pact2 gal4 activation domain vector Search Results


pact2  (Vector Laboratories)
96
Vector Laboratories pact2
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pact2, supplied by Vector Laboratories, 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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pact2  (Becton Dickinson)
90
Becton Dickinson pact2
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pact2, supplied by Becton Dickinson, 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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gal4 activation-domain vector pact2  (Becton Dickinson)
90
Becton Dickinson gal4 activation-domain vector pact2
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Gal4 Activation Domain Vector Pact2, supplied by Becton Dickinson, 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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pact2 gw vector  (Thermo Fisher)
97
Thermo Fisher pact2 gw vector
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pact2 Gw Vector, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pact2+gal4+activation+domain+vector/Leupeptin+hemisulfate/us09107936-255-23-36
Average 97 stars, based on 1 article reviews
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pgad424  (Becton Dickinson)
90
Becton Dickinson pgad424
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pgad424, supplied by Becton Dickinson, 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/product/pact2+gal4+activation+domain+vector/pgad424/pmc00166698-417-6-24
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pgbt9  (Becton Dickinson)
90
Becton Dickinson pgbt9
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pgbt9, supplied by Becton Dickinson, 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/product/pact2+gal4+activation+domain+vector/pgbt9/pmc00166698-417-17-24
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gal4 activation domain ad fusion proteins  (Santa Cruz Biotechnology)
95
Santa Cruz Biotechnology gal4 activation domain ad fusion proteins
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Gal4 Activation Domain Ad Fusion Proteins, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pact2+gal4+activation+domain+vector/GAL4/pm10409627-73-0-13
Average 95 stars, based on 1 article reviews
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hf7c  (Becton Dickinson)
90
Becton Dickinson hf7c
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Hf7c, supplied by Becton Dickinson, 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/product/pact2+gal4+activation+domain+vector/hf7c/pmc00166698-417-27-33
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expression library of random primed c-dna from e.histolytica  (Vertis Biotechnologie)
90
Vertis Biotechnologie expression library of random primed c-dna from e.histolytica
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Expression Library Of Random Primed C Dna From E.Histolytica, supplied by Vertis Biotechnologie, 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/product/pact2+gal4+activation+domain+vector/expression+library+of+random+primed+c+dna+from+e+histolytica/pmc02824750-224-8-12
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pgbkt7-ebag9 bait vector  (Becton Dickinson)
90
Becton Dickinson pgbkt7-ebag9 bait vector
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pgbkt7 Ebag9 Bait Vector, supplied by Becton Dickinson, 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/product/pact2+gal4+activation+domain+vector/pgbkt7/pmc00551489-57-7-25
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plexa-km bait vector  (Becton Dickinson)
90
Becton Dickinson plexa-km bait vector
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Plexa Km Bait Vector, supplied by Becton Dickinson, 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/product/pact2+gal4+activation+domain+vector/plexa+km+bait+vector/pmc02776101-436-1-19
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pact2.2gtwy  (Addgene inc)
92
Addgene inc pact2.2gtwy
FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, <t>pACT2).</t> Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.
Pact2.2gtwy, supplied by Addgene inc, 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/product/pact2+gal4+activation+domain+vector/pACT2%2E2gtwy+(Plasmid+%2311346)/pmc08086697-49-15-35
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Image Search Results


FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, pACT2). Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.

Journal: Journal of Biological Chemistry

Article Title: Isoform Specificity of Ankyrin-B

doi: 10.1074/jbc.m506697200

Figure Lengend Snippet: FIGURE 1. Identification of an inter-domain interaction within ankyrin-B. A, domain organization of 220-kDa ankyrin-B. Ankyrin-B contains a membrane-binding domain, spectrin-binding domain, death domain, and C-terminal domain. The combination of death and C-terminal domain is termed the “regulatory domain.” B, ankyrin-B regulatory domain interacts with the membrane-binding domain in yeast two-hybrid assays. The ankyrin-B regulatory domain (fused with DNA-binding domain pAS2-1; Bait) was co- transformed into AH109 yeast strain with various ankyrin-B Prey constructs representing various ankyrin-B domains (fused to the DNA activation domain, pACT2). Positive inter- action was assessed by growth on media lacking adenine, histidine, leucine, tryptophan (-AHLT). We observed a positive interaction only when pAS2-1 regulatory domain was expressed with pACT2 membrane-binding domain.

Article Snippet: Fragments were PCR-amplified and inserted either in the pACT2 (GAL-4 activation domain vector) or pAS2-1 (GAL-4 DNA-binding domain vector).

Techniques: Membrane, Binding Assay, Transformation Assay, Construct, Activation Assay

FIGURE 3. Identification of the ankyrin-B membrane-binding domain site on the ankyrin-B regulatory domain. Yeast AH109 cells were co-transformed with ankyrin-B membrane-binding domain (fused with GAL-4 DNA activation domain) and one of ten Prey plasmids containing full-length or partial sequence of the ankyrin-B regulatory domain (amino acids 1445–1840). The death domain does not bind the membrane- binding domain while the C-terminal domain alone maintains binding affinity similar to the regulatory domain construct. The minimal binding region within the C-terminal domain is between amino acids 1556 and 1630. Deletion of this minimal binding region, D7, eliminates the intramolecular interaction. FIGURE 4. Identification of amino acids within the ankyrin-B C-terminal domain required for ankyrin-B inter-domain interaction. A, amino acid sequence within the C-terminal domain that contains membrane-binding domain activity. Amino acids cho- sen for alanine conversion are highlighted in red. Alanine-scanning mutants were gen- erated in the regulatory domain (pAS2-1) construct (see “Material and Methods” for details). B, a total of nine alanine-scanning mutants were screened for loss of binding to themembrane-bindingdomain(pACT2)revealingthataminoacidsGlu1597,Glu1598,and Asp1599 (regulatory 1597EEDAAA (pAS2-1)) are required for binding the membrane-bind- ing domain. The remaining eight mutants showed equivalent binding to the non-mu- tated regulatory domain.

Journal: Journal of Biological Chemistry

Article Title: Isoform Specificity of Ankyrin-B

doi: 10.1074/jbc.m506697200

Figure Lengend Snippet: FIGURE 3. Identification of the ankyrin-B membrane-binding domain site on the ankyrin-B regulatory domain. Yeast AH109 cells were co-transformed with ankyrin-B membrane-binding domain (fused with GAL-4 DNA activation domain) and one of ten Prey plasmids containing full-length or partial sequence of the ankyrin-B regulatory domain (amino acids 1445–1840). The death domain does not bind the membrane- binding domain while the C-terminal domain alone maintains binding affinity similar to the regulatory domain construct. The minimal binding region within the C-terminal domain is between amino acids 1556 and 1630. Deletion of this minimal binding region, D7, eliminates the intramolecular interaction. FIGURE 4. Identification of amino acids within the ankyrin-B C-terminal domain required for ankyrin-B inter-domain interaction. A, amino acid sequence within the C-terminal domain that contains membrane-binding domain activity. Amino acids cho- sen for alanine conversion are highlighted in red. Alanine-scanning mutants were gen- erated in the regulatory domain (pAS2-1) construct (see “Material and Methods” for details). B, a total of nine alanine-scanning mutants were screened for loss of binding to themembrane-bindingdomain(pACT2)revealingthataminoacidsGlu1597,Glu1598,and Asp1599 (regulatory 1597EEDAAA (pAS2-1)) are required for binding the membrane-bind- ing domain. The remaining eight mutants showed equivalent binding to the non-mu- tated regulatory domain.

Article Snippet: Fragments were PCR-amplified and inserted either in the pACT2 (GAL-4 activation domain vector) or pAS2-1 (GAL-4 DNA-binding domain vector).

Techniques: Membrane, Binding Assay, Transformation Assay, Activation Assay, Sequencing, Construct, Activity Assay