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recombinant human tgf β receptor ii fc  (R&D Systems)
90
R&D Systems recombinant human tgf β receptor ii fc
Recombinant Human Tgf β Receptor Ii Fc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rhtgfβsrii  (R&D Systems)
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R&D Systems rhtgfβsrii
Rhtgfβsrii, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant human tgf receptor ii fc  (R&D Systems)
90
R&D Systems recombinant human tgf receptor ii fc
FIGURE 6. Amino acids in the CC loop region of the N-terminal domain of PSG1 are essential for induction of <t>TGF-1</t> from RAW264.7 macrophages. A, <t>recombinant</t> proteins used for these studies were separated on a 4–20% NuPAGE gel and stained with GelCode Blue. Lane 1, PSG1-A2-B2-Fc; lane 2, PSG1-N-Fc; lane 3, PSG1-N-CC-Fc; lane 4, PSG1-N-CC -Fc; lane 5, PSG1-N-YHY-Fc; lane 6, PSG1-N-LYHY-Fc. B, TGF-1 secretion following incubation of RAW264.7 murine macrophages with 3 g/ml control Fc protein (cntrl-Fc), PSG1-A2-Fc, and PSG1-N-Fc or 6 g/ml PSG1-A2-B2-Fc to achieve concentrations equimolar to the single-domain proteins. C, sequence alignment of the CC and CC loop regions of CEACAM5, PSG1, and PSG1 N-terminal domain mutants. Residues con- served in CEACAM5 and PSG1 are highlighted in gray. The C, C, and C -strands are indicated with green arrows above the corresponding sequence. Residues in the PSG1 N-terminal domain mutated to the residues corresponding to the same position in CEACAM5 are colored red. D, TGF-1 secretion of RAW264.7 macrophages following incubation with increasing concentrations of PSG1-N-CC-Fc, PSG1-N-CC -Fc, or control Fc protein. E, RAW264.7 macrophages were incubated with 12 g/ml wild-type PSG1 N-terminal domain (WT), PSG1-N-Y42N/H43R/Y44Q mutant (YHY3NRQ), PSG1-N-L41G/Y42N/H43R/Y44Q mutant (LYHY3GNRQ), or control Fc protein. For B–E, TGF-1 following acid activation was measured in the supernatants by ELISA as described under “Experimental Procedures.” *, p 0.05 by Student’s t test; ns, not significant. F, ribbon representation of the structural model of the PSG1 N-terminal domain. -Sheets are showningreenandlabeledwithuppercasewhiteletters.The-helixbetweenstrandsEandFisshowninorange,andloopsareshowningray.Residues 41LYHY44 of the CC loop are labeled and highlighted in red, and their side chains are shown in stick representation. The CC and CC loops and the N and C termini of the protein domain are indicated.
Recombinant Human Tgf Receptor Ii Fc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/recombinant human tgf receptor ii fc/product/R&D Systems
Average 90 stars, based on 1 article reviews
recombinant human tgf receptor ii fc - by Bioz Stars, 2026-05
90/100 stars
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human tgf β receptor ii fc  (R&D Systems)
90
R&D Systems human tgf β receptor ii fc
FIGURE 6. Amino acids in the CC loop region of the N-terminal domain of PSG1 are essential for induction of <t>TGF-1</t> from RAW264.7 macrophages. A, <t>recombinant</t> proteins used for these studies were separated on a 4–20% NuPAGE gel and stained with GelCode Blue. Lane 1, PSG1-A2-B2-Fc; lane 2, PSG1-N-Fc; lane 3, PSG1-N-CC-Fc; lane 4, PSG1-N-CC -Fc; lane 5, PSG1-N-YHY-Fc; lane 6, PSG1-N-LYHY-Fc. B, TGF-1 secretion following incubation of RAW264.7 murine macrophages with 3 g/ml control Fc protein (cntrl-Fc), PSG1-A2-Fc, and PSG1-N-Fc or 6 g/ml PSG1-A2-B2-Fc to achieve concentrations equimolar to the single-domain proteins. C, sequence alignment of the CC and CC loop regions of CEACAM5, PSG1, and PSG1 N-terminal domain mutants. Residues con- served in CEACAM5 and PSG1 are highlighted in gray. The C, C, and C -strands are indicated with green arrows above the corresponding sequence. Residues in the PSG1 N-terminal domain mutated to the residues corresponding to the same position in CEACAM5 are colored red. D, TGF-1 secretion of RAW264.7 macrophages following incubation with increasing concentrations of PSG1-N-CC-Fc, PSG1-N-CC -Fc, or control Fc protein. E, RAW264.7 macrophages were incubated with 12 g/ml wild-type PSG1 N-terminal domain (WT), PSG1-N-Y42N/H43R/Y44Q mutant (YHY3NRQ), PSG1-N-L41G/Y42N/H43R/Y44Q mutant (LYHY3GNRQ), or control Fc protein. For B–E, TGF-1 following acid activation was measured in the supernatants by ELISA as described under “Experimental Procedures.” *, p 0.05 by Student’s t test; ns, not significant. F, ribbon representation of the structural model of the PSG1 N-terminal domain. -Sheets are showningreenandlabeledwithuppercasewhiteletters.The-helixbetweenstrandsEandFisshowninorange,andloopsareshowningray.Residues 41LYHY44 of the CC loop are labeled and highlighted in red, and their side chains are shown in stick representation. The CC and CC loops and the N and C termini of the protein domain are indicated.
Human Tgf β Receptor Ii Fc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/human tgf β receptor ii fc/product/R&D Systems
Average 90 stars, based on 1 article reviews
human tgf β receptor ii fc - by Bioz Stars, 2026-05
90/100 stars
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FIGURE 6. Amino acids in the CC loop region of the N-terminal domain of PSG1 are essential for induction of TGF-1 from RAW264.7 macrophages. A, recombinant proteins used for these studies were separated on a 4–20% NuPAGE gel and stained with GelCode Blue. Lane 1, PSG1-A2-B2-Fc; lane 2, PSG1-N-Fc; lane 3, PSG1-N-CC-Fc; lane 4, PSG1-N-CC -Fc; lane 5, PSG1-N-YHY-Fc; lane 6, PSG1-N-LYHY-Fc. B, TGF-1 secretion following incubation of RAW264.7 murine macrophages with 3 g/ml control Fc protein (cntrl-Fc), PSG1-A2-Fc, and PSG1-N-Fc or 6 g/ml PSG1-A2-B2-Fc to achieve concentrations equimolar to the single-domain proteins. C, sequence alignment of the CC and CC loop regions of CEACAM5, PSG1, and PSG1 N-terminal domain mutants. Residues con- served in CEACAM5 and PSG1 are highlighted in gray. The C, C, and C -strands are indicated with green arrows above the corresponding sequence. Residues in the PSG1 N-terminal domain mutated to the residues corresponding to the same position in CEACAM5 are colored red. D, TGF-1 secretion of RAW264.7 macrophages following incubation with increasing concentrations of PSG1-N-CC-Fc, PSG1-N-CC -Fc, or control Fc protein. E, RAW264.7 macrophages were incubated with 12 g/ml wild-type PSG1 N-terminal domain (WT), PSG1-N-Y42N/H43R/Y44Q mutant (YHY3NRQ), PSG1-N-L41G/Y42N/H43R/Y44Q mutant (LYHY3GNRQ), or control Fc protein. For B–E, TGF-1 following acid activation was measured in the supernatants by ELISA as described under “Experimental Procedures.” *, p 0.05 by Student’s t test; ns, not significant. F, ribbon representation of the structural model of the PSG1 N-terminal domain. -Sheets are showningreenandlabeledwithuppercasewhiteletters.The-helixbetweenstrandsEandFisshowninorange,andloopsareshowningray.Residues 41LYHY44 of the CC loop are labeled and highlighted in red, and their side chains are shown in stick representation. The CC and CC loops and the N and C termini of the protein domain are indicated.

Journal: Journal of Biological Chemistry

Article Title: Induction and Activation of Latent Transforming Growth Factor-β1 Are Carried out by Two Distinct Domains of Pregnancy-specific Glycoprotein 1 (PSG1)

doi: 10.1074/jbc.m114.597518

Figure Lengend Snippet: FIGURE 6. Amino acids in the CC loop region of the N-terminal domain of PSG1 are essential for induction of TGF-1 from RAW264.7 macrophages. A, recombinant proteins used for these studies were separated on a 4–20% NuPAGE gel and stained with GelCode Blue. Lane 1, PSG1-A2-B2-Fc; lane 2, PSG1-N-Fc; lane 3, PSG1-N-CC-Fc; lane 4, PSG1-N-CC -Fc; lane 5, PSG1-N-YHY-Fc; lane 6, PSG1-N-LYHY-Fc. B, TGF-1 secretion following incubation of RAW264.7 murine macrophages with 3 g/ml control Fc protein (cntrl-Fc), PSG1-A2-Fc, and PSG1-N-Fc or 6 g/ml PSG1-A2-B2-Fc to achieve concentrations equimolar to the single-domain proteins. C, sequence alignment of the CC and CC loop regions of CEACAM5, PSG1, and PSG1 N-terminal domain mutants. Residues con- served in CEACAM5 and PSG1 are highlighted in gray. The C, C, and C -strands are indicated with green arrows above the corresponding sequence. Residues in the PSG1 N-terminal domain mutated to the residues corresponding to the same position in CEACAM5 are colored red. D, TGF-1 secretion of RAW264.7 macrophages following incubation with increasing concentrations of PSG1-N-CC-Fc, PSG1-N-CC -Fc, or control Fc protein. E, RAW264.7 macrophages were incubated with 12 g/ml wild-type PSG1 N-terminal domain (WT), PSG1-N-Y42N/H43R/Y44Q mutant (YHY3NRQ), PSG1-N-L41G/Y42N/H43R/Y44Q mutant (LYHY3GNRQ), or control Fc protein. For B–E, TGF-1 following acid activation was measured in the supernatants by ELISA as described under “Experimental Procedures.” *, p 0.05 by Student’s t test; ns, not significant. F, ribbon representation of the structural model of the PSG1 N-terminal domain. -Sheets are showningreenandlabeledwithuppercasewhiteletters.The-helixbetweenstrandsEandFisshowninorange,andloopsareshowningray.Residues 41LYHY44 of the CC loop are labeled and highlighted in red, and their side chains are shown in stick representation. The CC and CC loops and the N and C termini of the protein domain are indicated.

Article Snippet: The samples were transferred to a 96-well Nunc MaxiSorp plate that had been blocked with 0.5% BSA following an overnight coating step with either recombinant human TGF- receptor II-Fc or antiTGF- 1 antibody (R&D Systems).

Techniques: Recombinant, Staining, Incubation, Control, Sequencing, Mutagenesis, Activation Assay, Enzyme-linked Immunosorbent Assay, Labeling