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Cell Signaling Technology Inc py419 src family kinase

Src phosphorylates free TAB1 not bound to TAK1. A , Crystal structure of the TAK1-TAB1 fusion protein (PDB id: 2EVA ). An enlarged version of the interaction interface shows Y125 and R225 of the TAK1 kinase domain forming a hydrogen bond ( yellow dashed line ) with TAB1-Y481. The distance between the backbone amide nitrogen atom of Y125 and the side chain oxygen atom of Y481 is 3.4 Å, while the distance between the guanidinium nitrogen atom (Nη1) of R225 and the side chain oxygen atom of Y481 is 3.1 Å. The figure was generated using PyMol (DeLano Scientific; www.pymol.org ). B , COS-7 cells were transfected with EGFP-TAB1-C or TAK1-TAB1 with Src. C , COS-7 cells were transfected with EGFP-TAB1, Flag-TAK1, and Src. Cell lysates or anti-GFP immunoprecipitates were immunoblotted with primary antibodies against pY481-TAB1, EGFP, pT187-TAK1, TAK1, and <t>pY419-Src.</t> D , the relative quantification of pY481-TAB1 in lysates, normalized to total TAB1, is presented as the mean ± SD of three independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗∗ p < 0.01.

Py419 Src Family Kinase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 2298 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/py419+src+family+kinase/pmc12925544-188-3-23?v=Cell+Signaling+Technology+Inc
Average 96 stars, based on 2298 article reviews

py419 src family kinase - by Bioz Stars, 2026-07

96/100 stars

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1) Product Images from "The stress-activated kinase p38 mediates non-canonical activation of Src and tyrosine phosphorylation of the adapter protein TAB1"

Article Title: The stress-activated kinase p38 mediates non-canonical activation of Src and tyrosine phosphorylation of the adapter protein TAB1

Journal: The Journal of Biological Chemistry

doi: 10.1016/j.jbc.2026.111200

Figure Legend Snippet: Src phosphorylates free TAB1 not bound to TAK1. A , Crystal structure of the TAK1-TAB1 fusion protein (PDB id: 2EVA ). An enlarged version of the interaction interface shows Y125 and R225 of the TAK1 kinase domain forming a hydrogen bond ( yellow dashed line ) with TAB1-Y481. The distance between the backbone amide nitrogen atom of Y125 and the side chain oxygen atom of Y481 is 3.4 Å, while the distance between the guanidinium nitrogen atom (Nη1) of R225 and the side chain oxygen atom of Y481 is 3.1 Å. The figure was generated using PyMol (DeLano Scientific; www.pymol.org ). B , COS-7 cells were transfected with EGFP-TAB1-C or TAK1-TAB1 with Src. C , COS-7 cells were transfected with EGFP-TAB1, Flag-TAK1, and Src. Cell lysates or anti-GFP immunoprecipitates were immunoblotted with primary antibodies against pY481-TAB1, EGFP, pT187-TAK1, TAK1, and pY419-Src. D , the relative quantification of pY481-TAB1 in lysates, normalized to total TAB1, is presented as the mean ± SD of three independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗∗ p < 0.01.

Techniques Used: Generated, Transfection, Quantitative Proteomics

p38 directly phosphorylates Src to increase its kinase activity. A , comparison between the substrate consensus sequence of p38α and the amino acid sequences of human Src around S75. Asterisks indicate amino acids that are common to both. B , an in vitro kinase assay using recombinant His-tagged Src and GST-tagged p38α proteins. Immunoblot analyses were performed with the primary antibodies indicated. C , the relative quantification of pS75-Src and pY419-Src, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by Welch’s two-tailed t test was applied. ∗∗ p < 0.01. D , COS-7 cells were transfected with Src and p38α (WT, CA or KD), and then treated with SB203580 for 5 h. Immunoblot analyses were performed with the primary antibodies indicated. E , the relative quantification of pS75-Src and pY419-Src, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗∗ p < 0.01. F , Src immunoprecipitated from transfected COS-7 cells was preincubated with recombinant p38 for 60 min. After removal of p38, the tyrosine kinase activity of Src toward GST-TAB1-C at Y481 was evaluated by an additional 20-min incubation. The relative quantification of pY481-TAB1, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by Welch’s two-tailed t test was applied. ∗ p < 0.05. G , COS-7 cells were transfected with EGFP-TAB1, Src (WT or S75A), and p38α. Immunoblot analyses were performed with the primary antibodies indicated. H , the relative quantification of pY481-TAB1, normalized to total TAB1, is presented as the mean ± SD of four independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗ p < 0.05.

Figure Legend Snippet: p38 directly phosphorylates Src to increase its kinase activity. A , comparison between the substrate consensus sequence of p38α and the amino acid sequences of human Src around S75. Asterisks indicate amino acids that are common to both. B , an in vitro kinase assay using recombinant His-tagged Src and GST-tagged p38α proteins. Immunoblot analyses were performed with the primary antibodies indicated. C , the relative quantification of pS75-Src and pY419-Src, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by Welch’s two-tailed t test was applied. ∗∗ p < 0.01. D , COS-7 cells were transfected with Src and p38α (WT, CA or KD), and then treated with SB203580 for 5 h. Immunoblot analyses were performed with the primary antibodies indicated. E , the relative quantification of pS75-Src and pY419-Src, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗∗ p < 0.01. F , Src immunoprecipitated from transfected COS-7 cells was preincubated with recombinant p38 for 60 min. After removal of p38, the tyrosine kinase activity of Src toward GST-TAB1-C at Y481 was evaluated by an additional 20-min incubation. The relative quantification of pY481-TAB1, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by Welch’s two-tailed t test was applied. ∗ p < 0.05. G , COS-7 cells were transfected with EGFP-TAB1, Src (WT or S75A), and p38α. Immunoblot analyses were performed with the primary antibodies indicated. H , the relative quantification of pY481-TAB1, normalized to total TAB1, is presented as the mean ± SD of four independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗ p < 0.05.

Techniques Used: Activity Assay, Comparison, Sequencing, In Vitro, Kinase Assay, Recombinant, Western Blot, Quantitative Proteomics, Two Tailed Test, Transfection, Immunoprecipitation, Incubation

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Journal: The Journal of Biological Chemistry

Article Title: The stress-activated kinase p38 mediates non-canonical activation of Src and tyrosine phosphorylation of the adapter protein TAB1

doi: 10.1016/j.jbc.2026.111200

Figure Lengend Snippet: Src phosphorylates free TAB1 not bound to TAK1. A , Crystal structure of the TAK1-TAB1 fusion protein (PDB id: 2EVA ). An enlarged version of the interaction interface shows Y125 and R225 of the TAK1 kinase domain forming a hydrogen bond ( yellow dashed line ) with TAB1-Y481. The distance between the backbone amide nitrogen atom of Y125 and the side chain oxygen atom of Y481 is 3.4 Å, while the distance between the guanidinium nitrogen atom (Nη1) of R225 and the side chain oxygen atom of Y481 is 3.1 Å. The figure was generated using PyMol (DeLano Scientific; www.pymol.org ). B , COS-7 cells were transfected with EGFP-TAB1-C or TAK1-TAB1 with Src. C , COS-7 cells were transfected with EGFP-TAB1, Flag-TAK1, and Src. Cell lysates or anti-GFP immunoprecipitates were immunoblotted with primary antibodies against pY481-TAB1, EGFP, pT187-TAK1, TAK1, and pY419-Src. D , the relative quantification of pY481-TAB1 in lysates, normalized to total TAB1, is presented as the mean ± SD of three independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗∗ p < 0.01.

Article Snippet: Primary antibodies for pY419-Src family kinase (2101S), total-Src (2110S), pT180/pY182-p38 (4511S), pY701-STAT1 (sc-136229), total-STAT1 (sc-346), pY576/577-FAK (3281S), and total-FAK (3285S) were purchased from Cell Signaling Technology. pS75-Src (ab79308) was from Abcam.

Techniques: Generated, Transfection, Quantitative Proteomics

Journal: The Journal of Biological Chemistry

Article Title: The stress-activated kinase p38 mediates non-canonical activation of Src and tyrosine phosphorylation of the adapter protein TAB1

doi: 10.1016/j.jbc.2026.111200

Figure Lengend Snippet: p38 directly phosphorylates Src to increase its kinase activity. A , comparison between the substrate consensus sequence of p38α and the amino acid sequences of human Src around S75. Asterisks indicate amino acids that are common to both. B , an in vitro kinase assay using recombinant His-tagged Src and GST-tagged p38α proteins. Immunoblot analyses were performed with the primary antibodies indicated. C , the relative quantification of pS75-Src and pY419-Src, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by Welch’s two-tailed t test was applied. ∗∗ p < 0.01. D , COS-7 cells were transfected with Src and p38α (WT, CA or KD), and then treated with SB203580 for 5 h. Immunoblot analyses were performed with the primary antibodies indicated. E , the relative quantification of pS75-Src and pY419-Src, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗∗ p < 0.01. F , Src immunoprecipitated from transfected COS-7 cells was preincubated with recombinant p38 for 60 min. After removal of p38, the tyrosine kinase activity of Src toward GST-TAB1-C at Y481 was evaluated by an additional 20-min incubation. The relative quantification of pY481-TAB1, normalized to total Src, is presented as the mean ± SD of three independent experiments. p values were calculated by Welch’s two-tailed t test was applied. ∗ p < 0.05. G , COS-7 cells were transfected with EGFP-TAB1, Src (WT or S75A), and p38α. Immunoblot analyses were performed with the primary antibodies indicated. H , the relative quantification of pY481-TAB1, normalized to total TAB1, is presented as the mean ± SD of four independent experiments. p values were calculated by one-way ANOVA followed by either Tukey’s HSD test was applied. ∗ p < 0.05.

Techniques: Activity Assay, Comparison, Sequencing, In Vitro, Kinase Assay, Recombinant, Western Blot, Quantitative Proteomics, Two Tailed Test, Transfection, Immunoprecipitation, Incubation

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