p1 coding sequence Search Results


dna sequence coding for the c3 domain of adhesin p1  (GenScript corporation)
90
GenScript corporation dna sequence coding for the c3 domain of adhesin p1
(a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
Dna Sequence Coding For The C3 Domain Of Adhesin P1, 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
https://www.bioz.com/product/p1+coding+sequence/pmc10695118-144-9-27?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
dna sequence coding for the c3 domain of adhesin p1 - by Bioz Stars, 2026-08
90/100 stars
  Buy from Supplier
poly(a) trimmed, oligo(dt) primed, and 5 0 biased random primed reverse-transcription of cdna  (Incyte corporation)
90
Incyte corporation poly(a) trimmed, oligo(dt) primed, and 5 0 biased random primed reverse-transcription of cdna
(a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
Poly(a) Trimmed, Oligo(dt) Primed, And 5 0 Biased Random Primed Reverse Transcription Of Cdna, supplied by Incyte corporation, 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/p1+coding+sequence/pm15321681-43-15-16?v=Incyte+corporation
Average 90 stars, based on 1 article reviews
poly(a) trimmed, oligo(dt) primed, and 5 0 biased random primed reverse-transcription of cdna - by Bioz Stars, 2026-08
90/100 stars
  Buy from Supplier

Image Search Results


(a) Annotated 2D 1H,15N TROSY spectrum of Adhesin P1 C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.

Journal: Biomolecular NMR assignments

Article Title: Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1

doi: 10.1007/s12104-023-10158-y

Figure Lengend Snippet: (a) Annotated 2D 1H,15N TROSY spectrum of Adhesin P1 C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.

Article Snippet: The DNA sequence coding for the C3 domain of adhesin P1 (residues 1328–1490; Uniprot accession number P23504) was synthesized, with codon optimization for E. coli , by Genescript and inserted into pET21a(+) plasmid to yield the pET21a-C3-His 6 plasmid with a C-terminal His tag.

Techniques: Construct, Comparison