primary antibodies anti ptpn13 antibody Search Results


90
Bioss anti fap alexa fluor 647
Anti Fap Alexa Fluor 647, supplied by Bioss, 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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NSJ Bioreagents ha tag antibody
Ha Tag Antibody, supplied by NSJ Bioreagents, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Abnova rabbit anti-ptpn13 pab
Rabbit Anti Ptpn13 Pab, supplied by Abnova, 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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Proteintech anti ptpn13
Anti Ptpn13, supplied by Proteintech, 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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R&D Systems anti ptpn13
Anti Ptpn13, 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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egfr  (Abcam)
94
Abcam egfr
<t>PTPN13</t> rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of <t>EGFR/AKT</t> pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.
Egfr, supplied by Abcam, 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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Bio-Techne corporation ptpn13/ptpl1 antibody
<t>PTPN13</t> rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of <t>EGFR/AKT</t> pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.
Ptpn13/Ptpl1 Antibody, supplied by Bio-Techne corporation, 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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Bio-Techne corporation tnip2 antibody
<t>PTPN13</t> rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of <t>EGFR/AKT</t> pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.
Tnip2 Antibody, supplied by Bio-Techne corporation, 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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94
Boster Bio anti ptpn2
<t>PTPN13</t> rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of <t>EGFR/AKT</t> pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.
Anti Ptpn2, supplied by Boster Bio, 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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86
Merck & Co anti ha
Analysis of the interaction between β-catenin and PTPN13. β-catenin levels were analysed in T cells from a healthy control and patients from two different families harbouring PTPN13 mutations: Family A, carrying a homozygous p.R1838Q mutation (A-1), and Family B, carrying heterozygous p.W1274C and p.S1004del mutations (B-1, B-2). A representative Western blot is shown in ( A ), while the quantification of five independent experiments is presented in ( B ). ( C ) Schematic representation of the modular structure of β-catenin and the constructs used in the in vitro protein interaction experiments: full-length β-catenin (blue line), a construct lacking the C-terminal region (β-catenin ΔC, green line), and a construct containing only the C-terminal region (β-catenin C-terminal, boxed in purple). ( D ) Schematic representation of the modular structure of PTPN13 and the constructs used: full-length PTPN13, the N-terminal region including the KIND and FERM domains (boxed in orange), the central region containing the five PDZ domains (boxed in pink), and the C-terminal region containing the PTP domain (boxed in grey). The interaction between β-catenin and PTPN13 was assessed by pull-down assays as described in the Methods section. ( E ) Representative experiment showing the interaction between full-length PTPN13 and the three β-catenin constructs. The input extract is shown in the first lane, followed by the pull-down interaction in the subsequent lanes. ( F ) Quantification of these experiments. ( G ) Representative experiment demonstrating the interaction between full-length β-catenin and the four PTPN13 constructs. The upper panel shows the pull-down interaction, and the lower panel displays the corresponding input. ( H ) Quantification of these <t>experiments.</t> <t>Anti-HA</t> was used to detect (E–G) and quantify PTPN13 signals (F–H), as all constructs carry this tag. The arrowhead indicates the expected size of the PTPN13 construct. Statistically significant differences relative to the corresponding control (black column) are indicated as follows: *** p < 0.001 and ** p < 0.01. Cropped blots are shown for clarity. Original blots are presented in the Supplementary File.
Anti Ha, supplied by Merck & Co, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Cell Signaling Technology Inc antiphospho cdc2 antibody
Analysis of the interaction between β-catenin and PTPN13. β-catenin levels were analysed in T cells from a healthy control and patients from two different families harbouring PTPN13 mutations: Family A, carrying a homozygous p.R1838Q mutation (A-1), and Family B, carrying heterozygous p.W1274C and p.S1004del mutations (B-1, B-2). A representative Western blot is shown in ( A ), while the quantification of five independent experiments is presented in ( B ). ( C ) Schematic representation of the modular structure of β-catenin and the constructs used in the in vitro protein interaction experiments: full-length β-catenin (blue line), a construct lacking the C-terminal region (β-catenin ΔC, green line), and a construct containing only the C-terminal region (β-catenin C-terminal, boxed in purple). ( D ) Schematic representation of the modular structure of PTPN13 and the constructs used: full-length PTPN13, the N-terminal region including the KIND and FERM domains (boxed in orange), the central region containing the five PDZ domains (boxed in pink), and the C-terminal region containing the PTP domain (boxed in grey). The interaction between β-catenin and PTPN13 was assessed by pull-down assays as described in the Methods section. ( E ) Representative experiment showing the interaction between full-length PTPN13 and the three β-catenin constructs. The input extract is shown in the first lane, followed by the pull-down interaction in the subsequent lanes. ( F ) Quantification of these experiments. ( G ) Representative experiment demonstrating the interaction between full-length β-catenin and the four PTPN13 constructs. The upper panel shows the pull-down interaction, and the lower panel displays the corresponding input. ( H ) Quantification of these <t>experiments.</t> <t>Anti-HA</t> was used to detect (E–G) and quantify PTPN13 signals (F–H), as all constructs carry this tag. The arrowhead indicates the expected size of the PTPN13 construct. Statistically significant differences relative to the corresponding control (black column) are indicated as follows: *** p < 0.001 and ** p < 0.01. Cropped blots are shown for clarity. Original blots are presented in the Supplementary File.
Antiphospho Cdc2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
Abcam β actin
Analysis of the interaction between β-catenin and PTPN13. β-catenin levels were analysed in T cells from a healthy control and patients from two different families harbouring PTPN13 mutations: Family A, carrying a homozygous p.R1838Q mutation (A-1), and Family B, carrying heterozygous p.W1274C and p.S1004del mutations (B-1, B-2). A representative Western blot is shown in ( A ), while the quantification of five independent experiments is presented in ( B ). ( C ) Schematic representation of the modular structure of β-catenin and the constructs used in the in vitro protein interaction experiments: full-length β-catenin (blue line), a construct lacking the C-terminal region (β-catenin ΔC, green line), and a construct containing only the C-terminal region (β-catenin C-terminal, boxed in purple). ( D ) Schematic representation of the modular structure of PTPN13 and the constructs used: full-length PTPN13, the N-terminal region including the KIND and FERM domains (boxed in orange), the central region containing the five PDZ domains (boxed in pink), and the C-terminal region containing the PTP domain (boxed in grey). The interaction between β-catenin and PTPN13 was assessed by pull-down assays as described in the Methods section. ( E ) Representative experiment showing the interaction between full-length PTPN13 and the three β-catenin constructs. The input extract is shown in the first lane, followed by the pull-down interaction in the subsequent lanes. ( F ) Quantification of these experiments. ( G ) Representative experiment demonstrating the interaction between full-length β-catenin and the four PTPN13 constructs. The upper panel shows the pull-down interaction, and the lower panel displays the corresponding input. ( H ) Quantification of these <t>experiments.</t> <t>Anti-HA</t> was used to detect (E–G) and quantify PTPN13 signals (F–H), as all constructs carry this tag. The arrowhead indicates the expected size of the PTPN13 construct. Statistically significant differences relative to the corresponding control (black column) are indicated as follows: *** p < 0.001 and ** p < 0.01. Cropped blots are shown for clarity. Original blots are presented in the Supplementary File.
β Actin, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


PTPN13 rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of EGFR/AKT pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.

Journal: Journal of Cellular and Molecular Medicine

Article Title: MicroRNA‐30e‐5p promotes cell growth by targeting PTPN13 and indicates poor survival and recurrence in lung adenocarcinoma

doi: 10.1111/jcmm.13198

Figure Lengend Snippet: PTPN13 rescued tumour proliferation‐promoting effects by miR‐30e. ( A and B ) The effects of PTPN13 overexpression on cell proliferation in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by MTT assay. ( C and D ) The effects of PTPN13 overexpression on the protein expression of EGFR/AKT pathway in miR‐30e‐transfected A549 and NCI‐H23 cells indicated by western blotting. ( E and F ) The effects of PTPN13 knockdown on the protein expression of EGFR/AKT pathway in sh‐miR‐30e‐transfected A549 and NCI‐H23 cells indicated by Western blotting.

Article Snippet: Lentivirus‐mediated miR‐30e overexpression, miR‐30e shRNA and PTPN13 overexpression vectors, negative control vector (NC) and virion‐packaging elements were from Genechem (Shanghai, China); The primary antibodies of PTPN13 (rabbit monoclonal antibody, ab198882), β‐actin (mouse monoclonal antibody, ab8226), EGFR (rabbit monoclonal antibody, ab52894), AKT(rabbit polyclonal antibody, ab126811), p‐AKT(rabbit polyclonal antibody, ab18206) were from Abcam (Cambridge, MA, USA).

Techniques: Over Expression, Transfection, MTT Assay, Expressing, Western Blot

Analysis of the interaction between β-catenin and PTPN13. β-catenin levels were analysed in T cells from a healthy control and patients from two different families harbouring PTPN13 mutations: Family A, carrying a homozygous p.R1838Q mutation (A-1), and Family B, carrying heterozygous p.W1274C and p.S1004del mutations (B-1, B-2). A representative Western blot is shown in ( A ), while the quantification of five independent experiments is presented in ( B ). ( C ) Schematic representation of the modular structure of β-catenin and the constructs used in the in vitro protein interaction experiments: full-length β-catenin (blue line), a construct lacking the C-terminal region (β-catenin ΔC, green line), and a construct containing only the C-terminal region (β-catenin C-terminal, boxed in purple). ( D ) Schematic representation of the modular structure of PTPN13 and the constructs used: full-length PTPN13, the N-terminal region including the KIND and FERM domains (boxed in orange), the central region containing the five PDZ domains (boxed in pink), and the C-terminal region containing the PTP domain (boxed in grey). The interaction between β-catenin and PTPN13 was assessed by pull-down assays as described in the Methods section. ( E ) Representative experiment showing the interaction between full-length PTPN13 and the three β-catenin constructs. The input extract is shown in the first lane, followed by the pull-down interaction in the subsequent lanes. ( F ) Quantification of these experiments. ( G ) Representative experiment demonstrating the interaction between full-length β-catenin and the four PTPN13 constructs. The upper panel shows the pull-down interaction, and the lower panel displays the corresponding input. ( H ) Quantification of these experiments. Anti-HA was used to detect (E–G) and quantify PTPN13 signals (F–H), as all constructs carry this tag. The arrowhead indicates the expected size of the PTPN13 construct. Statistically significant differences relative to the corresponding control (black column) are indicated as follows: *** p < 0.001 and ** p < 0.01. Cropped blots are shown for clarity. Original blots are presented in the Supplementary File.

Journal: Scientific Reports

Article Title: Altered PTPN13–β-catenin interaction by pathogenic mutations and involvement of this axis in B-cell receptor signalling

doi: 10.1038/s41598-025-33151-y

Figure Lengend Snippet: Analysis of the interaction between β-catenin and PTPN13. β-catenin levels were analysed in T cells from a healthy control and patients from two different families harbouring PTPN13 mutations: Family A, carrying a homozygous p.R1838Q mutation (A-1), and Family B, carrying heterozygous p.W1274C and p.S1004del mutations (B-1, B-2). A representative Western blot is shown in ( A ), while the quantification of five independent experiments is presented in ( B ). ( C ) Schematic representation of the modular structure of β-catenin and the constructs used in the in vitro protein interaction experiments: full-length β-catenin (blue line), a construct lacking the C-terminal region (β-catenin ΔC, green line), and a construct containing only the C-terminal region (β-catenin C-terminal, boxed in purple). ( D ) Schematic representation of the modular structure of PTPN13 and the constructs used: full-length PTPN13, the N-terminal region including the KIND and FERM domains (boxed in orange), the central region containing the five PDZ domains (boxed in pink), and the C-terminal region containing the PTP domain (boxed in grey). The interaction between β-catenin and PTPN13 was assessed by pull-down assays as described in the Methods section. ( E ) Representative experiment showing the interaction between full-length PTPN13 and the three β-catenin constructs. The input extract is shown in the first lane, followed by the pull-down interaction in the subsequent lanes. ( F ) Quantification of these experiments. ( G ) Representative experiment demonstrating the interaction between full-length β-catenin and the four PTPN13 constructs. The upper panel shows the pull-down interaction, and the lower panel displays the corresponding input. ( H ) Quantification of these experiments. Anti-HA was used to detect (E–G) and quantify PTPN13 signals (F–H), as all constructs carry this tag. The arrowhead indicates the expected size of the PTPN13 construct. Statistically significant differences relative to the corresponding control (black column) are indicated as follows: *** p < 0.001 and ** p < 0.01. Cropped blots are shown for clarity. Original blots are presented in the Supplementary File.

Article Snippet: Commercial primary antibodies were obtained from the following sources: Becton Dickinson – anti-β-catenin (#610154), anti-BTK (#611116), anti-phospho-ERK (pT202/pY204) (#612358); Cell Signaling Technology – anti-phospho-BTK (pY223) (#5082S), anti-phospho-PLCγ2 (pY1217) (#3871S); MERCKanti-HA (#11867423001); Santa Cruz Biotechnology – anti-ERK (sc-94), anti-PLCγ2 (sc-5283), anti-PTPN13 (sc-67164).

Techniques: Control, Mutagenesis, Western Blot, Construct, In Vitro