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Addgene inc constructs expressing ptpn11 wild type wt

Figure 1. <t>PTPN11</t> mutation occurrence and co-occurrence alongside other mutations in both lung adenocarcinomas and squamous cell carcinomas. PTPN11 mutation occurrence rate across the genotyped tumour tissue of NSCLC patients (n = 356) and TCGA data (n = 586) (A). Oncoprint shows the gene alterations in each individual with PTPN11-mutated NSCLC (n = 37), focusing on known cancer-related genes. Each box represents a patient; genes and corresponding alteration frequencies are listed (B). The type of PTPN11 mutation occurring across both adenocarcinomas (LUAD) and squamous cell carcinoma cohorts (LUSC) is displayed (n = 37) (C).

Constructs Expressing Ptpn11 Wild Type Wt, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 8 article reviews

constructs expressing ptpn11 wild type wt - by Bioz Stars, 2026-05

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1) Product Images from "Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC)."

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

Journal: International journal of molecular sciences

doi: 10.3390/ijms241310545

Figure 1. PTPN11 mutation occurrence and co-occurrence alongside other mutations in both lung adenocarcinomas and squamous cell carcinomas. PTPN11 mutation occurrence rate across the genotyped tumour tissue of NSCLC patients (n = 356) and TCGA data (n = 586) (A). Oncoprint shows the gene alterations in each individual with PTPN11-mutated NSCLC (n = 37), focusing on known cancer-related genes. Each box represents a patient; genes and corresponding alteration frequencies are listed (B). The type of PTPN11 mutation occurring across both adenocarcinomas (LUAD) and squamous cell carcinoma cohorts (LUSC) is displayed (n = 37) (C).

Figure Legend Snippet: Figure 1. PTPN11 mutation occurrence and co-occurrence alongside other mutations in both lung adenocarcinomas and squamous cell carcinomas. PTPN11 mutation occurrence rate across the genotyped tumour tissue of NSCLC patients (n = 356) and TCGA data (n = 586) (A). Oncoprint shows the gene alterations in each individual with PTPN11-mutated NSCLC (n = 37), focusing on known cancer-related genes. Each box represents a patient; genes and corresponding alteration frequencies are listed (B). The type of PTPN11 mutation occurring across both adenocarcinomas (LUAD) and squamous cell carcinoma cohorts (LUSC) is displayed (n = 37) (C).

Techniques Used: Mutagenesis

Figure 2. PTPN11 mutations promote IL-3-independent survival of Ba/F3 cells. The stable expression of E76A and A72D PTPN11 mutations promoted IL-3 independent survival of Ba/F3 cells. Ba/F3 cells transduced with indicated vectors (EV = empty vector, pBabe) were plated in the absence of IL-3. Viable cells were determined at 0 h, 24 h, 48 h, 96 h, and 120 h. Results are representative of three independent experiments. Data are represented as mean ± s.e.m. **** p < 0.0001.

Figure Legend Snippet: Figure 2. PTPN11 mutations promote IL-3-independent survival of Ba/F3 cells. The stable expression of E76A and A72D PTPN11 mutations promoted IL-3 independent survival of Ba/F3 cells. Ba/F3 cells transduced with indicated vectors (EV = empty vector, pBabe) were plated in the absence of IL-3. Viable cells were determined at 0 h, 24 h, 48 h, 96 h, and 120 h. Results are representative of three independent experiments. Data are represented as mean ± s.e.m. **** p < 0.0001.

Techniques Used: Expressing, Transduction, Plasmid Preparation

Figure 3. PTPN11 mutations result in elevated SHP2-phosphatse activity and activate MAPK and PI3K pathway signalling. Serum-starved cells treated with 100 ng/mL EGF for 5 min were lysed, and SHP2 was immunoprecipitated from whole cell lysates. Immunoprecipitate was used to de- termine phosphatase activity, as described in the materials and methods. (A) SHP2-phosphatse activity in H661 (PTPN11-mutated) compared to H1703 (PTPN11-WT), Calu-3 (PTPN11-WT), and H157 (PTPN11-WT, KRAS-mutated). Shp2-phosphatase activity in H1701 (B) and H1299 (C) cells transduced with indicated PTPN11 mutations. Data are represented as mean ± s.e.m. (n = 3). (D) NCI-H1703 and NCI-H157 cells were transduced with wildtype or mutated PTPN11: a serum starved and stimulated with an epidermal growth factor (100 ng/mL) for 5 min. p-ERK1/2—phospho- ERK 1/2; t-ERK1/2—total ERK 1/2; p-AKT ser 473—phospho-AKT (phosphorylated at serine 473); t-AKT—total AKT. Blots are representative of 3 independent experiments. (NS = No Signiﬁcance, * p < 0.05, ** p < 0.01, *** p <0.001)

Figure Legend Snippet: Figure 3. PTPN11 mutations result in elevated SHP2-phosphatse activity and activate MAPK and PI3K pathway signalling. Serum-starved cells treated with 100 ng/mL EGF for 5 min were lysed, and SHP2 was immunoprecipitated from whole cell lysates. Immunoprecipitate was used to de- termine phosphatase activity, as described in the materials and methods. (A) SHP2-phosphatse activity in H661 (PTPN11-mutated) compared to H1703 (PTPN11-WT), Calu-3 (PTPN11-WT), and H157 (PTPN11-WT, KRAS-mutated). Shp2-phosphatase activity in H1701 (B) and H1299 (C) cells transduced with indicated PTPN11 mutations. Data are represented as mean ± s.e.m. (n = 3). (D) NCI-H1703 and NCI-H157 cells were transduced with wildtype or mutated PTPN11: a serum starved and stimulated with an epidermal growth factor (100 ng/mL) for 5 min. p-ERK1/2—phospho- ERK 1/2; t-ERK1/2—total ERK 1/2; p-AKT ser 473—phospho-AKT (phosphorylated at serine 473); t-AKT—total AKT. Blots are representative of 3 independent experiments. (NS = No Signiﬁcance, * p < 0.05, ** p < 0.01, *** p <0.001)

Techniques Used: Activity Assay, Immunoprecipitation, Transduction

Figure 4. PTPN11/Shp2 inactivation with the PTPN11/Shp2 phosphatase mutation C459S. NCI-H157, NCI-H1703, and NCI-H661 cells were transduced with PTPN11 C459S: serum starved and stimulated with an epidermal growth factor (100 ng/mL) for 5 min. Parental cells were transfected with an empty vector. Phosphorylated-ERK 1/2 (pERK); total ERK 1/2 (tERK); Phosphorylated AKT (phosphory- lated at serine 473) (pAKT); total AKT (tAKT). Blots are representative of 3 independent experiments.

Figure Legend Snippet: Figure 4. PTPN11/Shp2 inactivation with the PTPN11/Shp2 phosphatase mutation C459S. NCI-H157, NCI-H1703, and NCI-H661 cells were transduced with PTPN11 C459S: serum starved and stimulated with an epidermal growth factor (100 ng/mL) for 5 min. Parental cells were transfected with an empty vector. Phosphorylated-ERK 1/2 (pERK); total ERK 1/2 (tERK); Phosphorylated AKT (phosphory- lated at serine 473) (pAKT); total AKT (tAKT). Blots are representative of 3 independent experiments.

Techniques Used: Mutagenesis, Transduction, Transfection, Plasmid Preparation

Figure 5. SHP2 inhibitor (SHPi) improves the response to MAPK and PI3K pathway targeting therapies. H661 and H1703 cells plated and after 24 h were treated with SHPi (10 µM) daily or Cop (20 nM) or Ref (10 µM) alone or in combination with SHPi. 72 h following treatment, an Alamar Blue cell viability assay was performed (A). Data (n = 3 independent experiments) are expressed as mean ± SEM. Statistical signiﬁcance was determined using one-way ANOVA correcting for multiple comparisons using Tukey’s test and reporting adjusted p values. (* p < 0.05, ** p < 0.01).

Figure Legend Snippet: Figure 5. SHP2 inhibitor (SHPi) improves the response to MAPK and PI3K pathway targeting therapies. H661 and H1703 cells plated and after 24 h were treated with SHPi (10 µM) daily or Cop (20 nM) or Ref (10 µM) alone or in combination with SHPi. 72 h following treatment, an Alamar Blue cell viability assay was performed (A). Data (n = 3 independent experiments) are expressed as mean ± SEM. Statistical signiﬁcance was determined using one-way ANOVA correcting for multiple comparisons using Tukey’s test and reporting adjusted p values. (* p < 0.05, ** p < 0.01).

Techniques Used: Viability Assay

Figure 7. PTPN11 and PI3K targeting treatments do not alter tumour formation or invasion in a chick embryo xenograft model. 2 × 106 H661 cells were implanted into the CAM according to the assay schedule (A) on day 7 of embryonic development. Following 72 h of tumour establishment, developing tumours were treated in situ. SHPi (10 µM) treatments were added daily, and Cop (20 nM) treatments were added once on day 10. On day 14, tumour visibility was noted as either visible (VT) or non-visible (NVT). Statistical signiﬁcance was determined using Fisher’s exact test, and no statistical signiﬁcance was found (B) On day 14, xenografts were excised with the silicon ring, formalin-ﬁxed, and stained for H&E (C,D). Areas of tumour were denoted by black arrows, and CAM areas were demonstrated by red arrows and matrigel was denoted by grey arrows. Images were collected an EVOS m5000 microscope with EVOS imaging software at 4× and 20× magniﬁcation (D).

Figure Legend Snippet: Figure 7. PTPN11 and PI3K targeting treatments do not alter tumour formation or invasion in a chick embryo xenograft model. 2 × 106 H661 cells were implanted into the CAM according to the assay schedule (A) on day 7 of embryonic development. Following 72 h of tumour establishment, developing tumours were treated in situ. SHPi (10 µM) treatments were added daily, and Cop (20 nM) treatments were added once on day 10. On day 14, tumour visibility was noted as either visible (VT) or non-visible (NVT). Statistical signiﬁcance was determined using Fisher’s exact test, and no statistical signiﬁcance was found (B) On day 14, xenografts were excised with the silicon ring, formalin-ﬁxed, and stained for H&E (C,D). Areas of tumour were denoted by black arrows, and CAM areas were demonstrated by red arrows and matrigel was denoted by grey arrows. Images were collected an EVOS m5000 microscope with EVOS imaging software at 4× and 20× magniﬁcation (D).

Techniques Used: In Situ, Staining, Microscopy, Imaging, Software

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Journal: International journal of molecular sciences

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

doi: 10.3390/ijms241310545

Figure Lengend Snippet: Figure 1. PTPN11 mutation occurrence and co-occurrence alongside other mutations in both lung adenocarcinomas and squamous cell carcinomas. PTPN11 mutation occurrence rate across the genotyped tumour tissue of NSCLC patients (n = 356) and TCGA data (n = 586) (A). Oncoprint shows the gene alterations in each individual with PTPN11-mutated NSCLC (n = 37), focusing on known cancer-related genes. Each box represents a patient; genes and corresponding alteration frequencies are listed (B). The type of PTPN11 mutation occurring across both adenocarcinomas (LUAD) and squamous cell carcinoma cohorts (LUSC) is displayed (n = 37) (C).

Article Snippet: The constructs expressing PTPN11 wild type (WT), E76A, and C459S (Ben Neel, Addgene plasmids 8329, 8331, and 8382, respectively) were obtained.

Techniques: Mutagenesis

Journal: International journal of molecular sciences

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

doi: 10.3390/ijms241310545

Figure Lengend Snippet: Figure 2. PTPN11 mutations promote IL-3-independent survival of Ba/F3 cells. The stable expression of E76A and A72D PTPN11 mutations promoted IL-3 independent survival of Ba/F3 cells. Ba/F3 cells transduced with indicated vectors (EV = empty vector, pBabe) were plated in the absence of IL-3. Viable cells were determined at 0 h, 24 h, 48 h, 96 h, and 120 h. Results are representative of three independent experiments. Data are represented as mean ± s.e.m. **** p < 0.0001.

Article Snippet: The constructs expressing PTPN11 wild type (WT), E76A, and C459S (Ben Neel, Addgene plasmids 8329, 8331, and 8382, respectively) were obtained.

Techniques: Expressing, Transduction, Plasmid Preparation

Journal: International journal of molecular sciences

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

doi: 10.3390/ijms241310545

Figure Lengend Snippet: Figure 3. PTPN11 mutations result in elevated SHP2-phosphatse activity and activate MAPK and PI3K pathway signalling. Serum-starved cells treated with 100 ng/mL EGF for 5 min were lysed, and SHP2 was immunoprecipitated from whole cell lysates. Immunoprecipitate was used to de- termine phosphatase activity, as described in the materials and methods. (A) SHP2-phosphatse activity in H661 (PTPN11-mutated) compared to H1703 (PTPN11-WT), Calu-3 (PTPN11-WT), and H157 (PTPN11-WT, KRAS-mutated). Shp2-phosphatase activity in H1701 (B) and H1299 (C) cells transduced with indicated PTPN11 mutations. Data are represented as mean ± s.e.m. (n = 3). (D) NCI-H1703 and NCI-H157 cells were transduced with wildtype or mutated PTPN11: a serum starved and stimulated with an epidermal growth factor (100 ng/mL) for 5 min. p-ERK1/2—phospho- ERK 1/2; t-ERK1/2—total ERK 1/2; p-AKT ser 473—phospho-AKT (phosphorylated at serine 473); t-AKT—total AKT. Blots are representative of 3 independent experiments. (NS = No Signiﬁcance, * p < 0.05, ** p < 0.01, *** p <0.001)

Article Snippet: The constructs expressing PTPN11 wild type (WT), E76A, and C459S (Ben Neel, Addgene plasmids 8329, 8331, and 8382, respectively) were obtained.

Techniques: Activity Assay, Immunoprecipitation, Transduction

Journal: International journal of molecular sciences

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

doi: 10.3390/ijms241310545

Figure Lengend Snippet: Figure 4. PTPN11/Shp2 inactivation with the PTPN11/Shp2 phosphatase mutation C459S. NCI-H157, NCI-H1703, and NCI-H661 cells were transduced with PTPN11 C459S: serum starved and stimulated with an epidermal growth factor (100 ng/mL) for 5 min. Parental cells were transfected with an empty vector. Phosphorylated-ERK 1/2 (pERK); total ERK 1/2 (tERK); Phosphorylated AKT (phosphory- lated at serine 473) (pAKT); total AKT (tAKT). Blots are representative of 3 independent experiments.

Article Snippet: The constructs expressing PTPN11 wild type (WT), E76A, and C459S (Ben Neel, Addgene plasmids 8329, 8331, and 8382, respectively) were obtained.

Techniques: Mutagenesis, Transduction, Transfection, Plasmid Preparation

Journal: International journal of molecular sciences

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

doi: 10.3390/ijms241310545

Figure Lengend Snippet: Figure 5. SHP2 inhibitor (SHPi) improves the response to MAPK and PI3K pathway targeting therapies. H661 and H1703 cells plated and after 24 h were treated with SHPi (10 µM) daily or Cop (20 nM) or Ref (10 µM) alone or in combination with SHPi. 72 h following treatment, an Alamar Blue cell viability assay was performed (A). Data (n = 3 independent experiments) are expressed as mean ± SEM. Statistical signiﬁcance was determined using one-way ANOVA correcting for multiple comparisons using Tukey’s test and reporting adjusted p values. (* p < 0.05, ** p < 0.01).

Article Snippet: The constructs expressing PTPN11 wild type (WT), E76A, and C459S (Ben Neel, Addgene plasmids 8329, 8331, and 8382, respectively) were obtained.

Techniques: Viability Assay

Journal: International journal of molecular sciences

Article Title: Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC).

doi: 10.3390/ijms241310545

Figure Lengend Snippet: Figure 7. PTPN11 and PI3K targeting treatments do not alter tumour formation or invasion in a chick embryo xenograft model. 2 × 106 H661 cells were implanted into the CAM according to the assay schedule (A) on day 7 of embryonic development. Following 72 h of tumour establishment, developing tumours were treated in situ. SHPi (10 µM) treatments were added daily, and Cop (20 nM) treatments were added once on day 10. On day 14, tumour visibility was noted as either visible (VT) or non-visible (NVT). Statistical signiﬁcance was determined using Fisher’s exact test, and no statistical signiﬁcance was found (B) On day 14, xenografts were excised with the silicon ring, formalin-ﬁxed, and stained for H&E (C,D). Areas of tumour were denoted by black arrows, and CAM areas were demonstrated by red arrows and matrigel was denoted by grey arrows. Images were collected an EVOS m5000 microscope with EVOS imaging software at 4× and 20× magniﬁcation (D).

Article Snippet: The constructs expressing PTPN11 wild type (WT), E76A, and C459S (Ben Neel, Addgene plasmids 8329, 8331, and 8382, respectively) were obtained.

Techniques: In Situ, Staining, Microscopy, Imaging, Software

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1) Product Images from "Protein Tyrosine Phosphatase Non-Receptor 11 ( PTPN11 /Shp2) as a Driver Oncogene and a Novel Therapeutic Target in Non-Small Cell Lung Cancer (NSCLC)."

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