length sequencing Search Results


90
Genentech inc full length hghr cdna coding sequence
Full Length Hghr Cdna Coding Sequence, supplied by Genentech inc, 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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Labomics Inc luciferase reporter constructs containing the full-length 3’utr sequence of the cyp11b2 gene
Luciferase Reporter Constructs Containing The Full Length 3’utr Sequence Of The Cyp11b2 Gene, supplied by Labomics Inc, 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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Genome Systems Inc full-length cdna clone containing the complete coding sequence of human ab-crystallin
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GenScript corporation coding sequences of full-length taf8 and taf10
Coding Sequences Of Full Length Taf8 And Taf10, 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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GenScript corporation full length codon optimized cdna sequence encoding dianthus caryophyllus ethylene receptor dcetr1
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Full Length Codon Optimized Cdna Sequence Encoding Dianthus Caryophyllus Ethylene Receptor Dcetr1, 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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Average 90 stars, based on 1 article reviews
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GenScript corporation pxn-as1-l full-length sequences
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Pxn As1 L Full Length Sequences, 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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GenScript corporation synthetic mtdef4 gene (seq id no:72)
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Synthetic Mtdef4 Gene (Seq Id No:72), 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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Makoto USA Inc plasmids p(+)jps07e2
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Plasmids P(+)Jps07e2, supplied by Makoto USA Inc, 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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Oxford Nanopore transcriptome sequencing
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Transcriptome Sequencing, supplied by Oxford Nanopore, 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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Average 90 stars, based on 1 article reviews
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BGI Shenzhen full-length hbv genome sequences pthbv2
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Full Length Hbv Genome Sequences Pthbv2, supplied by BGI Shenzhen, 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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Average 90 stars, based on 1 article reviews
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Oxford Nanopore sequencing read length and coverage
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Sequencing Read Length And Coverage, supplied by Oxford Nanopore, 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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Blue Heron Biotech full-length mutant toxins a and b open reading frames (orfs) based on strain 630δgenome sequences
Molecular binding studies of carnation ethylene receptor <t>DcETR1.</t> ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).
Full Length Mutant Toxins A And B Open Reading Frames (Orfs) Based On Strain 630δgenome Sequences, supplied by Blue Heron Biotech, 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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Average 90 stars, based on 1 article reviews
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Image Search Results


Molecular binding studies of carnation ethylene receptor DcETR1. ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).

Journal: Scientific Reports

Article Title: The NOP-1 peptide derived from the central regulator of ethylene signaling EIN2 delays floral senescence in cut flowers

doi: 10.1038/s41598-018-37571-x

Figure Lengend Snippet: Molecular binding studies of carnation ethylene receptor DcETR1. ( A ) Microscale Thermophoresis (MST) binding studies using recombinant carnation ethylene receptor DcETR1 and AtEIN2. Titration of unlabeled AtEIN2 to labeled DcETR1 (•) revealed binding of both proteins at a dissociation constant (K D ) of 135 nM ± 0.35 nM, indicating a tight interaction between DcETR1 and AtEIN2. ( B ) MST binding studies on DcETR1 and NOP-1. Titration of unlabeled NOP-1 to labeled DcETR1 (•) resulted in a K D of 3.49 µM ± 0.55 µM. Asterisks (*) indicate the labeling of DcETR1 with AlexaFluor488-NHS. Negative controls using chemically denatured DcETR1 shows no interaction with the EIN2 protein or the NOP-1 peptide (•).

Article Snippet: According to the published sequence (Carnation DB: Dca62022.1), full length codon optimized cDNA sequence encoding Dianthus caryophyllus ethylene receptor DcETR1 was ordered at GenScript United States.

Techniques: Binding Assay, Microscale Thermophoresis, Recombinant, Titration, Labeling