 , 20,23(OH) 2 D 3 , or 1,25(OH) 2 D 3 and then treated with TGF-β1 as described. Total collagen (A and C) and hyaluronan (A) and collagen type 1 (B) were measured versus PBS + EtOH and TGF-β1 + EtOH controls, respectively. Data are presented as mean ± SEM of 3 replicates, and P values for statistically significant differences between control and treatments are shown above the bars. Results were confirmed using 2 additional normal human dermal fibroblast lines (data not shown).

    Journal: The Journal of Clinical Endocrinology and Metabolism

    Article Title: 20S-Hydroxyvitamin D3, Noncalcemic Product of CYP11A1 Action on Vitamin D3, Exhibits Potent Antifibrogenic Activity in Vivo

    doi: 10.1210/jc.2012-3074

    Figure Lengend Snippet: Vitamin D hydroxyderivatives inhibit total collagen and hyaluronan production stimulated by TGF-β1. Scleroderma human dermal fibroblast line 08 (A and B) or normal human dermal fibroblasts line 442 (C) were exposed to 20(OH)D 3 , 20,23(OH) 2 D 3 , or 1,25(OH) 2 D 3 and then treated with TGF-β1 as described. Total collagen (A and C) and hyaluronan (A) and collagen type 1 (B) were measured versus PBS + EtOH and TGF-β1 + EtOH controls, respectively. Data are presented as mean ± SEM of 3 replicates, and P values for statistically significant differences between control and treatments are shown above the bars. Results were confirmed using 2 additional normal human dermal fibroblast lines (data not shown).

    Article Snippet: The confluent fibroblasts were preincubated in serum-free media for 24 hours, and vitamin D hydroxyderivatives (10−9 or 10−10 M) were added to 3 replicate wells 2 hours prior to addition of recombinant human TGF-β1 (R & D Systems, Minneapolis, Minnesota) to a final concentration of 5 ng/mL.

    Techniques: