c321 δa Search Results


strain c321 δa exp  (Addgene inc)
93
Addgene inc strain c321 δa exp
Strain C321 δa Exp, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
strain c321 δa exp - by Bioz Stars, 2026-03
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escherichia coli c321 δprfa gro  (Addgene inc)
93
Addgene inc escherichia coli c321 δprfa gro
(A) Expression yield of PglC (left) or PglA (right) variants normalized to the expression of the corresponding WT protein, in the presence or absence of BCN. Expression was quantified by anti-His western blot. (B) Heatmap representing the amber suppression efficiency at individual sites on PglC (left) and PglA (right) (see Figure S2 for details on the structure prediction). The structure of PglC from C. jejuni was predicted with the online server iTasser using the PglC crystal structure (PDB: 5W7L) from C. concisus as template (Ray et al., 2018; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). The position of PglC with respect to the membrane plane was determined using the server “Orientations of Proteins in Membranes” Lomize et al., 2012). Positions selected for the insertions of non-canonical amino acids were selected based on their position within this predicted structure (surfaced exposed and in a diverse physico-chemical environment) and also based on the alignment of 15,000 sequences (non-conserved residues) Lukose et al., 2015). The structure of PglA from C. jejuni was predicted with the online server iTasser using the structure of the glycosyl transferases WbnH (PDB: 4XYW) from E. coli as the template (Martinez-Fleites et al., 2006; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). Position of PglA with respect to the membrane plane was also determined using the server “Orientations of Proteins in Membranes”. Amber suppression efficiencies were calculated as the difference between the quantity of variant expressed in the presence and absence of BCN, normalized by the quantity of expressed WT protein. See also Tables S2 and S3, and Figure S2.
Escherichia Coli C321 δprfa Gro, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/escherichia coli c321 δprfa gro/product/Addgene inc
Average 93 stars, based on 1 article reviews
escherichia coli c321 δprfa gro - by Bioz Stars, 2026-03
93/100 stars
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c321  (Addgene inc)
93
Addgene inc c321
(A) Expression yield of PglC (left) or PglA (right) variants normalized to the expression of the corresponding WT protein, in the presence or absence of BCN. Expression was quantified by anti-His western blot. (B) Heatmap representing the amber suppression efficiency at individual sites on PglC (left) and PglA (right) (see Figure S2 for details on the structure prediction). The structure of PglC from C. jejuni was predicted with the online server iTasser using the PglC crystal structure (PDB: 5W7L) from C. concisus as template (Ray et al., 2018; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). The position of PglC with respect to the membrane plane was determined using the server “Orientations of Proteins in Membranes” Lomize et al., 2012). Positions selected for the insertions of non-canonical amino acids were selected based on their position within this predicted structure (surfaced exposed and in a diverse physico-chemical environment) and also based on the alignment of 15,000 sequences (non-conserved residues) Lukose et al., 2015). The structure of PglA from C. jejuni was predicted with the online server iTasser using the structure of the glycosyl transferases WbnH (PDB: 4XYW) from E. coli as the template (Martinez-Fleites et al., 2006; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). Position of PglA with respect to the membrane plane was also determined using the server “Orientations of Proteins in Membranes”. Amber suppression efficiencies were calculated as the difference between the quantity of variant expressed in the presence and absence of BCN, normalized by the quantity of expressed WT protein. See also Tables S2 and S3, and Figure S2.
C321, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/c321/product/Addgene inc
Average 93 stars, based on 1 article reviews
c321 - by Bioz Stars, 2026-03
93/100 stars
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cp025268  (Addgene inc)
88
Addgene inc cp025268
(A) Expression yield of PglC (left) or PglA (right) variants normalized to the expression of the corresponding WT protein, in the presence or absence of BCN. Expression was quantified by anti-His western blot. (B) Heatmap representing the amber suppression efficiency at individual sites on PglC (left) and PglA (right) (see Figure S2 for details on the structure prediction). The structure of PglC from C. jejuni was predicted with the online server iTasser using the PglC crystal structure (PDB: 5W7L) from C. concisus as template (Ray et al., 2018; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). The position of PglC with respect to the membrane plane was determined using the server “Orientations of Proteins in Membranes” Lomize et al., 2012). Positions selected for the insertions of non-canonical amino acids were selected based on their position within this predicted structure (surfaced exposed and in a diverse physico-chemical environment) and also based on the alignment of 15,000 sequences (non-conserved residues) Lukose et al., 2015). The structure of PglA from C. jejuni was predicted with the online server iTasser using the structure of the glycosyl transferases WbnH (PDB: 4XYW) from E. coli as the template (Martinez-Fleites et al., 2006; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). Position of PglA with respect to the membrane plane was also determined using the server “Orientations of Proteins in Membranes”. Amber suppression efficiencies were calculated as the difference between the quantity of variant expressed in the presence and absence of BCN, normalized by the quantity of expressed WT protein. See also Tables S2 and S3, and Figure S2.
Cp025268, supplied by Addgene inc, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/cp025268/product/Addgene inc
Average 88 stars, based on 1 article reviews
cp025268 - by Bioz Stars, 2026-03
88/100 stars
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Image Search Results


(A) Expression yield of PglC (left) or PglA (right) variants normalized to the expression of the corresponding WT protein, in the presence or absence of BCN. Expression was quantified by anti-His western blot. (B) Heatmap representing the amber suppression efficiency at individual sites on PglC (left) and PglA (right) (see Figure S2 for details on the structure prediction). The structure of PglC from C. jejuni was predicted with the online server iTasser using the PglC crystal structure (PDB: 5W7L) from C. concisus as template (Ray et al., 2018; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). The position of PglC with respect to the membrane plane was determined using the server “Orientations of Proteins in Membranes” Lomize et al., 2012). Positions selected for the insertions of non-canonical amino acids were selected based on their position within this predicted structure (surfaced exposed and in a diverse physico-chemical environment) and also based on the alignment of 15,000 sequences (non-conserved residues) Lukose et al., 2015). The structure of PglA from C. jejuni was predicted with the online server iTasser using the structure of the glycosyl transferases WbnH (PDB: 4XYW) from E. coli as the template (Martinez-Fleites et al., 2006; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). Position of PglA with respect to the membrane plane was also determined using the server “Orientations of Proteins in Membranes”. Amber suppression efficiencies were calculated as the difference between the quantity of variant expressed in the presence and absence of BCN, normalized by the quantity of expressed WT protein. See also Tables S2 and S3, and Figure S2.

Journal: Cell chemical biology

Article Title: A Strategic Approach for Fluorescence Imaging of Membrane Proteins in a Native-Like Environment

doi: 10.1016/j.chembiol.2019.11.008

Figure Lengend Snippet: (A) Expression yield of PglC (left) or PglA (right) variants normalized to the expression of the corresponding WT protein, in the presence or absence of BCN. Expression was quantified by anti-His western blot. (B) Heatmap representing the amber suppression efficiency at individual sites on PglC (left) and PglA (right) (see Figure S2 for details on the structure prediction). The structure of PglC from C. jejuni was predicted with the online server iTasser using the PglC crystal structure (PDB: 5W7L) from C. concisus as template (Ray et al., 2018; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). The position of PglC with respect to the membrane plane was determined using the server “Orientations of Proteins in Membranes” Lomize et al., 2012). Positions selected for the insertions of non-canonical amino acids were selected based on their position within this predicted structure (surfaced exposed and in a diverse physico-chemical environment) and also based on the alignment of 15,000 sequences (non-conserved residues) Lukose et al., 2015). The structure of PglA from C. jejuni was predicted with the online server iTasser using the structure of the glycosyl transferases WbnH (PDB: 4XYW) from E. coli as the template (Martinez-Fleites et al., 2006; Roy et al., 2010; Yang et al., 2015; Zhang, 2008). Position of PglA with respect to the membrane plane was also determined using the server “Orientations of Proteins in Membranes”. Amber suppression efficiencies were calculated as the difference between the quantity of variant expressed in the presence and absence of BCN, normalized by the quantity of expressed WT protein. See also Tables S2 and S3, and Figure S2.

Article Snippet: Escherichia coli C321.ΔprfA (GRO) , Lajoie et al., 2013 , Addgene bacterial strain #48998.

Techniques: Expressing, Western Blot, Membrane, Variant Assay

KEY RESOURCES TABLE

Journal: Cell chemical biology

Article Title: A Strategic Approach for Fluorescence Imaging of Membrane Proteins in a Native-Like Environment

doi: 10.1016/j.chembiol.2019.11.008

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Escherichia coli C321.ΔprfA (GRO) , Lajoie et al., 2013 , Addgene bacterial strain #48998.

Techniques: Recombinant, Plasmid Preparation, Mutagenesis, Sequencing, Expressing, Software