bche antibody d 5 Search Results


mouse monoclonal anti bche antibody  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology mouse monoclonal anti bche antibody
Map of gene constructs. (A) pTRBO-prBChE-KDEL, (B) pTRBO-prBChE, and (C) p35S-P19, 35S: Cauliflower Mosaic Virus (CaMV) promotor, RAmy3DSP : rice alpha-amylase 3D gene signal peptide, Replicase : replicase gene of tobacco mosaic virus (TMV), MP : movement protein, <t>BChE</t> : codon optimized sequences for the human butyrylcholinesterase gene. 3XFLAG : specific amino acid codon sequences used for immunodetection and purification of the protein. KDEL : Codons encoding lysine, aspartic acid, glutamic acid, leucine, specifying the endoplamsmic retention sequence. P19: P19 gene from Tomato Bushy Stunt Virus (TBSV).
Mouse Monoclonal Anti Bche Antibody, supplied by Santa Cruz Biotechnology, 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/product/bche+antibody+d+5/pmc04909763-74-26-31?v=Santa+Cruz+Biotechnology
Average 93 stars, based on 1 article reviews
mouse monoclonal anti bche antibody - by Bioz Stars, 2026-07
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Map of gene constructs. (A) pTRBO-prBChE-KDEL, (B) pTRBO-prBChE, and (C) p35S-P19, 35S: Cauliflower Mosaic Virus (CaMV) promotor, RAmy3DSP : rice alpha-amylase 3D gene signal peptide, Replicase : replicase gene of tobacco mosaic virus (TMV), MP : movement protein, BChE : codon optimized sequences for the human butyrylcholinesterase gene. 3XFLAG : specific amino acid codon sequences used for immunodetection and purification of the protein. KDEL : Codons encoding lysine, aspartic acid, glutamic acid, leucine, specifying the endoplamsmic retention sequence. P19: P19 gene from Tomato Bushy Stunt Virus (TBSV).

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: Map of gene constructs. (A) pTRBO-prBChE-KDEL, (B) pTRBO-prBChE, and (C) p35S-P19, 35S: Cauliflower Mosaic Virus (CaMV) promotor, RAmy3DSP : rice alpha-amylase 3D gene signal peptide, Replicase : replicase gene of tobacco mosaic virus (TMV), MP : movement protein, BChE : codon optimized sequences for the human butyrylcholinesterase gene. 3XFLAG : specific amino acid codon sequences used for immunodetection and purification of the protein. KDEL : Codons encoding lysine, aspartic acid, glutamic acid, leucine, specifying the endoplamsmic retention sequence. P19: P19 gene from Tomato Bushy Stunt Virus (TBSV).

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: Construct, Virus, Immunodetection, Purification, Sequencing

(A) SDS-PAGE and (B) Western blot of ER retained and apoplast targeted prBChE protein extracted using different extraction buffers. (A) Coomassie stained gel with 15 mU: lane1: (prBChE-ER pH 4 extract), lane 2: (prBChE-ER pH 8 extract), lane 3 (prBChE pH 4 extract), lane 4 (prBChE pH 8 extract), lane 5: (3 μg of equine BChE control) loaded under non-reduced conditions. Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa. (B) Western blot analysis using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: (A) SDS-PAGE and (B) Western blot of ER retained and apoplast targeted prBChE protein extracted using different extraction buffers. (A) Coomassie stained gel with 15 mU: lane1: (prBChE-ER pH 4 extract), lane 2: (prBChE-ER pH 8 extract), lane 3 (prBChE pH 4 extract), lane 4 (prBChE pH 8 extract), lane 5: (3 μg of equine BChE control) loaded under non-reduced conditions. Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa. (B) Western blot analysis using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: SDS Page, Western Blot, Extraction, Staining, Control, Molecular Weight

(A) SDS-PAGE and (B) Western blot of purified prBChE protein compared to serial dilutions of PEG-rBChE protein control. (A) Coomassie stained gel: lanes 1 and 2 contain duplicate loadings of 7 μg of prBChE protein. Lanes 3 to 6 contain serial dilutions of PEG-rBChE control (lane 3: 1, lane 4: 3, lane 5: 7, and lane 6: 10 μg), all loaded under reduced conditions. Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa. Because the goat recombinant BChE is PEGylated, its monomeric mobility on SDS-PAGE is approximately 200 kDa. However, the unPEGylated goat BChE co-migrates with prBChE as revealed by SDS-PAGE. (B) Western blot analysis using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: (A) SDS-PAGE and (B) Western blot of purified prBChE protein compared to serial dilutions of PEG-rBChE protein control. (A) Coomassie stained gel: lanes 1 and 2 contain duplicate loadings of 7 μg of prBChE protein. Lanes 3 to 6 contain serial dilutions of PEG-rBChE control (lane 3: 1, lane 4: 3, lane 5: 7, and lane 6: 10 μg), all loaded under reduced conditions. Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa. Because the goat recombinant BChE is PEGylated, its monomeric mobility on SDS-PAGE is approximately 200 kDa. However, the unPEGylated goat BChE co-migrates with prBChE as revealed by SDS-PAGE. (B) Western blot analysis using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: SDS Page, Western Blot, Purification, Control, Staining, Molecular Weight, Recombinant

Initial reaction velocity kinetics of BTCh hydrolysis by BChE enzyme. The hydrolysis rate of BTCh substrate was monitored by measuring BChE activity (prBChE vs. human BChE control) over a large substrate concentration (10 μM–7.5 mM) in 0.1 M phosphate buffer pH 7.4, 0.267 mM DNTB.

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: Initial reaction velocity kinetics of BTCh hydrolysis by BChE enzyme. The hydrolysis rate of BTCh substrate was monitored by measuring BChE activity (prBChE vs. human BChE control) over a large substrate concentration (10 μM–7.5 mM) in 0.1 M phosphate buffer pH 7.4, 0.267 mM DNTB.

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: Activity Assay, Control, Concentration Assay

Oligomer distribution analysis by Western blot using (A) non-reducing and (B) reducing conditions SDS-PAGE analysis. Western blot analysis was developed using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody of 0.25 μg of equine BuChE control (lane 1) and 0.25 μg pure prBChE protein (lane 2). Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa.

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: Oligomer distribution analysis by Western blot using (A) non-reducing and (B) reducing conditions SDS-PAGE analysis. Western blot analysis was developed using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody of 0.25 μg of equine BuChE control (lane 1) and 0.25 μg pure prBChE protein (lane 2). Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa.

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: Western Blot, SDS Page, Control, Staining, Molecular Weight

(A) Coomassie stained, (B) Western blot, and (C) activity stained Native gel analysis of prBChE, compared to BChE control. (A,B) Coomassie stained and Western blot 7.5% gel with 3 μg of purified prBChE (lane 3) compared to BChE mammalian serum enzymes (1.5 μg of human protein: lane 1, 3 μg equine protein: lane 2). (C) Activity stained of 0.25 mU pure prBChE (lane 2) and 0.25 mU equine control (lane 1).

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: (A) Coomassie stained, (B) Western blot, and (C) activity stained Native gel analysis of prBChE, compared to BChE control. (A,B) Coomassie stained and Western blot 7.5% gel with 3 μg of purified prBChE (lane 3) compared to BChE mammalian serum enzymes (1.5 μg of human protein: lane 1, 3 μg equine protein: lane 2). (C) Activity stained of 0.25 mU pure prBChE (lane 2) and 0.25 mU equine control (lane 1).

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: Staining, Western Blot, Activity Assay, Control, Purification

(A) Coomassie stained and (B) Western blot of Native gel analysis of denatured prBChE, compared to denatured equine BChE control. (A) Coomassie stained gel, lane 1: 1 μg equine BChE control under native conditions, lane 2: 1 μg of denatured equine BChE control under reducing conditions, lane 3: 1 μg prBChE under native conditions, lane 4: 1 μg of denatured prBChE under reducing conditions. (B) Western blot analysis developed with 0.5 μg equine BChE control and prBChE using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: (A) Coomassie stained and (B) Western blot of Native gel analysis of denatured prBChE, compared to denatured equine BChE control. (A) Coomassie stained gel, lane 1: 1 μg equine BChE control under native conditions, lane 2: 1 μg of denatured equine BChE control under reducing conditions, lane 3: 1 μg prBChE under native conditions, lane 4: 1 μg of denatured prBChE under reducing conditions. (B) Western blot analysis developed with 0.5 μg equine BChE control and prBChE using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: Staining, Western Blot, Control

(A) Western blot analysis of a native gel of crude preparation of prBChE. Western blot analysis was performed using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody of crude extract preparation of 0.25 μg prBChE (lane 3) compared to 0.25 μg of equine control (lane 1) and 0.25 μg pure prBChE protein (lane2). (B) Native gel analysis of different prBChE variants. 45 mU of prBChE-ER (lane 1), prBChE (lane 2), prBChE-AWF (lane 3) and equine control (lane 4) were loaded to a 7.5% gel and stained for BChE activity according to the method of .

Journal: Frontiers in Plant Science

Article Title: Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana

doi: 10.3389/fpls.2016.00743

Figure Lengend Snippet: (A) Western blot analysis of a native gel of crude preparation of prBChE. Western blot analysis was performed using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody of crude extract preparation of 0.25 μg prBChE (lane 3) compared to 0.25 μg of equine control (lane 1) and 0.25 μg pure prBChE protein (lane2). (B) Native gel analysis of different prBChE variants. 45 mU of prBChE-ER (lane 1), prBChE (lane 2), prBChE-AWF (lane 3) and equine control (lane 4) were loaded to a 7.5% gel and stained for BChE activity according to the method of .

Article Snippet: The blots were developed with either 1:2,500 dilution of monoclonal anti-FLAG M2-Peroxidase (HRP) antibody (Sigma–Aldrich, St. Louis, MO, USA) in 5% NFDM solution or with 1:200 mouse monoclonal anti-BChE antibody (D-5; Santa Cruz biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution followed by 1:2000 goat anti-mouse HRP conjugated secondary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) in 5% NFDM solution.

Techniques: Western Blot, Control, Staining, Activity Assay