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Proteintech sos1 rabbit pab

Figure 4. ECM1 recruits GRB2 and <t>SOS1</t> to the membrane to activate the MAPK signaling pathway. A) Aﬃnity puriﬁcation MS analysis of ECM1 interaction complexes in C4-2B cells (left). Representative mass spectra of GRB2 and SOS1 peptides (right). B) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells with ECM1 (200 ng mL−1) treatment. C) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with Veh (PBS) or ECM1 (200 ng mL−1). Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D,E) WB analysis of GRB2 and <t>SOS1</t> <t>protein</t> expression in whole lysis (WL) and membrane proteins from C4-2B cells treated with increasing concentrations of ECM1 (0, 200, 400, 800 ng mL−1), or with the addition of either DMEM or CM. GAPDH was used as a loading control for whole lysis, and PMCA1 for membrane proteins. F) IP detection of the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells treated with CM. G) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with DMEM or CM. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). H,I) WB analysis of MEK, p-MEK, ERK1/2, and p-ERK1/2 expression in the indicated C4-2B cells treated with or without ECM1 (200 ng mL−1). ns, not signiﬁcant; *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Sos1 Rabbit Pab, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sos1+rabbit+pab/SOS1+Antibody/pm39563492-370-34-37
Average 93 stars, based on 15 article reviews

sos1 rabbit pab - by Bioz Stars, 2026-10

93/100 stars

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1) Product Images from "Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer."

Article Title: Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

doi: 10.1002/advs.202407662

Figure 4. ECM1 recruits GRB2 and SOS1 to the membrane to activate the MAPK signaling pathway. A) Aﬃnity puriﬁcation MS analysis of ECM1 interaction complexes in C4-2B cells (left). Representative mass spectra of GRB2 and SOS1 peptides (right). B) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells with ECM1 (200 ng mL−1) treatment. C) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with Veh (PBS) or ECM1 (200 ng mL−1). Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D,E) WB analysis of GRB2 and SOS1 protein expression in whole lysis (WL) and membrane proteins from C4-2B cells treated with increasing concentrations of ECM1 (0, 200, 400, 800 ng mL−1), or with the addition of either DMEM or CM. GAPDH was used as a loading control for whole lysis, and PMCA1 for membrane proteins. F) IP detection of the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells treated with CM. G) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with DMEM or CM. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). H,I) WB analysis of MEK, p-MEK, ERK1/2, and p-ERK1/2 expression in the indicated C4-2B cells treated with or without ECM1 (200 ng mL−1). ns, not signiﬁcant; *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Figure Legend Snippet: Figure 4. ECM1 recruits GRB2 and SOS1 to the membrane to activate the MAPK signaling pathway. A) Aﬃnity puriﬁcation MS analysis of ECM1 interaction complexes in C4-2B cells (left). Representative mass spectra of GRB2 and SOS1 peptides (right). B) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells with ECM1 (200 ng mL−1) treatment. C) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with Veh (PBS) or ECM1 (200 ng mL−1). Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D,E) WB analysis of GRB2 and SOS1 protein expression in whole lysis (WL) and membrane proteins from C4-2B cells treated with increasing concentrations of ECM1 (0, 200, 400, 800 ng mL−1), or with the addition of either DMEM or CM. GAPDH was used as a loading control for whole lysis, and PMCA1 for membrane proteins. F) IP detection of the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells treated with CM. G) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with DMEM or CM. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). H,I) WB analysis of MEK, p-MEK, ERK1/2, and p-ERK1/2 expression in the indicated C4-2B cells treated with or without ECM1 (200 ng mL−1). ns, not signiﬁcant; *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Techniques Used: Membrane, Staining, Expressing, Lysis, Control

Figure 5. Phosphorylated ENO1 bridges ECM1 with GRB2 and SOS1 at the membrane. A) Representative mass spectra of ENO1 peptide. B) IP analysis detected the interaction between ECM1 and ENO1 in C4-2B cells. C) IF staining and quantiﬁcation of ENO1 and ECM1 in C4-2B cells. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D) Proximity ligation assay (PLA) analysis of the interaction between ECM1-Flag and ENO1 (Scale bar, 10 μm). E) IP assays of the interaction between ENO1 and GRB2 as well as SOS1 in C4-2B cells in the presence or absence of ECM1 (200 ng mL−1). F) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in the indicated C4-2B cells

Figure Legend Snippet: Figure 5. Phosphorylated ENO1 bridges ECM1 with GRB2 and SOS1 at the membrane. A) Representative mass spectra of ENO1 peptide. B) IP analysis detected the interaction between ECM1 and ENO1 in C4-2B cells. C) IF staining and quantiﬁcation of ENO1 and ECM1 in C4-2B cells. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D) Proximity ligation assay (PLA) analysis of the interaction between ECM1-Flag and ENO1 (Scale bar, 10 μm). E) IP assays of the interaction between ENO1 and GRB2 as well as SOS1 in C4-2B cells in the presence or absence of ECM1 (200 ng mL−1). F) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in the indicated C4-2B cells

Techniques Used: Membrane, Staining, Proximity Ligation Assay

Figure 7. PhAH attenuates ENO1-mediated PCa cell resistance to ENZ. A) Chemical structure of PhAH. B) Ligand interaction diagram (left) and binding amino acid residue sites (right) of the highest-scoring PhAH and ENO1 protein molecular docking complex (RMSD = 1.9977; E_score = −3.9538). C) WB detection of the interaction between ECM1 and ENO1, as well as Tyr phosphorylation of ENO1 following immunoprecipitating ENO1 in C4-2B cells in the presence of ECM1 (200 ng mL−1) with or without PhAH (1 μM). D) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells

Figure Legend Snippet: Figure 7. PhAH attenuates ENO1-mediated PCa cell resistance to ENZ. A) Chemical structure of PhAH. B) Ligand interaction diagram (left) and binding amino acid residue sites (right) of the highest-scoring PhAH and ENO1 protein molecular docking complex (RMSD = 1.9977; E_score = −3.9538). C) WB detection of the interaction between ECM1 and ENO1, as well as Tyr phosphorylation of ENO1 following immunoprecipitating ENO1 in C4-2B cells in the presence of ECM1 (200 ng mL−1) with or without PhAH (1 μM). D) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells

Techniques Used: Binding Assay, Residue, Phospho-proteomics, Staining

Figure 9. Schematic diagram illustrating that increased osteoblast-derived ECM1 from the bone microenvironment of BMPC patients induced by ENZ treatment, interacts with the ENO1 receptor on the prostate cancer cell membrane, further recruiting adapter proteins including GRB2 and SOS1, which activates the downstream MAPK signaling pathway to promote the proliferation of PCa cells and induce anti-androgen resistance.

Figure Legend Snippet: Figure 9. Schematic diagram illustrating that increased osteoblast-derived ECM1 from the bone microenvironment of BMPC patients induced by ENZ treatment, interacts with the ENO1 receptor on the prostate cancer cell membrane, further recruiting adapter proteins including GRB2 and SOS1, which activates the downstream MAPK signaling pathway to promote the proliferation of PCa cells and induce anti-androgen resistance.

Techniques Used: Derivative Assay, Membrane

Incubation:

Article Title: Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.
Article Snippet: .. Subsequently, cells were respectively incubated overnight at 4 °C with primary antibodies including ECM1 Rabbit pAb (Proteintech; 11521-1-AP, 1:250), ENO1 Mouse mAb (Thermo Fisher Scientific; MA5-47393, 1:2000), GRB2 Rabbit pAb (Proteintech; 10254-2-AP, 1:50) or SOS1 Rabbit pAb (Proteintech; 55041-1-AP, 1:100). .. The next day, Alexa Fluor 488 conjugate goat anti-mouse IgG (H+L) (Cell Signaling Technology; #4408, 1:500) or Alexa Fluor 555 conjugate goat anti-rabbit IgG (H+L) (Cell Signaling Technology; #4413, 1;500) was used as the secondary antibody and incubated with cells at room temperature for 1 h. Specifically, the cell membrane was stained with the red fluorescent probe DiI (Beyotime; C1036).

Article Title: Osteoblast‐Derived ECM1 Promotes Anti‐Androgen Resistance in Bone Metastatic Prostate Cancer
Article Snippet: .. Subsequently, cells were respectively incubated overnight at 4 °C with primary antibodies including ECM1 Rabbit pAb (Proteintech; 11521‐1‐AP, 1:250), ENO1 Mouse mAb (Thermo Fisher Scientific; MA5‐47393, 1:2000), GRB2 Rabbit pAb (Proteintech; 10254‐2‐AP, 1:50) or SOS1 Rabbit pAb (Proteintech; 55041‐1‐AP, 1:100). .. The next day, Alexa Fluor 488 conjugate goat anti‐mouse IgG (H+L) (Cell Signaling Technology; #4408, 1:500) or Alexa Fluor 555 conjugate goat anti‐rabbit IgG (H+L) (Cell Signaling Technology; #4413, 1;500) was used as the secondary antibody and incubated with cells at room temperature for 1 h. Specifically, the cell membrane was stained with the red fluorescent probe DiI (Beyotime; C1036).

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Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.

doi: 10.1002/advs.202407662

Figure Lengend Snippet: Figure 4. ECM1 recruits GRB2 and SOS1 to the membrane to activate the MAPK signaling pathway. A) Aﬃnity puriﬁcation MS analysis of ECM1 interaction complexes in C4-2B cells (left). Representative mass spectra of GRB2 and SOS1 peptides (right). B) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells with ECM1 (200 ng mL−1) treatment. C) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with Veh (PBS) or ECM1 (200 ng mL−1). Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D,E) WB analysis of GRB2 and SOS1 protein expression in whole lysis (WL) and membrane proteins from C4-2B cells treated with increasing concentrations of ECM1 (0, 200, 400, 800 ng mL−1), or with the addition of either DMEM or CM. GAPDH was used as a loading control for whole lysis, and PMCA1 for membrane proteins. F) IP detection of the interaction between ECM1 and GRB2 as well as SOS1 in C4-2B cells treated with CM. G) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells treated with DMEM or CM. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). H,I) WB analysis of MEK, p-MEK, ERK1/2, and p-ERK1/2 expression in the indicated C4-2B cells treated with or without ECM1 (200 ng mL−1). ns, not signiﬁcant; *, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001.

Article Snippet: Subsequently, cells were respectively incubated overnight at 4 °C with primary antibodies including ECM1 Rabbit pAb (Proteintech; 11521-1-AP, 1:250), ENO1 Mouse mAb (Thermo Fisher Scientific; MA5-47393, 1:2000), GRB2 Rabbit pAb (Proteintech; 10254-2-AP, 1:50) or SOS1 Rabbit pAb (Proteintech; 55041-1-AP, 1:100).

Techniques: Membrane, Staining, Expressing, Lysis, Control

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.

doi: 10.1002/advs.202407662

Figure Lengend Snippet: Figure 5. Phosphorylated ENO1 bridges ECM1 with GRB2 and SOS1 at the membrane. A) Representative mass spectra of ENO1 peptide. B) IP analysis detected the interaction between ECM1 and ENO1 in C4-2B cells. C) IF staining and quantiﬁcation of ENO1 and ECM1 in C4-2B cells. Pearson R value greater than 0.5 indicated co-localization of the two proteins (Scale bar, 5 μm). D) Proximity ligation assay (PLA) analysis of the interaction between ECM1-Flag and ENO1 (Scale bar, 10 μm). E) IP assays of the interaction between ENO1 and GRB2 as well as SOS1 in C4-2B cells in the presence or absence of ECM1 (200 ng mL−1). F) IP analysis detected the interaction between ECM1 and GRB2 as well as SOS1 in the indicated C4-2B cells

Techniques: Membrane, Staining, Proximity Ligation Assay

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.

doi: 10.1002/advs.202407662

Figure Lengend Snippet: Figure 7. PhAH attenuates ENO1-mediated PCa cell resistance to ENZ. A) Chemical structure of PhAH. B) Ligand interaction diagram (left) and binding amino acid residue sites (right) of the highest-scoring PhAH and ENO1 protein molecular docking complex (RMSD = 1.9977; E_score = −3.9538). C) WB detection of the interaction between ECM1 and ENO1, as well as Tyr phosphorylation of ENO1 following immunoprecipitating ENO1 in C4-2B cells in the presence of ECM1 (200 ng mL−1) with or without PhAH (1 μM). D) IF staining and quantiﬁcation of GRB2, SOS1, and DiI in C4-2B cells

Techniques: Binding Assay, Residue, Phospho-proteomics, Staining

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.

doi: 10.1002/advs.202407662

Figure Lengend Snippet: Figure 9. Schematic diagram illustrating that increased osteoblast-derived ECM1 from the bone microenvironment of BMPC patients induced by ENZ treatment, interacts with the ENO1 receptor on the prostate cancer cell membrane, further recruiting adapter proteins including GRB2 and SOS1, which activates the downstream MAPK signaling pathway to promote the proliferation of PCa cells and induce anti-androgen resistance.

Techniques: Derivative Assay, Membrane

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sos1 rabbit pab (Proteintech)

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1) Product Images from "Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer."

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