tgf β1 receptor Search Results


tgf-β1 receptor kinase inhibitor (tki), ly-2157299  (Eli Lilly)
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Eli Lilly tgf-β1 receptor kinase inhibitor (tki), ly-2157299
Tgf β1 Receptor Kinase Inhibitor (Tki), Ly 2157299, supplied by Eli Lilly, 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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genomic instability in the type ii tgf-β1 receptor gene  (Weksler)
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Weksler genomic instability in the type ii tgf-β1 receptor gene
Genomic Instability In The Type Ii Tgf β1 Receptor Gene, supplied by Weksler, 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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affinity labeling cell surface tgf-β receptors with [ 125 i]-tgf-β1  (NEN Life Science)
90
NEN Life Science affinity labeling cell surface tgf-β receptors with [ 125 i]-tgf-β1
(A–C) Effects of TRAF2 and TRAF6 mutants on the activation of exogenous FLAG-p38, <t>HA-JNK</t> or FLAG-Smad2 by the constitutively active TβRI(TD) in R1BL17 cells. The levels of phosphorylated and total p38 were analyzed by Western blot analyses (A), and the activity of immunoprecipitated HA-JNK was determined in an in vitro kinase reaction using GST-c-Jun as the substrate (B). Only the TRAF6 mutant inhibited the activation of both p38 and JNK. Neither TRAF2 nor TRAF6 affected Smad2 phosphorylation (C). (D) Effect of the TRAF6 RNAi on the activation of endogenous JNK and p38 <t>by</t> <t>TGF-β.</t> AML12 cells were treated with TGF-β as indicated two days after siRNA transfection. The levels of phospho- or total JNK and p38 in cell lysates were analyzed by Western blots. (E) Rescuing JNK and p38 activation in TRAF6-siRNA transfected AML12 cells with wild type human TRAF6 cDNA. TGF-β treatment was for 30 minutes. (F) Western analyses showing absent JNK activation but unabated Smad2 activation by TGF-β in TRAF6-deficient MEFs. (G) Restoration of the TGF-β-induced JNK activation in TRAF6-deficient MEFs with wild type TRAF6 but not the RING domain mutant TRAF6(C70A).
Affinity Labeling Cell Surface Tgf β Receptors With [ 125 I] Tgf β1, supplied by NEN Life Science, 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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affinity labeling cell surface tgf-β receptors with [ 125 i]-tgf-β1 - by Bioz Stars, 2026-02
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tgf-β1 receptor inhibitor ly364947  (Aladdin Co Ltd)
90
Aladdin Co Ltd tgf-β1 receptor inhibitor ly364947
(A–C) Effects of TRAF2 and TRAF6 mutants on the activation of exogenous FLAG-p38, <t>HA-JNK</t> or FLAG-Smad2 by the constitutively active TβRI(TD) in R1BL17 cells. The levels of phosphorylated and total p38 were analyzed by Western blot analyses (A), and the activity of immunoprecipitated HA-JNK was determined in an in vitro kinase reaction using GST-c-Jun as the substrate (B). Only the TRAF6 mutant inhibited the activation of both p38 and JNK. Neither TRAF2 nor TRAF6 affected Smad2 phosphorylation (C). (D) Effect of the TRAF6 RNAi on the activation of endogenous JNK and p38 <t>by</t> <t>TGF-β.</t> AML12 cells were treated with TGF-β as indicated two days after siRNA transfection. The levels of phospho- or total JNK and p38 in cell lysates were analyzed by Western blots. (E) Rescuing JNK and p38 activation in TRAF6-siRNA transfected AML12 cells with wild type human TRAF6 cDNA. TGF-β treatment was for 30 minutes. (F) Western analyses showing absent JNK activation but unabated Smad2 activation by TGF-β in TRAF6-deficient MEFs. (G) Restoration of the TGF-β-induced JNK activation in TRAF6-deficient MEFs with wild type TRAF6 but not the RING domain mutant TRAF6(C70A).
Tgf β1 Receptor Inhibitor Ly364947, supplied by Aladdin Co Ltd, 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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oligonucleotide primers gm-csf, csf-1, tnf-α, tgf-β1, ifn-γ, il-2, lif lif-receptor  (CRUACHEM LIMITED)
90
CRUACHEM LIMITED oligonucleotide primers gm-csf, csf-1, tnf-α, tgf-β1, ifn-γ, il-2, lif lif-receptor
(A–C) Effects of TRAF2 and TRAF6 mutants on the activation of exogenous FLAG-p38, <t>HA-JNK</t> or FLAG-Smad2 by the constitutively active TβRI(TD) in R1BL17 cells. The levels of phosphorylated and total p38 were analyzed by Western blot analyses (A), and the activity of immunoprecipitated HA-JNK was determined in an in vitro kinase reaction using GST-c-Jun as the substrate (B). Only the TRAF6 mutant inhibited the activation of both p38 and JNK. Neither TRAF2 nor TRAF6 affected Smad2 phosphorylation (C). (D) Effect of the TRAF6 RNAi on the activation of endogenous JNK and p38 <t>by</t> <t>TGF-β.</t> AML12 cells were treated with TGF-β as indicated two days after siRNA transfection. The levels of phospho- or total JNK and p38 in cell lysates were analyzed by Western blots. (E) Rescuing JNK and p38 activation in TRAF6-siRNA transfected AML12 cells with wild type human TRAF6 cDNA. TGF-β treatment was for 30 minutes. (F) Western analyses showing absent JNK activation but unabated Smad2 activation by TGF-β in TRAF6-deficient MEFs. (G) Restoration of the TGF-β-induced JNK activation in TRAF6-deficient MEFs with wild type TRAF6 but not the RING domain mutant TRAF6(C70A).
Oligonucleotide Primers Gm Csf, Csf 1, Tnf α, Tgf β1, Ifn γ, Il 2, Lif Lif Receptor, supplied by CRUACHEM LIMITED, 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/oligonucleotide primers gm-csf, csf-1, tnf-α, tgf-β1, ifn-γ, il-2, lif lif-receptor/product/CRUACHEM LIMITED
Average 90 stars, based on 1 article reviews
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sb431542  (Macklin Inc)
90
Macklin Inc sb431542
(A–C) Effects of TRAF2 and TRAF6 mutants on the activation of exogenous FLAG-p38, <t>HA-JNK</t> or FLAG-Smad2 by the constitutively active TβRI(TD) in R1BL17 cells. The levels of phosphorylated and total p38 were analyzed by Western blot analyses (A), and the activity of immunoprecipitated HA-JNK was determined in an in vitro kinase reaction using GST-c-Jun as the substrate (B). Only the TRAF6 mutant inhibited the activation of both p38 and JNK. Neither TRAF2 nor TRAF6 affected Smad2 phosphorylation (C). (D) Effect of the TRAF6 RNAi on the activation of endogenous JNK and p38 <t>by</t> <t>TGF-β.</t> AML12 cells were treated with TGF-β as indicated two days after siRNA transfection. The levels of phospho- or total JNK and p38 in cell lysates were analyzed by Western blots. (E) Rescuing JNK and p38 activation in TRAF6-siRNA transfected AML12 cells with wild type human TRAF6 cDNA. TGF-β treatment was for 30 minutes. (F) Western analyses showing absent JNK activation but unabated Smad2 activation by TGF-β in TRAF6-deficient MEFs. (G) Restoration of the TGF-β-induced JNK activation in TRAF6-deficient MEFs with wild type TRAF6 but not the RING domain mutant TRAF6(C70A).
Sb431542, supplied by Macklin Inc, 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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Average 90 stars, based on 1 article reviews
sb431542 - by Bioz Stars, 2026-02
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Image Search Results


(A–C) Effects of TRAF2 and TRAF6 mutants on the activation of exogenous FLAG-p38, HA-JNK or FLAG-Smad2 by the constitutively active TβRI(TD) in R1BL17 cells. The levels of phosphorylated and total p38 were analyzed by Western blot analyses (A), and the activity of immunoprecipitated HA-JNK was determined in an in vitro kinase reaction using GST-c-Jun as the substrate (B). Only the TRAF6 mutant inhibited the activation of both p38 and JNK. Neither TRAF2 nor TRAF6 affected Smad2 phosphorylation (C). (D) Effect of the TRAF6 RNAi on the activation of endogenous JNK and p38 by TGF-β. AML12 cells were treated with TGF-β as indicated two days after siRNA transfection. The levels of phospho- or total JNK and p38 in cell lysates were analyzed by Western blots. (E) Rescuing JNK and p38 activation in TRAF6-siRNA transfected AML12 cells with wild type human TRAF6 cDNA. TGF-β treatment was for 30 minutes. (F) Western analyses showing absent JNK activation but unabated Smad2 activation by TGF-β in TRAF6-deficient MEFs. (G) Restoration of the TGF-β-induced JNK activation in TRAF6-deficient MEFs with wild type TRAF6 but not the RING domain mutant TRAF6(C70A).

Journal:

Article Title: TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-?

doi: 10.1016/j.molcel.2008.09.002

Figure Lengend Snippet: (A–C) Effects of TRAF2 and TRAF6 mutants on the activation of exogenous FLAG-p38, HA-JNK or FLAG-Smad2 by the constitutively active TβRI(TD) in R1BL17 cells. The levels of phosphorylated and total p38 were analyzed by Western blot analyses (A), and the activity of immunoprecipitated HA-JNK was determined in an in vitro kinase reaction using GST-c-Jun as the substrate (B). Only the TRAF6 mutant inhibited the activation of both p38 and JNK. Neither TRAF2 nor TRAF6 affected Smad2 phosphorylation (C). (D) Effect of the TRAF6 RNAi on the activation of endogenous JNK and p38 by TGF-β. AML12 cells were treated with TGF-β as indicated two days after siRNA transfection. The levels of phospho- or total JNK and p38 in cell lysates were analyzed by Western blots. (E) Rescuing JNK and p38 activation in TRAF6-siRNA transfected AML12 cells with wild type human TRAF6 cDNA. TGF-β treatment was for 30 minutes. (F) Western analyses showing absent JNK activation but unabated Smad2 activation by TGF-β in TRAF6-deficient MEFs. (G) Restoration of the TGF-β-induced JNK activation in TRAF6-deficient MEFs with wild type TRAF6 but not the RING domain mutant TRAF6(C70A).

Article Snippet: The JNK kinase assay, affinity labeling cell surface TGF-β receptors with [ 125 I]-TGF-β1(NEN), regular and sequential immunoprecipitation experiments were described previously ( Chen and Derynck, 1994 ; Yu et al., 2002 ).

Techniques: Activation Assay, Western Blot, Activity Assay, Immunoprecipitation, In Vitro, Mutagenesis, Phospho-proteomics, Transfection