Structured Review

Bio-Rad high performance liquid chromatography
High Performance Liquid Chromatography, supplied by Bio-Rad, 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/result/high performance liquid chromatography/product/Bio-Rad
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
high performance liquid chromatography - by Bioz Stars, 2021-09
86/100 stars

Images

Related Articles

High Performance Liquid Chromatography:

Article Title: Responses to Low- and High-Intensity Exercise in Adolescents with Type 1 Diabetes in Relation to Their Level of VO2 Max
Article Snippet: .. HbA1c was determined by high-performance liquid chromatography (HPLC) using the Bio-Rad VARIANT™ HbA1c Program (Bio-Rad Laboratories, Inc., Hercules, CA, USA), with its values represented as percentages. ..

Article Title: Association of time in range, as assessed by continuous glucose monitoring, with painful diabetic polyneuropathy
Article Snippet: .. HbA1c levels were measured by high‐performance liquid chromatography with a VARIANT II Hemoglobin A1c analyzer (Bio‐Rad Laboratories, Hercules, CA, USA). ..

Article Title: Quantification of All-Trans Retinoic Acid by Liquid Chromatography–Tandem Mass Spectrometry and Association with Lipid Profile in Patients with Type 2 Diabetes
Article Snippet: .. HbA1c quantification was performed on whole-blood EDTA samples, and analyses were executed using a VARIANT II HbA1c analyzer (BioRad, Hercules, CA, USA) that utilizes cation-exchange high-performance liquid chromatography. ..

Article Title: Deciphering CT texture features of human visceral fat to evaluate metabolic disorders and surgery-induced weight loss effects
Article Snippet: .. Glycosylated hemoglobin (HbA1c) was measured by high-pressure liquid chromatography using the VARIANT II Glycohemoglobin Testing System (Bio-Rad Laboratories, Hercules, CA, USA). ..

Article Title: Increased Serum GDF15 Related to Improvement in Metabolism by Lifestyle Intervention Among Young Overweight and Obese Adults
Article Snippet: .. HbA1c was measured by using high-performance liquid chromatography with a VARIANT II Hemoglobin A1c analyzer (Bio-Rad Laboratories, Hercules, CA). ..

Variant Assay:

Article Title: Responses to Low- and High-Intensity Exercise in Adolescents with Type 1 Diabetes in Relation to Their Level of VO2 Max
Article Snippet: .. HbA1c was determined by high-performance liquid chromatography (HPLC) using the Bio-Rad VARIANT™ HbA1c Program (Bio-Rad Laboratories, Inc., Hercules, CA, USA), with its values represented as percentages. ..

Article Title: Association of time in range, as assessed by continuous glucose monitoring, with painful diabetic polyneuropathy
Article Snippet: .. HbA1c levels were measured by high‐performance liquid chromatography with a VARIANT II Hemoglobin A1c analyzer (Bio‐Rad Laboratories, Hercules, CA, USA). ..

Article Title: Glutathione S-Transferase (GSTT1 rs17856199) and Nitric Oxide Synthase (NOS2 rs2297518) Genotype Combination as Potential Oxidative Stress-Related Molecular Markers for Type 2 Diabetes Mellitus
Article Snippet: .. Sample Collection and Biochemical AnalysisVenous blood samples (10 mL) were collected after an overnight fast (10–12 h); 4 mL on EDTA tubes for molecular analysis, 3 mL also on EDTA for glycated hemoglobin A1c (HbA1c) determination (VARIANT II TURBO Hemoglobin Testing System, Bio-Rad, USA), and 3 mL on serum separator tubes for other chemical assays. ..

Article Title: Association of aryl hydrocarbon receptor transactivating activity, a potential biomarker for persistent organic pollutants, with the risk of gestational diabetes mellitus
Article Snippet: .. HbA1c levels were determined at the initial diagnosis of GDM and before delivery by the Variant II HbA1c program (BioRad; Hercules, CA). ..

Article Title: Antioxidants-Related Superoxide Dismutase (SOD), Catalase (CAT), Glutathione Peroxidase (GPX), Glutathione-S-Transferase (GST), and Nitric Oxide Synthase (NOS) Gene Variants Analysis in an Obese Population: A Preliminary Case-Control Study
Article Snippet: .. The former tubes were sent for either the molecular analysis (4 mL) or glycated hemoglobin A1c (HbA1c; 3 mL) determination (VARIANT II TURBO Hb Testing System, Bio-Rad, Hercules, CA, USA). ..

Article Title: Quantification of All-Trans Retinoic Acid by Liquid Chromatography–Tandem Mass Spectrometry and Association with Lipid Profile in Patients with Type 2 Diabetes
Article Snippet: .. HbA1c quantification was performed on whole-blood EDTA samples, and analyses were executed using a VARIANT II HbA1c analyzer (BioRad, Hercules, CA, USA) that utilizes cation-exchange high-performance liquid chromatography. ..

Article Title: Deciphering CT texture features of human visceral fat to evaluate metabolic disorders and surgery-induced weight loss effects
Article Snippet: .. Glycosylated hemoglobin (HbA1c) was measured by high-pressure liquid chromatography using the VARIANT II Glycohemoglobin Testing System (Bio-Rad Laboratories, Hercules, CA, USA). ..

Article Title: Increased Serum GDF15 Related to Improvement in Metabolism by Lifestyle Intervention Among Young Overweight and Obese Adults
Article Snippet: .. HbA1c was measured by using high-performance liquid chromatography with a VARIANT II Hemoglobin A1c analyzer (Bio-Rad Laboratories, Hercules, CA). ..

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 86
    Bio-Rad hba1c
    Plasma APOC3 is a strong predictor of CAD events in subjects with T1DM and is independent of traditional CAD risk factors. HRs for CAD events per 1 SD increase in log fasting plasma TGs or log serum APOC3, as calculated by Cox proportional hazards models (47 subjects with events; 181 total subjects). Also shown are 95% CIs and P values. A total of 47 participants had a primary endpoint CAD event, defined as a first nonfatal myocardial infarction, coronary revascularization, or death from CAD. Model 1 is a model adjusted for age, sex, and diabetes duration. Model 2 is model 1 further adjusted for nonlipid risk factors: <t>HbA1c,</t> systolic and diastolic blood pressure, and current smoking status. Model 3 is model 1 further adjusted for lipid risk factors: LDL-C and HDL-C. Model 4 is model 1 further adjusted for log fasting TGs.
    Hba1c, supplied by Bio-Rad, 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/result/hba1c/product/Bio-Rad
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hba1c - by Bioz Stars, 2021-09
    86/100 stars
      Buy from Supplier

    86
    Bio-Rad hba1c levels
    Age- and sex-adjusted area under the curve for the prediction of abnormal thermal thresholds in at least 1 lower limb according to <t>HbA1c</t> and FPG. AUROC = area under the receiver operating characteristic curve, CI = confidence interval, FPG = fasting plasma glucose, HbA1c = glycated hemoglobin.
    Hba1c Levels, supplied by Bio-Rad, 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/result/hba1c levels/product/Bio-Rad
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hba1c levels - by Bioz Stars, 2021-09
    86/100 stars
      Buy from Supplier

    86
    Bio-Rad western blotting sds page analysis
    The recombinant soluble catalytic domain of APRc displays autoprocessing activity dependent on the catalytic aspartate residue. (A) The soluble catalytic domain (amino acids 87–231) was fused to GST and produced in E. coli . Upon purification, the auto-activation of rGST-APRc 87–231 was performed in vitro in 0.1 M sodium acetate buffer pH 6 at 37°C for 48 h and monitored by <t>SDS-PAGE</t> stained with Coomassie blue. rGST-APRc 87–231 undergoes multi-step auto-activation processing, resulting in the formation of the activated form APRc 105–231 with ∼14.2 kDa (left panel). Mutation of the active site aspartic acid by alanine in this fusion construct [rGST-APRc(D140A) 87–231 ] clearly impaired the auto-catalytic activity of the protease (right panel). (B) Schematic representation of full-length APRc domain organization. APRc is predicted to comprise three transmembrane domains (TM 1–3) at the N terminus and the soluble catalytic domain at the C terminus. The three auto-cleavage sites (shown in A) identified by Edman degradation are highlighted by order of cleavage (1–3). (C) Activity of wt rGST-APRc 87–231 towards oxidized insulin B chain was tested over activation time. Samples from each time point evaluated in panel A were incubated with oxidized insulin B chain. Reaction products were then evaluated by RP-HPLC showing that substrate cleavage (appearance of four major peaks) was concomitant with appearance of the final activation product. T0, T12, T24, T36 and T48, correspond to the different time points of activation (hours) tested, as shown in A. (D) rGST-APRc 87–231 auto-processing ability during expression was evaluated in total lysates of E. coli cells expressing wt rGST-APRc 87–231 or the correspondent active site mutant rGST-APRc(D140A) 87–231 over a time-course of 3 h and subsequently subjected to Western blot analysis with anti-APRc antibody. A band with approximately 15 kDa was only detected for the wt construct. Incubation and expression time course in hours (h) are indicated above gels and the molecular weight markers in kilodaltons (kDa) are shown on the left.
    Western Blotting Sds Page Analysis, supplied by Bio-Rad, 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/result/western blotting sds page analysis/product/Bio-Rad
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    western blotting sds page analysis - by Bioz Stars, 2021-09
    86/100 stars
      Buy from Supplier

    Image Search Results


    Plasma APOC3 is a strong predictor of CAD events in subjects with T1DM and is independent of traditional CAD risk factors. HRs for CAD events per 1 SD increase in log fasting plasma TGs or log serum APOC3, as calculated by Cox proportional hazards models (47 subjects with events; 181 total subjects). Also shown are 95% CIs and P values. A total of 47 participants had a primary endpoint CAD event, defined as a first nonfatal myocardial infarction, coronary revascularization, or death from CAD. Model 1 is a model adjusted for age, sex, and diabetes duration. Model 2 is model 1 further adjusted for nonlipid risk factors: HbA1c, systolic and diastolic blood pressure, and current smoking status. Model 3 is model 1 further adjusted for lipid risk factors: LDL-C and HDL-C. Model 4 is model 1 further adjusted for log fasting TGs.

    Journal: The Journal of Clinical Investigation

    Article Title: Increased apolipoprotein C3 drives cardiovascular risk in type 1 diabetes

    doi: 10.1172/JCI127308

    Figure Lengend Snippet: Plasma APOC3 is a strong predictor of CAD events in subjects with T1DM and is independent of traditional CAD risk factors. HRs for CAD events per 1 SD increase in log fasting plasma TGs or log serum APOC3, as calculated by Cox proportional hazards models (47 subjects with events; 181 total subjects). Also shown are 95% CIs and P values. A total of 47 participants had a primary endpoint CAD event, defined as a first nonfatal myocardial infarction, coronary revascularization, or death from CAD. Model 1 is a model adjusted for age, sex, and diabetes duration. Model 2 is model 1 further adjusted for nonlipid risk factors: HbA1c, systolic and diastolic blood pressure, and current smoking status. Model 3 is model 1 further adjusted for lipid risk factors: LDL-C and HDL-C. Model 4 is model 1 further adjusted for log fasting TGs.

    Article Snippet: HPLC was used to measure HbA1c (Bio-Rad variant).

    Techniques:

    Variation in study variables over the 24-week study window for the mITT population. a Mean HbA1c (%). The analysis excluded measurements obtained > 14 days after treatment cessation and for Week 24 (LOCF), the analysis included measurements obtained ≤14 days after the last dose of study medication. b Mean fasting blood glucose (mmol/l). The analysis excluded measurements obtained > 1 day after treatment cessation. c Mean nocturnal blood glucose (mmol/l). The analysis excluded measurements obtained > 1 day after treatment cessation. d Mean eight-point SMBG (mmol/l). Error bars represent the standard deviation. LOCF, last observation carried forward; SMBG, self-measured blood glucose

    Journal: BMC Endocrine Disorders

    Article Title: A randomised, open-labelstudy of insulin glargine or neutral protamine Hagedorn insulin in Chinese paediatric patients with type 1 diabetes mellitus

    doi: 10.1186/s12902-016-0146-2

    Figure Lengend Snippet: Variation in study variables over the 24-week study window for the mITT population. a Mean HbA1c (%). The analysis excluded measurements obtained > 14 days after treatment cessation and for Week 24 (LOCF), the analysis included measurements obtained ≤14 days after the last dose of study medication. b Mean fasting blood glucose (mmol/l). The analysis excluded measurements obtained > 1 day after treatment cessation. c Mean nocturnal blood glucose (mmol/l). The analysis excluded measurements obtained > 1 day after treatment cessation. d Mean eight-point SMBG (mmol/l). Error bars represent the standard deviation. LOCF, last observation carried forward; SMBG, self-measured blood glucose

    Article Snippet: HbA1c was measured at screening, Week 0, Week 12, and Week 24 at a central laboratory using a high-performance liquid chromatography system (Variant™ II Hemoglobin Testing System, Bio-Rad, Hercules, CA, USA).

    Techniques: Standard Deviation

    Age- and sex-adjusted area under the curve for the prediction of abnormal thermal thresholds in at least 1 lower limb according to HbA1c and FPG. AUROC = area under the receiver operating characteristic curve, CI = confidence interval, FPG = fasting plasma glucose, HbA1c = glycated hemoglobin.

    Journal: Medicine

    Article Title: Association between thermal threshold abnormalities and peripheral artery disease in patients with type 2 diabetes

    doi: 10.1097/MD.0000000000013803

    Figure Lengend Snippet: Age- and sex-adjusted area under the curve for the prediction of abnormal thermal thresholds in at least 1 lower limb according to HbA1c and FPG. AUROC = area under the receiver operating characteristic curve, CI = confidence interval, FPG = fasting plasma glucose, HbA1c = glycated hemoglobin.

    Article Snippet: HbA1c levels were measured using boronate affinity high-performance liquid chromatography (Bio-Rad variant II HbA1c REORDER PACK 1000TEST/PKG, Alfred Nobel Drive Hercules, California, USA).

    Techniques:

    The recombinant soluble catalytic domain of APRc displays autoprocessing activity dependent on the catalytic aspartate residue. (A) The soluble catalytic domain (amino acids 87–231) was fused to GST and produced in E. coli . Upon purification, the auto-activation of rGST-APRc 87–231 was performed in vitro in 0.1 M sodium acetate buffer pH 6 at 37°C for 48 h and monitored by SDS-PAGE stained with Coomassie blue. rGST-APRc 87–231 undergoes multi-step auto-activation processing, resulting in the formation of the activated form APRc 105–231 with ∼14.2 kDa (left panel). Mutation of the active site aspartic acid by alanine in this fusion construct [rGST-APRc(D140A) 87–231 ] clearly impaired the auto-catalytic activity of the protease (right panel). (B) Schematic representation of full-length APRc domain organization. APRc is predicted to comprise three transmembrane domains (TM 1–3) at the N terminus and the soluble catalytic domain at the C terminus. The three auto-cleavage sites (shown in A) identified by Edman degradation are highlighted by order of cleavage (1–3). (C) Activity of wt rGST-APRc 87–231 towards oxidized insulin B chain was tested over activation time. Samples from each time point evaluated in panel A were incubated with oxidized insulin B chain. Reaction products were then evaluated by RP-HPLC showing that substrate cleavage (appearance of four major peaks) was concomitant with appearance of the final activation product. T0, T12, T24, T36 and T48, correspond to the different time points of activation (hours) tested, as shown in A. (D) rGST-APRc 87–231 auto-processing ability during expression was evaluated in total lysates of E. coli cells expressing wt rGST-APRc 87–231 or the correspondent active site mutant rGST-APRc(D140A) 87–231 over a time-course of 3 h and subsequently subjected to Western blot analysis with anti-APRc antibody. A band with approximately 15 kDa was only detected for the wt construct. Incubation and expression time course in hours (h) are indicated above gels and the molecular weight markers in kilodaltons (kDa) are shown on the left.

    Journal: PLoS Pathogens

    Article Title: RC1339/APRc from Rickettsia conorii Is a Novel Aspartic Protease with Properties of Retropepsin-Like Enzymes

    doi: 10.1371/journal.ppat.1004324

    Figure Lengend Snippet: The recombinant soluble catalytic domain of APRc displays autoprocessing activity dependent on the catalytic aspartate residue. (A) The soluble catalytic domain (amino acids 87–231) was fused to GST and produced in E. coli . Upon purification, the auto-activation of rGST-APRc 87–231 was performed in vitro in 0.1 M sodium acetate buffer pH 6 at 37°C for 48 h and monitored by SDS-PAGE stained with Coomassie blue. rGST-APRc 87–231 undergoes multi-step auto-activation processing, resulting in the formation of the activated form APRc 105–231 with ∼14.2 kDa (left panel). Mutation of the active site aspartic acid by alanine in this fusion construct [rGST-APRc(D140A) 87–231 ] clearly impaired the auto-catalytic activity of the protease (right panel). (B) Schematic representation of full-length APRc domain organization. APRc is predicted to comprise three transmembrane domains (TM 1–3) at the N terminus and the soluble catalytic domain at the C terminus. The three auto-cleavage sites (shown in A) identified by Edman degradation are highlighted by order of cleavage (1–3). (C) Activity of wt rGST-APRc 87–231 towards oxidized insulin B chain was tested over activation time. Samples from each time point evaluated in panel A were incubated with oxidized insulin B chain. Reaction products were then evaluated by RP-HPLC showing that substrate cleavage (appearance of four major peaks) was concomitant with appearance of the final activation product. T0, T12, T24, T36 and T48, correspond to the different time points of activation (hours) tested, as shown in A. (D) rGST-APRc 87–231 auto-processing ability during expression was evaluated in total lysates of E. coli cells expressing wt rGST-APRc 87–231 or the correspondent active site mutant rGST-APRc(D140A) 87–231 over a time-course of 3 h and subsequently subjected to Western blot analysis with anti-APRc antibody. A band with approximately 15 kDa was only detected for the wt construct. Incubation and expression time course in hours (h) are indicated above gels and the molecular weight markers in kilodaltons (kDa) are shown on the left.

    Article Snippet: SDS-PAGE and western blotting SDS-PAGE analysis was performed in a Bio-Rad Mini Protean III electrophoresis apparatus using 4–20% or 12.5% polyacrylamide gels.

    Techniques: Recombinant, Activity Assay, Produced, Purification, Activation Assay, In Vitro, SDS Page, Staining, Mutagenesis, Construct, Incubation, High Performance Liquid Chromatography, Expressing, Western Blot, Molecular Weight

    Auto-processing activity of the last intermediate of activation rAPRc 99–231 . (A) The intermediate of activation APRc 99–231 was fused to C-terminal His-tag and produced in E. coli . Upon purification, the auto-activation assays were performed in vitro in 0.1 M sodium acetate buffer pH 6 at 37°C for 48 h and monitored by SDS-PAGE stained with Coomassie blue. rAPRc 99–231 undergoes auto-processing, resulting in the formation of the activated form. (B) Activity of rAPRc 99–231 towards the fluorogenic substrate MCA-Lys-Ala-Leu-Ile-Pro-Ser-Tyr-Lys-Trp-Ser-Lys-DNP was tested over activation time. Substrate cleavage increased with accumulation of the final activation product. The error bars represent standard deviation of the mean. (C) The quaternary configuration of rAPRc 99–231 precursor and activated forms was assessed by incubating the protease with the cross-linker DSS. Both DSS treated and untreated protein samples were subjected to Western blot analysis with anti-APRc antibody. In the presence of the cross-linking agent, a significant proportion of the protein migrated as a dimer, although the monomeric forms and larger aggregates were also observed. The molecular weight markers in kilodaltons (kDa) are shown on the left.

    Journal: PLoS Pathogens

    Article Title: RC1339/APRc from Rickettsia conorii Is a Novel Aspartic Protease with Properties of Retropepsin-Like Enzymes

    doi: 10.1371/journal.ppat.1004324

    Figure Lengend Snippet: Auto-processing activity of the last intermediate of activation rAPRc 99–231 . (A) The intermediate of activation APRc 99–231 was fused to C-terminal His-tag and produced in E. coli . Upon purification, the auto-activation assays were performed in vitro in 0.1 M sodium acetate buffer pH 6 at 37°C for 48 h and monitored by SDS-PAGE stained with Coomassie blue. rAPRc 99–231 undergoes auto-processing, resulting in the formation of the activated form. (B) Activity of rAPRc 99–231 towards the fluorogenic substrate MCA-Lys-Ala-Leu-Ile-Pro-Ser-Tyr-Lys-Trp-Ser-Lys-DNP was tested over activation time. Substrate cleavage increased with accumulation of the final activation product. The error bars represent standard deviation of the mean. (C) The quaternary configuration of rAPRc 99–231 precursor and activated forms was assessed by incubating the protease with the cross-linker DSS. Both DSS treated and untreated protein samples were subjected to Western blot analysis with anti-APRc antibody. In the presence of the cross-linking agent, a significant proportion of the protein migrated as a dimer, although the monomeric forms and larger aggregates were also observed. The molecular weight markers in kilodaltons (kDa) are shown on the left.

    Article Snippet: SDS-PAGE and western blotting SDS-PAGE analysis was performed in a Bio-Rad Mini Protean III electrophoresis apparatus using 4–20% or 12.5% polyacrylamide gels.

    Techniques: Activity Assay, Activation Assay, Produced, Purification, In Vitro, SDS Page, Staining, Standard Deviation, Western Blot, Molecular Weight