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Sangon Biotech codon optimized gene sequence
Codon Optimized Gene Sequence, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/codon+optimization/gene+sequence/pm42296048-193-1-11
Average 86 stars, based on 1 article reviews
codon optimized gene sequence - by Bioz Stars, 2026-11
86/100 stars

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Related Articles

Sequencing:

Article Title: Development of a novel high-affinity anti-NGAL monoclonal antibody pair for sensitive detection of acute kidney injury.
Article Snippet: Neutrophil Gelatinase-Associated Lipocalin (NGAL) is an early marker for Acute Kidney Injury (AKI) recommended by the International Society of Nephrology (ISN).. This study obtained recombinant NGAL protein via a prokaryotic expression system.. After immunizing BALB/c mice, four NGAL-specific monoclonal antibodies were screened using hybridoma technology.

Article Title: Molecular chaperone effects on recombinant yield and binding characteristics of an ABA-specific scFv in Escherichia coli
Article Snippet: The E. coli strain BL21 (DE3) was purchased from Sangon Biotech (China). .. The ABA-scFv gene sequence, referenced from , was synthesized by Sangon Biotech and cloned into the pET30a vector to create the expression plasmid pET30a-ABA-scFv . .. To establish the chaperone co-expression systems, BL21 (DE3) competent cells were first transformed with one of five molecular chaperone plasmids: pG-KJE8 , pGro7 , pKJE7 , pG-Tf2 , or pTf16 (Takara, Japan), as detailed in .

Article Title: A genetically programmable, conjugation-free nanomedicine platform for modular antibody-guided drug delivery
Article Snippet: .. The scFv-ALB fusion gene sequence was synthesized by Sangon Biotech and subcloned into the mammalian expression vector pX17.4 to construct the recombinant plasmid pX17.4-scFv-ALB (αHER2). ..

Article Title: Development of a Highly Sensitive ELISA for Detecting Antibodies Against a Novel Variant Avian Reovirus Based on Dual σC and σB Antigens.
Article Snippet: .. Based on the nucleotide sequence of the LY383 strain (GenBank accession number: AWV55509), the σC and σB gene sequences were synthesized by Sangon Biotech (Shanghai, China) and subsequently cloned into the pMD19T vector (Takara, Kyoto, Japan). ..

Article Title: Production method of recombinant
Article Snippet: .. Strain and Plasmid Used in the Present Invention For genes of the 7β-HSDH and the GDH, Sangon Biotech (Shanghai) Co., Ltd. performs a codon optimization and a complete gene synthesis on a gene sequence according to codon bias of E. coli. .. An E. coli BL21(DE3) strain is purchased from Sangon Biotech (Shanghai) Co., Ltd.

Article Title: An Autocatalytic Molecular Sensor Enables Rapid, Sensitive, and One-Pot Detection of Nucleic Acids.
Article Snippet: Circulating nucleic acids are emerging disease markers whose clinical applications are hindered by the lack of rapid, sensitive, convenient, and cost-effective detection assays.. Inspired by the natural replication of virus, here, we developed a biomimetic one-step, one-pot, isothermal detection assay named RAPID to realize rapid and sensitive detection of nucleic acids with minimal reliance on instruments.. The core element of RAPID is an autocatalytic molecular sensor that exploits the viral replication endonuclease of duck circovirus (i.e., DCV) to transform rolling circle amplification (RCA) from linear to exponential.

Article Title: High-level expression of Pandalus borealis duplex-specific nuclease by Komagataella phaffii via promoter and peptide selection
Article Snippet: Duplex-specific nuclease (DSN) is a necessary component to digest double-stranded DNA (dsDNA) and DNA in DNA-RNA hybrid duplexes specifically, and widely used in food analysis and biological sample treatment.. However, few cases were reported to produce DSN harnessing genetic engineering, which limited the application and pushed up the cost of DSN.. In this study, Pandalus borealis DSN gene was expressed by the famous microbial host, Komagataella phaffii, through three steps including promoter and signal peptide selection, DSN gene expression cassette increasing, cultivation optimization to reach 2.6 × 105 U/μL in fermentation broth.

Synthesized:

Article Title: Development of a novel high-affinity anti-NGAL monoclonal antibody pair for sensitive detection of acute kidney injury.
Article Snippet: Neutrophil Gelatinase-Associated Lipocalin (NGAL) is an early marker for Acute Kidney Injury (AKI) recommended by the International Society of Nephrology (ISN).. This study obtained recombinant NGAL protein via a prokaryotic expression system.. After immunizing BALB/c mice, four NGAL-specific monoclonal antibodies were screened using hybridoma technology.

Article Title: Molecular chaperone effects on recombinant yield and binding characteristics of an ABA-specific scFv in Escherichia coli
Article Snippet: The E. coli strain BL21 (DE3) was purchased from Sangon Biotech (China). .. The ABA-scFv gene sequence, referenced from , was synthesized by Sangon Biotech and cloned into the pET30a vector to create the expression plasmid pET30a-ABA-scFv . .. To establish the chaperone co-expression systems, BL21 (DE3) competent cells were first transformed with one of five molecular chaperone plasmids: pG-KJE8 , pGro7 , pKJE7 , pG-Tf2 , or pTf16 (Takara, Japan), as detailed in .

Article Title: A genetically programmable, conjugation-free nanomedicine platform for modular antibody-guided drug delivery
Article Snippet: .. The scFv-ALB fusion gene sequence was synthesized by Sangon Biotech and subcloned into the mammalian expression vector pX17.4 to construct the recombinant plasmid pX17.4-scFv-ALB (αHER2). ..

Article Title: Development of a Highly Sensitive ELISA for Detecting Antibodies Against a Novel Variant Avian Reovirus Based on Dual σC and σB Antigens.
Article Snippet: .. Based on the nucleotide sequence of the LY383 strain (GenBank accession number: AWV55509), the σC and σB gene sequences were synthesized by Sangon Biotech (Shanghai, China) and subsequently cloned into the pMD19T vector (Takara, Kyoto, Japan). ..

Article Title: An Autocatalytic Molecular Sensor Enables Rapid, Sensitive, and One-Pot Detection of Nucleic Acids.
Article Snippet: Circulating nucleic acids are emerging disease markers whose clinical applications are hindered by the lack of rapid, sensitive, convenient, and cost-effective detection assays.. Inspired by the natural replication of virus, here, we developed a biomimetic one-step, one-pot, isothermal detection assay named RAPID to realize rapid and sensitive detection of nucleic acids with minimal reliance on instruments.. The core element of RAPID is an autocatalytic molecular sensor that exploits the viral replication endonuclease of duck circovirus (i.e., DCV) to transform rolling circle amplification (RCA) from linear to exponential.

Article Title: High-level expression of Pandalus borealis duplex-specific nuclease by Komagataella phaffii via promoter and peptide selection
Article Snippet: Duplex-specific nuclease (DSN) is a necessary component to digest double-stranded DNA (dsDNA) and DNA in DNA-RNA hybrid duplexes specifically, and widely used in food analysis and biological sample treatment.. However, few cases were reported to produce DSN harnessing genetic engineering, which limited the application and pushed up the cost of DSN.. In this study, Pandalus borealis DSN gene was expressed by the famous microbial host, Komagataella phaffii, through three steps including promoter and signal peptide selection, DSN gene expression cassette increasing, cultivation optimization to reach 2.6 × 105 U/μL in fermentation broth.

other:

Article Title: Self-Assembled Nanoparticles with Kynureninase-Fc Fusion Protein and Pheophorbide A for Photodynamic Immunometabolic Cancer Therapy.
Article Snippet: The sequence of the gene was custom-synthesized by Sangon Biotech Co., Ltd. (Shanghai, China).

Clone Assay:

Article Title: Molecular chaperone effects on recombinant yield and binding characteristics of an ABA-specific scFv in Escherichia coli
Article Snippet: The E. coli strain BL21 (DE3) was purchased from Sangon Biotech (China). .. The ABA-scFv gene sequence, referenced from , was synthesized by Sangon Biotech and cloned into the pET30a vector to create the expression plasmid pET30a-ABA-scFv . .. To establish the chaperone co-expression systems, BL21 (DE3) competent cells were first transformed with one of five molecular chaperone plasmids: pG-KJE8 , pGro7 , pKJE7 , pG-Tf2 , or pTf16 (Takara, Japan), as detailed in .

Article Title: Development of a Highly Sensitive ELISA for Detecting Antibodies Against a Novel Variant Avian Reovirus Based on Dual σC and σB Antigens.
Article Snippet: .. Based on the nucleotide sequence of the LY383 strain (GenBank accession number: AWV55509), the σC and σB gene sequences were synthesized by Sangon Biotech (Shanghai, China) and subsequently cloned into the pMD19T vector (Takara, Kyoto, Japan). ..

Article Title: An Autocatalytic Molecular Sensor Enables Rapid, Sensitive, and One-Pot Detection of Nucleic Acids.
Article Snippet: Circulating nucleic acids are emerging disease markers whose clinical applications are hindered by the lack of rapid, sensitive, convenient, and cost-effective detection assays.. Inspired by the natural replication of virus, here, we developed a biomimetic one-step, one-pot, isothermal detection assay named RAPID to realize rapid and sensitive detection of nucleic acids with minimal reliance on instruments.. The core element of RAPID is an autocatalytic molecular sensor that exploits the viral replication endonuclease of duck circovirus (i.e., DCV) to transform rolling circle amplification (RCA) from linear to exponential.

Plasmid Preparation:

Article Title: Molecular chaperone effects on recombinant yield and binding characteristics of an ABA-specific scFv in Escherichia coli
Article Snippet: The E. coli strain BL21 (DE3) was purchased from Sangon Biotech (China). .. The ABA-scFv gene sequence, referenced from , was synthesized by Sangon Biotech and cloned into the pET30a vector to create the expression plasmid pET30a-ABA-scFv . .. To establish the chaperone co-expression systems, BL21 (DE3) competent cells were first transformed with one of five molecular chaperone plasmids: pG-KJE8 , pGro7 , pKJE7 , pG-Tf2 , or pTf16 (Takara, Japan), as detailed in .

Article Title: A genetically programmable, conjugation-free nanomedicine platform for modular antibody-guided drug delivery
Article Snippet: .. The scFv-ALB fusion gene sequence was synthesized by Sangon Biotech and subcloned into the mammalian expression vector pX17.4 to construct the recombinant plasmid pX17.4-scFv-ALB (αHER2). ..

Article Title: Production method of recombinant
Article Snippet: .. Strain and Plasmid Used in the Present Invention For genes of the 7β-HSDH and the GDH, Sangon Biotech (Shanghai) Co., Ltd. performs a codon optimization and a complete gene synthesis on a gene sequence according to codon bias of E. coli. .. An E. coli BL21(DE3) strain is purchased from Sangon Biotech (Shanghai) Co., Ltd.

Expressing:

Article Title: Molecular chaperone effects on recombinant yield and binding characteristics of an ABA-specific scFv in Escherichia coli
Article Snippet: The E. coli strain BL21 (DE3) was purchased from Sangon Biotech (China). .. The ABA-scFv gene sequence, referenced from , was synthesized by Sangon Biotech and cloned into the pET30a vector to create the expression plasmid pET30a-ABA-scFv . .. To establish the chaperone co-expression systems, BL21 (DE3) competent cells were first transformed with one of five molecular chaperone plasmids: pG-KJE8 , pGro7 , pKJE7 , pG-Tf2 , or pTf16 (Takara, Japan), as detailed in .

Article Title: A genetically programmable, conjugation-free nanomedicine platform for modular antibody-guided drug delivery
Article Snippet: .. The scFv-ALB fusion gene sequence was synthesized by Sangon Biotech and subcloned into the mammalian expression vector pX17.4 to construct the recombinant plasmid pX17.4-scFv-ALB (αHER2). ..

Construct:

Article Title: A genetically programmable, conjugation-free nanomedicine platform for modular antibody-guided drug delivery
Article Snippet: .. The scFv-ALB fusion gene sequence was synthesized by Sangon Biotech and subcloned into the mammalian expression vector pX17.4 to construct the recombinant plasmid pX17.4-scFv-ALB (αHER2). ..

Recombinant:

Article Title: A genetically programmable, conjugation-free nanomedicine platform for modular antibody-guided drug delivery
Article Snippet: .. The scFv-ALB fusion gene sequence was synthesized by Sangon Biotech and subcloned into the mammalian expression vector pX17.4 to construct the recombinant plasmid pX17.4-scFv-ALB (αHER2). ..

Derivative Assay:

Article Title: An Autocatalytic Molecular Sensor Enables Rapid, Sensitive, and One-Pot Detection of Nucleic Acids.
Article Snippet: Circulating nucleic acids are emerging disease markers whose clinical applications are hindered by the lack of rapid, sensitive, convenient, and cost-effective detection assays.. Inspired by the natural replication of virus, here, we developed a biomimetic one-step, one-pot, isothermal detection assay named RAPID to realize rapid and sensitive detection of nucleic acids with minimal reliance on instruments.. The core element of RAPID is an autocatalytic molecular sensor that exploits the viral replication endonuclease of duck circovirus (i.e., DCV) to transform rolling circle amplification (RCA) from linear to exponential.



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Image Search Results


Journal: bioRxiv

Article Title: Synthetic biology-guided modular engineering of the secreted cutinase Fo Cut5a with a carbohydrate-binding module improves poly(ester-urethane) depolymerization in Yarrowia lipolytica

doi: 10.64898/2026.10.15.759203

Figure Lengend Snippet: Modular components used to construct the FoCut5a fusion library. The table lists the four signal peptides, four interdomain linkers, and six substrate-binding domains (SBDs) combined in this study, together with their source organisms and amino acid sequences. The catalytic module, FoCut5a, was common to all 96 possible module combinations generated in the library. Signal peptides were included to direct protein secretion in Y. lipolytica, whereas linkers and SBDs were selected to modulate domain spacing and substrate-binding properties, respectively. All SBDs were fused to a common C-terminal V5-His₆ tag (GKPIPNPLLGLDSTRTGHHHHHH). Amino acid sequences are reported using the standard one-letter code.

Article Snippet: The four esterases ( Fo Cut5a, Da PUase, Se1JFR, and Apar EST) and six SBDs were obtained as Y. lipolytica codon-optimized synthetic DNA fragments (Twist Bioscience, USA).

Techniques: Construct, Generated

Selection of a secreted esterase in Y. lipolytica . (a) Schematic representation of the integration cassette containing promoter (pTEF1), a signal peptide (SigPep), the esterase coding sequence, terminator (tLIP2), and auxotrophic marker (URA3). The expression cassette is flanked by homology arms for site-specific integration into the F11 locus (IntF11 Up and IntF11 Rev) and by NotI restriction sites, which are used to linearize the cassette prior to transformation. Four esterases ( Fo Cut5a, Da PUase, Se1JFR, and Apar EST) were each combined with four candidate signal peptides (SigPep1-SigPep4; teal), generating four secretion variants per esterase. (b) Esterase activity in culture supernatants of individual transformants, quantified by p -nitrophenyl butyrate ( p NPB) hydrolysis and expressed as mU/mL, where 1 mU corresponds to the release of 1 nmol of p -nitrophenol ( p NP) per minute. Each dot represents an independent transformant and corresponds to the mean of two technical replicates (n = 12 transformants for Fo Cut5a, Da PUase and Se1JFR; n = 11 for Apar EST). Boxes indicate the interquartile range (IQR) with the median shown as a horizontal line; whiskers extend to 1.5 × IQR, and dots represent individual transformants. Statistical significance was assessed by two-sided Mann-Whitney U tests comparing Fo Cut5a with each of the other esterases, followed by Holm correction for multiple testing ( Fo Cut5a vs Da PUase: adjusted P = 0.068; vs Se1JFR: adjusted P = 0.091; vs Apar EST: adjusted P = 0.091).

Journal: bioRxiv

Article Title: Synthetic biology-guided modular engineering of the secreted cutinase Fo Cut5a with a carbohydrate-binding module improves poly(ester-urethane) depolymerization in Yarrowia lipolytica

doi: 10.64898/2026.10.15.759203

Figure Lengend Snippet: Selection of a secreted esterase in Y. lipolytica . (a) Schematic representation of the integration cassette containing promoter (pTEF1), a signal peptide (SigPep), the esterase coding sequence, terminator (tLIP2), and auxotrophic marker (URA3). The expression cassette is flanked by homology arms for site-specific integration into the F11 locus (IntF11 Up and IntF11 Rev) and by NotI restriction sites, which are used to linearize the cassette prior to transformation. Four esterases ( Fo Cut5a, Da PUase, Se1JFR, and Apar EST) were each combined with four candidate signal peptides (SigPep1-SigPep4; teal), generating four secretion variants per esterase. (b) Esterase activity in culture supernatants of individual transformants, quantified by p -nitrophenyl butyrate ( p NPB) hydrolysis and expressed as mU/mL, where 1 mU corresponds to the release of 1 nmol of p -nitrophenol ( p NP) per minute. Each dot represents an independent transformant and corresponds to the mean of two technical replicates (n = 12 transformants for Fo Cut5a, Da PUase and Se1JFR; n = 11 for Apar EST). Boxes indicate the interquartile range (IQR) with the median shown as a horizontal line; whiskers extend to 1.5 × IQR, and dots represent individual transformants. Statistical significance was assessed by two-sided Mann-Whitney U tests comparing Fo Cut5a with each of the other esterases, followed by Holm correction for multiple testing ( Fo Cut5a vs Da PUase: adjusted P = 0.068; vs Se1JFR: adjusted P = 0.091; vs Apar EST: adjusted P = 0.091).

Article Snippet: The four esterases ( Fo Cut5a, Da PUase, Se1JFR, and Apar EST) and six SBDs were obtained as Y. lipolytica codon-optimized synthetic DNA fragments (Twist Bioscience, USA).

Techniques: Selection, Sequencing, Marker, Expressing, Transformation Assay, Activity Assay, MANN-WHITNEY

(a,b) Release of poly(ester-urethane)-derived monomers from Impranil DLN-SD by Y. lipolytica strain YM4B5105 expressing Fo Cut5a. (a) Accumulation of adipic acid (blue) and neopentyl glycol (mauve), and (b) 1,6-hexanediol (violet) and 6-hydroxycaproate (teal), quantified by LC-MS after 0, 7, 24, 72, and 144 h of cultivation on 1% Impranil DLN-SD. Data points represent the mean of 2-5 independent measurements (n varied depending on the analyte and time point), and error bars indicate the standard error of the mean (SEM). (c) Proposed structure of Impranil DLN-SD, consisting of alternating polyester soft segments (y) and urethane hard segments (x) repeated along the poly(ester-urethane) chain (z). Monomeric units are colour-coded as in panels a and b; hexamethylene diisocyanate (amber) was not detected among the degradation products. Ester bonds (red) indicate the Fo Cut5a cleavage sites (arrows), releasing adipic acid, 1,6-hexanediol, and neopentyl glycol. The diol connecting soft and hard segments remains linked to the hard segment because it is flanked by an ester bond and a urethane bond. No carbamate bond hydrolysis was observed, consistent with the absence of hexamethylene diisocyanate in the culture supernatant. (d) Proposed metabolic conversion of 1,6-hexanediol to 6-hydroxycaproate via the intermediate 6-hydroxyhexanal.

Journal: bioRxiv

Article Title: Synthetic biology-guided modular engineering of the secreted cutinase Fo Cut5a with a carbohydrate-binding module improves poly(ester-urethane) depolymerization in Yarrowia lipolytica

doi: 10.64898/2026.10.15.759203

Figure Lengend Snippet: (a,b) Release of poly(ester-urethane)-derived monomers from Impranil DLN-SD by Y. lipolytica strain YM4B5105 expressing Fo Cut5a. (a) Accumulation of adipic acid (blue) and neopentyl glycol (mauve), and (b) 1,6-hexanediol (violet) and 6-hydroxycaproate (teal), quantified by LC-MS after 0, 7, 24, 72, and 144 h of cultivation on 1% Impranil DLN-SD. Data points represent the mean of 2-5 independent measurements (n varied depending on the analyte and time point), and error bars indicate the standard error of the mean (SEM). (c) Proposed structure of Impranil DLN-SD, consisting of alternating polyester soft segments (y) and urethane hard segments (x) repeated along the poly(ester-urethane) chain (z). Monomeric units are colour-coded as in panels a and b; hexamethylene diisocyanate (amber) was not detected among the degradation products. Ester bonds (red) indicate the Fo Cut5a cleavage sites (arrows), releasing adipic acid, 1,6-hexanediol, and neopentyl glycol. The diol connecting soft and hard segments remains linked to the hard segment because it is flanked by an ester bond and a urethane bond. No carbamate bond hydrolysis was observed, consistent with the absence of hexamethylene diisocyanate in the culture supernatant. (d) Proposed metabolic conversion of 1,6-hexanediol to 6-hydroxycaproate via the intermediate 6-hydroxyhexanal.

Article Snippet: The four esterases ( Fo Cut5a, Da PUase, Se1JFR, and Apar EST) and six SBDs were obtained as Y. lipolytica codon-optimized synthetic DNA fragments (Twist Bioscience, USA).

Techniques: Derivative Assay, Expressing, Liquid Chromatography with Mass Spectroscopy

Polyurethane degradation products released by engineered and control strains. Y. lipolytica strains were cultivated in YNB supplemented with 1% Impranil DLN-SD, and the concentrations of adipic acid (a) and 6-hydroxycaproate (b) in culture supernatants were monitored by HPLC over 144 h. The empty-backbone control strain YM4B5102 is shown in grey, while engineered strains YM4B5105, YM4B5106, YM4B5107, and YM4B5108 are shown in dark red, purple, green, and blue, respectively. Data points represent the mean of 2-5 independent measurements (n varied depending on the analyte and time point), and error bars indicate the standard error of the mean (SEM).

Journal: bioRxiv

Article Title: Synthetic biology-guided modular engineering of the secreted cutinase Fo Cut5a with a carbohydrate-binding module improves poly(ester-urethane) depolymerization in Yarrowia lipolytica

doi: 10.64898/2026.10.15.759203

Figure Lengend Snippet: Polyurethane degradation products released by engineered and control strains. Y. lipolytica strains were cultivated in YNB supplemented with 1% Impranil DLN-SD, and the concentrations of adipic acid (a) and 6-hydroxycaproate (b) in culture supernatants were monitored by HPLC over 144 h. The empty-backbone control strain YM4B5102 is shown in grey, while engineered strains YM4B5105, YM4B5106, YM4B5107, and YM4B5108 are shown in dark red, purple, green, and blue, respectively. Data points represent the mean of 2-5 independent measurements (n varied depending on the analyte and time point), and error bars indicate the standard error of the mean (SEM).

Article Snippet: The four esterases ( Fo Cut5a, Da PUase, Se1JFR, and Apar EST) and six SBDs were obtained as Y. lipolytica codon-optimized synthetic DNA fragments (Twist Bioscience, USA).

Techniques: Control