antibody cdx2 gtx Search Results


antibody cdx2 gtx#32513  (GeneTex)
90
GeneTex antibody cdx2 gtx#32513
Antibody Cdx2 Gtx#32513, supplied by GeneTex, 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/antibody cdx2 gtx#32513/product/GeneTex
Average 90 stars, based on 1 article reviews
antibody cdx2 gtx#32513 - by Bioz Stars, 2026-04
90/100 stars
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oct2  (Proteintech)
92
Proteintech oct2
Oct2, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/oct2/product/Proteintech
Average 92 stars, based on 1 article reviews
oct2 - by Bioz Stars, 2026-04
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magi1  (Millipore)
90
Millipore magi1
AmotL2 associates to the E-cadherin junctional complex. ( a ) Endogenous amotL2, co-immunoprecipitates with E-cadherin, α-catenin, β-catenin, <t>MAGI1</t> and actin in MDCK cells. The experiment was repeated four times with the same result. Affinity purified rabbit IgG was used as negative control. ( b ) Schematic model depicting the protein binding domains of the human p100 AmotL2 protein (ensemble ENST00000422605). Putative coiled-coil domain (314–572), C-terminal PDZ-binding motif (778–780) and the N-terminal LPTY (104–107) and PPQY (210–213) WW-binding sites. Listed are also the deletion constructs (black lines) and the mutation constructs used to define the E-cadherin binding site. ( c ). Immunoprecipitation analysis using exogenous transfected fragments of human amotL2 (as shown in ( b )). Comparison of the binding patterns to the distinct fragments identified a domain between 220–307 a.a. as being essential for the association to E-cadherin. The experiment was repeated three times showing the same result. ( d ) Mutation of the PPQY motif (Y213A), LPTY (Y107A) or deletion of the PDZ-binding motif (ΔILI) did not affect the binding to E-cadherin. When the LPTY motif was mutated to LPTA (Y107A), the binding of AmotL2 to MAGI1 and actin was lost. The double mutant construct LPTA_PPQA (Y107A_Y213A) showed a binding efficiency similar to the LPTA (Y107A) mutant. Thus, these data show that MAGI1/actin and E-cadherin associate to distinct binding sites of the N-terminal domain of AmotL2. The experiment was repeated three times with the same result.
Magi1, supplied by Millipore, 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/magi1/product/Millipore
Average 90 stars, based on 1 article reviews
magi1 - by Bioz Stars, 2026-04
90/100 stars
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tubulin  (Millipore)
90
Millipore tubulin
AmotL2 associates to the E-cadherin junctional complex. ( a ) Endogenous amotL2, co-immunoprecipitates with E-cadherin, α-catenin, β-catenin, <t>MAGI1</t> and actin in MDCK cells. The experiment was repeated four times with the same result. Affinity purified rabbit IgG was used as negative control. ( b ) Schematic model depicting the protein binding domains of the human p100 AmotL2 protein (ensemble ENST00000422605). Putative coiled-coil domain (314–572), C-terminal PDZ-binding motif (778–780) and the N-terminal LPTY (104–107) and PPQY (210–213) WW-binding sites. Listed are also the deletion constructs (black lines) and the mutation constructs used to define the E-cadherin binding site. ( c ). Immunoprecipitation analysis using exogenous transfected fragments of human amotL2 (as shown in ( b )). Comparison of the binding patterns to the distinct fragments identified a domain between 220–307 a.a. as being essential for the association to E-cadherin. The experiment was repeated three times showing the same result. ( d ) Mutation of the PPQY motif (Y213A), LPTY (Y107A) or deletion of the PDZ-binding motif (ΔILI) did not affect the binding to E-cadherin. When the LPTY motif was mutated to LPTA (Y107A), the binding of AmotL2 to MAGI1 and actin was lost. The double mutant construct LPTA_PPQA (Y107A_Y213A) showed a binding efficiency similar to the LPTA (Y107A) mutant. Thus, these data show that MAGI1/actin and E-cadherin associate to distinct binding sites of the N-terminal domain of AmotL2. The experiment was repeated three times with the same result.
Tubulin, supplied by Millipore, 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/tubulin/product/Millipore
Average 90 stars, based on 1 article reviews
tubulin - by Bioz Stars, 2026-04
90/100 stars
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Image Search Results


AmotL2 associates to the E-cadherin junctional complex. ( a ) Endogenous amotL2, co-immunoprecipitates with E-cadherin, α-catenin, β-catenin, MAGI1 and actin in MDCK cells. The experiment was repeated four times with the same result. Affinity purified rabbit IgG was used as negative control. ( b ) Schematic model depicting the protein binding domains of the human p100 AmotL2 protein (ensemble ENST00000422605). Putative coiled-coil domain (314–572), C-terminal PDZ-binding motif (778–780) and the N-terminal LPTY (104–107) and PPQY (210–213) WW-binding sites. Listed are also the deletion constructs (black lines) and the mutation constructs used to define the E-cadherin binding site. ( c ). Immunoprecipitation analysis using exogenous transfected fragments of human amotL2 (as shown in ( b )). Comparison of the binding patterns to the distinct fragments identified a domain between 220–307 a.a. as being essential for the association to E-cadherin. The experiment was repeated three times showing the same result. ( d ) Mutation of the PPQY motif (Y213A), LPTY (Y107A) or deletion of the PDZ-binding motif (ΔILI) did not affect the binding to E-cadherin. When the LPTY motif was mutated to LPTA (Y107A), the binding of AmotL2 to MAGI1 and actin was lost. The double mutant construct LPTA_PPQA (Y107A_Y213A) showed a binding efficiency similar to the LPTA (Y107A) mutant. Thus, these data show that MAGI1/actin and E-cadherin associate to distinct binding sites of the N-terminal domain of AmotL2. The experiment was repeated three times with the same result.

Journal: Scientific Reports

Article Title: The E-cadherin/AmotL2 complex organizes actin filaments required for epithelial hexagonal packing and blastocyst hatching

doi: 10.1038/s41598-017-10102-w

Figure Lengend Snippet: AmotL2 associates to the E-cadherin junctional complex. ( a ) Endogenous amotL2, co-immunoprecipitates with E-cadherin, α-catenin, β-catenin, MAGI1 and actin in MDCK cells. The experiment was repeated four times with the same result. Affinity purified rabbit IgG was used as negative control. ( b ) Schematic model depicting the protein binding domains of the human p100 AmotL2 protein (ensemble ENST00000422605). Putative coiled-coil domain (314–572), C-terminal PDZ-binding motif (778–780) and the N-terminal LPTY (104–107) and PPQY (210–213) WW-binding sites. Listed are also the deletion constructs (black lines) and the mutation constructs used to define the E-cadherin binding site. ( c ). Immunoprecipitation analysis using exogenous transfected fragments of human amotL2 (as shown in ( b )). Comparison of the binding patterns to the distinct fragments identified a domain between 220–307 a.a. as being essential for the association to E-cadherin. The experiment was repeated three times showing the same result. ( d ) Mutation of the PPQY motif (Y213A), LPTY (Y107A) or deletion of the PDZ-binding motif (ΔILI) did not affect the binding to E-cadherin. When the LPTY motif was mutated to LPTA (Y107A), the binding of AmotL2 to MAGI1 and actin was lost. The double mutant construct LPTA_PPQA (Y107A_Y213A) showed a binding efficiency similar to the LPTA (Y107A) mutant. Thus, these data show that MAGI1/actin and E-cadherin associate to distinct binding sites of the N-terminal domain of AmotL2. The experiment was repeated three times with the same result.

Article Snippet: The following primary antibodies were used: actin (abcam, ab 3280); for human and dog cells: AmotL2 (polyclonal antibodies reactive to human AmotL2 C-terminal peptide, NH2- CLDSVATSRVQDLSDMVEILI -COOH); for zebrafish: AmotL2 (polyclonal antibody reactive to zebrafish amotL2 C-terminal peptide NH2- CQKAPSAVDLFKGVDDVSAE- COOH), custom made by Innovagen (Lund, Sweden); for mouse blastocysts: AmotL2 (GeneTex, GTX 120712; for human blastocysts: AmotL2 (Aviva, OAAB05455); α-catenin (BD, 610193); β-catenin (BD, 610154); CDX2 (BioSite, MU392A-UC); for human and dog cells: E-cadherin (BD, 610181); for mouse blastocysts: E-cadherin (Sigma, U3254); Ezrin (BD, 610602); GFP (Life technologies, A10262); MAGI1 (Sigma, WH0009223M3); Tubulin (Sigma, T5168); YAP1 (Santa Cruz, sc-101199); ZO-1 (Invitrogene, 339100).

Techniques: Affinity Purification, Negative Control, Protein Binding, Binding Assay, Construct, Mutagenesis, Immunoprecipitation, Transfection