aida 2.1 software package (Raytest GmbH)
90
Structured Review
Raytest GmbH
aida 2.1 software package
Aida 2.1 Software Package, supplied by Raytest GmbH, 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/aida+2%2E1+software+package/aida+2+31+software/pm29972788-231-25-29
Average 90 stars, based on 1 article reviews
Aida 2.1 Software Package, supplied by Raytest GmbH, 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/aida+2%2E1+software+package/aida+2+31+software/pm29972788-231-25-29
Average 90 stars, based on 1 article reviews
aida 2.1 software package - by Bioz Stars,
2026-09
90/100 stars
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Activity Assay:Article Title: Molecular Characterization of the Human Cα-formylglycine-generating Enzyme Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12OcatA, C12OsalD, MCIcatB, and SalOH were determined using the Article Title: ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12O catA , C12O salD , MCI catB , and SalOH were determined using the Article Title: Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase. Article Snippet: Activity assays of steroid sulfatase (STS) and arylsulfatase A (ASA) were performed as described earlier (Conary et al., 1986).Western blot signals were quantified using the Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme Article Snippet: Quantification of Western blot signals was performed using Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme* Article Snippet: Quantification of Western blot signals was performed using Article Title: Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals. Article Snippet: In the catalytic center of eukaryotic and prokaryotic sulfatases, a unique amino acid, Ca-formylglycine (FGly), can be found that is essential for enzymatic activity [1–5].. The FGly participates as an aldehyde hydrate in the hydrolysis of sulfate esters according to a novel trans-sulfation ⁄ elimination mechanism [5–9].. The FGly in all eukaryotic and in most prokaryotic sulfatases is post-translationally generated by oxidation of a specific cysteine residue and, in most cases, this oxidation is catalyzed by the recently discovered formylglycine-generating enzyme (FGE), a novel oxygenase with unusual structural and catalytic properties [10–15]. Software:Article Title: Molecular Characterization of the Human Cα-formylglycine-generating Enzyme Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12OcatA, C12OsalD, MCIcatB, and SalOH were determined using the Article Title: ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12O catA , C12O salD , MCI catB , and SalOH were determined using the Article Title: Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase. Article Snippet: Activity assays of steroid sulfatase (STS) and arylsulfatase A (ASA) were performed as described earlier (Conary et al., 1986).Western blot signals were quantified using the Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme Article Snippet: Quantification of Western blot signals was performed using Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme* Article Snippet: Quantification of Western blot signals was performed using Article Title: Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals. Article Snippet: In the catalytic center of eukaryotic and prokaryotic sulfatases, a unique amino acid, Ca-formylglycine (FGly), can be found that is essential for enzymatic activity [1–5].. The FGly participates as an aldehyde hydrate in the hydrolysis of sulfate esters according to a novel trans-sulfation ⁄ elimination mechanism [5–9].. The FGly in all eukaryotic and in most prokaryotic sulfatases is post-translationally generated by oxidation of a specific cysteine residue and, in most cases, this oxidation is catalyzed by the recently discovered formylglycine-generating enzyme (FGE), a novel oxygenase with unusual structural and catalytic properties [10–15]. Western Blot:Article Title: Molecular Characterization of the Human Cα-formylglycine-generating Enzyme Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12OcatA, C12OsalD, MCIcatB, and SalOH were determined using the Article Title: ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12O catA , C12O salD , MCI catB , and SalOH were determined using the Article Title: Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase. Article Snippet: Activity assays of steroid sulfatase (STS) and arylsulfatase A (ASA) were performed as described earlier (Conary et al., 1986).Western blot signals were quantified using the Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme Article Snippet: Quantification of Western blot signals was performed using Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme* Article Snippet: Quantification of Western blot signals was performed using Article Title: Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals. Article Snippet: In the catalytic center of eukaryotic and prokaryotic sulfatases, a unique amino acid, Ca-formylglycine (FGly), can be found that is essential for enzymatic activity [1–5].. The FGly participates as an aldehyde hydrate in the hydrolysis of sulfate esters according to a novel trans-sulfation ⁄ elimination mechanism [5–9].. The FGly in all eukaryotic and in most prokaryotic sulfatases is post-translationally generated by oxidation of a specific cysteine residue and, in most cases, this oxidation is catalyzed by the recently discovered formylglycine-generating enzyme (FGE), a novel oxygenase with unusual structural and catalytic properties [10–15]. Fluorescence:Article Title: Molecular Characterization of the Human Cα-formylglycine-generating Enzyme Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12OcatA, C12OsalD, MCIcatB, and SalOH were determined using the Article Title: ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum Article Snippet: Western blot signals were quantified using the Article Title: A Gene Cluster Involved in Degradation of Substituted Salicylates via ortho Cleavage in Pseudomonas sp. Strain MT1 Encodes Enzymes Specifically Adapted for Transformation of 4-Methylcatechol and 3-Methylmuconate Article Snippet: The fluorescence intensity was integrated, and the relative intensities of the bands corresponding to C12O catA , C12O salD , MCI catB , and SalOH were determined using the Article Title: Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase. Article Snippet: Activity assays of steroid sulfatase (STS) and arylsulfatase A (ASA) were performed as described earlier (Conary et al., 1986).Western blot signals were quantified using the Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme Article Snippet: Quantification of Western blot signals was performed using Article Title: Proprotein Convertases Process and Thereby Inactivate Formylglycine-generating Enzyme* Article Snippet: Quantification of Western blot signals was performed using Article Title: Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals. Article Snippet: In the catalytic center of eukaryotic and prokaryotic sulfatases, a unique amino acid, Ca-formylglycine (FGly), can be found that is essential for enzymatic activity [1–5].. The FGly participates as an aldehyde hydrate in the hydrolysis of sulfate esters according to a novel trans-sulfation ⁄ elimination mechanism [5–9].. The FGly in all eukaryotic and in most prokaryotic sulfatases is post-translationally generated by oxidation of a specific cysteine residue and, in most cases, this oxidation is catalyzed by the recently discovered formylglycine-generating enzyme (FGE), a novel oxygenase with unusual structural and catalytic properties [10–15]. |