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human c peptide elisa kit  (R&D Systems)


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    R&D Systems human c peptide elisa kit
    Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain <t>(yellow),</t> <t>C-peptide</t> (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by <t>ELISA,</t> as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).
    Human C Peptide Elisa Kit, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+c+peptide+elisa+kit/bio_rxiv__64898__2026__03__30__715452-194-11-15?v=R%26D+Systems
    Average 94 stars, based on 50 article reviews
    human c peptide elisa kit - by Bioz Stars, 2026-07
    94/100 stars

    Images

    1) Product Images from "BLAST: A blue light-assisted secretion toolkit tunable by reversible protein-protein interactions"

    Article Title: BLAST: A blue light-assisted secretion toolkit tunable by reversible protein-protein interactions

    Journal: bioRxiv

    doi: 10.64898/2026.03.30.715452

    Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain (yellow), C-peptide (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by ELISA, as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).
    Figure Legend Snippet: Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain (yellow), C-peptide (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by ELISA, as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).

    Techniques Used: Construct, Transfection, Enzyme-linked Immunosorbent Assay, Plasmid Preparation



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    Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain <t>(yellow),</t> <t>C-peptide</t> (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by <t>ELISA,</t> as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).
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    Image Search Results


    Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain (yellow), C-peptide (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by ELISA, as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).

    Journal: bioRxiv

    Article Title: BLAST: A blue light-assisted secretion toolkit tunable by reversible protein-protein interactions

    doi: 10.64898/2026.03.30.715452

    Figure Lengend Snippet: Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain (yellow), C-peptide (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by ELISA, as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).

    Article Snippet: Secreted human C-peptide levels in the supernatant were quantified using a Human C-peptide ELISA Kit (R&D Systems; Catalog #DICP00).

    Techniques: Construct, Transfection, Enzyme-linked Immunosorbent Assay, Plasmid Preparation

    Percent change (95% CI) in maternal metabolic composite measures of beta cell function and insulin resistance, including (A) PI:INS ratio, (B) PI:CP ratio, (C) HOMA-IR, (D) TyG index, per doubling of second trimester plasma PFOA, PFOS, PFHxS, PFNA, PFDA, and PFUnDA concentrations. Models were adjusted for maternal age at index pregnancy, pre-pregnancy BMI, race and ethnicity, education at index pregnancy, diet quality assessment score at index pregnancy, and smoking status at follow-up. Abbreviations: CP, C-peptide; HOMA-IR, Homeostatic Model of Insulin Resistance; INS, insulin; PFDA, perfluorodecanoic acid; PFHxS, perfluorohexane sulfonic acid; PFNA, perfluorononanoic acid; PFOA, perfluorooctanoic acid; PFOS, perfluorooctanesulfonic acid; PFUnDA, perfluoroundecanoic acid; PI, proinsulin; TyG, triglyceride-glucose.

    Journal: The Journal of Clinical Endocrinology and Metabolism

    Article Title: Prenatal Concentrations of Perfluoroalkyl Substances and Maternal Beta Cell Function at 7 to 9 Years of Follow-Up

    doi: 10.1210/clinem/dgaf143

    Figure Lengend Snippet: Percent change (95% CI) in maternal metabolic composite measures of beta cell function and insulin resistance, including (A) PI:INS ratio, (B) PI:CP ratio, (C) HOMA-IR, (D) TyG index, per doubling of second trimester plasma PFOA, PFOS, PFHxS, PFNA, PFDA, and PFUnDA concentrations. Models were adjusted for maternal age at index pregnancy, pre-pregnancy BMI, race and ethnicity, education at index pregnancy, diet quality assessment score at index pregnancy, and smoking status at follow-up. Abbreviations: CP, C-peptide; HOMA-IR, Homeostatic Model of Insulin Resistance; INS, insulin; PFDA, perfluorodecanoic acid; PFHxS, perfluorohexane sulfonic acid; PFNA, perfluorononanoic acid; PFOA, perfluorooctanoic acid; PFOS, perfluorooctanesulfonic acid; PFUnDA, perfluoroundecanoic acid; PI, proinsulin; TyG, triglyceride-glucose.

    Article Snippet: C-peptide and mature human insulin concentrations were measured with C-peptide Chemiluminescence ELISA kits (#80-CPTHU-CH01, ALPCO Diagnostics, Salem, New Hampshire; RRID: AB_3665034) and Human Insulin Chemiluminescence ELISA kits (#80-INSHU-CH01, ALPCO Diagnostics, Salem, New Hampshire; RRID: AB_2894946) according to manufacturer's instructions.

    Techniques: Cell Function Assay, Clinical Proteomics

    Percent change (95% CI) in fasted maternal metabolic measures 7 to 9 years later including (A) proinsulin, (B) insulin, (C) C-peptide, (D) HbA1c, (E) fasting glucose per doubling of second trimester plasma PFOA, PFOS, PFHxS, PFNA, PFDA, and PFUnDA concentrations. Models were adjusted for maternal age at index pregnancy, pre-pregnancy BMI, race and ethnicity, education at index pregnancy, diet quality assessment score at index pregnancy, and smoking status at follow-up. Abbreviations: HbA1c, hemoglobin A1c; PFDA, perfluorodecanoic acid; PFHxS, perfluorohexane sulfonic acid; PFNA, perfluorononanoic acid; PFOA, perfluorooctanoic acid; PFOS, perfluorooctanesulfonic acid; PFUnDA, perfluoroundecanoic acid.

    Journal: The Journal of Clinical Endocrinology and Metabolism

    Article Title: Prenatal Concentrations of Perfluoroalkyl Substances and Maternal Beta Cell Function at 7 to 9 Years of Follow-Up

    doi: 10.1210/clinem/dgaf143

    Figure Lengend Snippet: Percent change (95% CI) in fasted maternal metabolic measures 7 to 9 years later including (A) proinsulin, (B) insulin, (C) C-peptide, (D) HbA1c, (E) fasting glucose per doubling of second trimester plasma PFOA, PFOS, PFHxS, PFNA, PFDA, and PFUnDA concentrations. Models were adjusted for maternal age at index pregnancy, pre-pregnancy BMI, race and ethnicity, education at index pregnancy, diet quality assessment score at index pregnancy, and smoking status at follow-up. Abbreviations: HbA1c, hemoglobin A1c; PFDA, perfluorodecanoic acid; PFHxS, perfluorohexane sulfonic acid; PFNA, perfluorononanoic acid; PFOA, perfluorooctanoic acid; PFOS, perfluorooctanesulfonic acid; PFUnDA, perfluoroundecanoic acid.

    Article Snippet: C-peptide and mature human insulin concentrations were measured with C-peptide Chemiluminescence ELISA kits (#80-CPTHU-CH01, ALPCO Diagnostics, Salem, New Hampshire; RRID: AB_3665034) and Human Insulin Chemiluminescence ELISA kits (#80-INSHU-CH01, ALPCO Diagnostics, Salem, New Hampshire; RRID: AB_2894946) according to manufacturer's instructions.

    Techniques: Clinical Proteomics