bluescript ii ks(1) phagemid (Agilent technologies)
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bluescript ii ks(1) phagemid
Bluescript Ii Ks(1) Phagemid, supplied by Agilent technologies, 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/bluescript+ii+ks(1)+phagemid/pm11527427-49-29-34
Average 90 stars, based on 1 article reviews
Bluescript Ii Ks(1) Phagemid, supplied by Agilent technologies, 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/bluescript+ii+ks(1)+phagemid/pm11527427-49-29-34
Average 90 stars, based on 1 article reviews
bluescript ii ks(1) phagemid - by Bioz Stars,
2026-10
90/100 stars
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Construct:Article Title: Design and evaluation of a tryptophanless RecA protein with wild type activity. Article Snippet: f t f b R o t o t a d a I f ( p i N R o e R t t t The C-terminal domain of the Escherichia coli RecA rotein contains two tryptophan residues whose naive fluorescence emission provides an interfering ackground signal when other fluorophores such as ,N-ethenoadenine, 2-aminopurine and other tryptohan residues are used to probe the protein’s activiies.. Replacement of the wild type tryptophans with onfluorescent residues is not trivial because one ryptophan is highly conserved and the C-terminal omain functions in both DNA binding as well as inerfilament protein–protein contact.. We undertook the ask of creating a tryptophanless RecA protein with T RecA activity by selecting suitable amino acid relacements for Trp290 and Trp308. Subcloning:Article Title: Design and evaluation of a tryptophanless RecA protein with wild type activity. Article Snippet: f t f b R o t o t a d a I f ( p i N R o e R t t t The C-terminal domain of the Escherichia coli RecA rotein contains two tryptophan residues whose naive fluorescence emission provides an interfering ackground signal when other fluorophores such as ,N-ethenoadenine, 2-aminopurine and other tryptohan residues are used to probe the protein’s activiies.. Replacement of the wild type tryptophans with onfluorescent residues is not trivial because one ryptophan is highly conserved and the C-terminal omain functions in both DNA binding as well as inerfilament protein–protein contact.. We undertook the ask of creating a tryptophanless RecA protein with T RecA activity by selecting suitable amino acid relacements for Trp290 and Trp308. Clone Assay:Article Title: Design and evaluation of a tryptophanless RecA protein with wild type activity. Article Snippet: f t f b R o t o t a d a I f ( p i N R o e R t t t The C-terminal domain of the Escherichia coli RecA rotein contains two tryptophan residues whose naive fluorescence emission provides an interfering ackground signal when other fluorophores such as ,N-ethenoadenine, 2-aminopurine and other tryptohan residues are used to probe the protein’s activiies.. Replacement of the wild type tryptophans with onfluorescent residues is not trivial because one ryptophan is highly conserved and the C-terminal omain functions in both DNA binding as well as inerfilament protein–protein contact.. We undertook the ask of creating a tryptophanless RecA protein with T RecA activity by selecting suitable amino acid relacements for Trp290 and Trp308. |