pf3a wg bydv Search Results


pf3a-wg (bydv)-flexi backbone  (Promega)
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cfp  (Promega)
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Promega cfp
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tnt® sp6 high-yield protein expression system  (Promega)
90
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flexi vector system  (Promega)
90
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in vitro transcription/translation system from wheat germ extract  (Promega)
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Promega in vitro transcription/translation system from wheat germ extract
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maxr60q cdna  (GenScript corporation)
90
GenScript corporation maxr60q cdna
Maxr60q Cdna, supplied by GenScript 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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max cdna  (GenScript corporation)
90
GenScript corporation max cdna
Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and <t>MXD1-MAX</t> heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells
Max Cdna, supplied by GenScript 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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wheat germ (wg) cell free expression mix  (Promega)
90
Promega wheat germ (wg) cell free expression mix
Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and <t>MXD1-MAX</t> heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells
Wheat Germ (Wg) Cell Free Expression Mix, supplied by Promega, 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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c-myc cdna  (GenScript corporation)
90
GenScript corporation c-myc cdna
Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and <t>MXD1-MAX</t> heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells
C Myc Cdna, supplied by GenScript 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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emsa cdnas  (GenScript corporation)
90
GenScript corporation emsa cdnas
Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and <t>MXD1-MAX</t> heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells
Emsa Cdnas, supplied by GenScript 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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pezr-h-ln  (Promega)
90
Promega pezr-h-ln
Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and <t>MXD1-MAX</t> heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells
Pezr H Ln, supplied by Promega, 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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tnt sp6 high yield wheat germ mastermix  (Promega)
90
Promega tnt sp6 high yield wheat germ mastermix
Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and <t>MXD1-MAX</t> heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells
Tnt Sp6 High Yield Wheat Germ Mastermix, supplied by Promega, 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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Image Search Results


Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and MXD1-MAX heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells

Journal: Genome Medicine

Article Title: A case study of an integrative genomic and experimental therapeutic approach for rare tumors: identification of vulnerabilities in a pediatric poorly differentiated carcinoma

doi: 10.1186/s13073-016-0366-0

Figure Lengend Snippet: Structural and functional analyses of Variants of Unknown Significance (VUS). a – c Structures of MAX homodimer and C-MYC-MAX and MXD1-MAX heterodimers in complex with DNA. a MAX-MAX homodimer crystal structure (PDB id: 1AN2) in which the subunit A ( yellow for carbon atoms) and B ( cyan for carbon atoms) are represented and the side chains of several invariant residues are depicted with stick models and labeled. b Crystal structure of C-MYC/-MAX heterodimer in complex with DNA (PDB id: 1NKP). MAX and C-MYC carbon atoms are represented in yellow and purple , respectively. c Crystal structure of MAX-MXD1 heterodimer in complex with DNA (PDB id: 1NLW). MAX and MXD1 carbon atoms are represented in yellow and green , respectively. In all structures presented, the MAX p.R60Q mutation is shown in magenta. Dashed lines ( black and magenta ) represent hydrogen bonds. The sugar-phosphate backbone of DNA is shown in orange with two selected nucleotides from each subunit shown as stick models. d MAX R60Q mutant heterodimerizes with C-MYC and MXD1 and binds to DNA. The indicated proteins were transcribed and translated in vitro and incubated with an E-box containing probe. Specific proteins/DNA complex bands are indicated on the left . Non-specific (ns) binding products present in the probe-only and vector control lanes are indicated on the left . e , f Structures of wild-type BRAF and BRAF p.K483E mutant. e Model of the BRAF kinase domain in complex with ATP ( black for carbon atoms) and a Mg 2+ ion ( dark green ), in which the side chains of five essential residues in BRAF, are shown, and labeled. The helix αC in its active conformation ( dark violet ) (PDB id: 4MNE) and in inactive conformation ( light gray ) (PDB id: 4WO5) is represented as cartoon and the side chain of the invariant E501 is depicted with stick models in two orientations. f Model of the BRAF kinase domain in which K483 is replaced by E ( magenta for carbon atoms). g Proteins levels and phosphorylation level of ERK1/2 upon transient transfection of the indicated BRAF proteins in HEK 293 T cells

Article Snippet: MAX, MAXR60Q, C-MYC, and MXD1 cDNAs were generated by gene synthesis (GenScript) and cloned into pF3A WG (BYDV) Flexi® Vector (Promega).

Techniques: Functional Assay, Labeling, Mutagenesis, In Vitro, Incubation, Binding Assay, Plasmid Preparation, Control, Phospho-proteomics, Transfection