Review

human duo set elisa kits (R&D Systems)

R&D Systems is a verified supplier

R&D Systems manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

R&D Systems human duo set elisa kits
$Characterization <t>of</t> <t>IL-1α</t> overexpression constructs in Cal27 HNSCC cells. Gene expression (A-C), protein release (D) and protein expression (E-G) of the three IL1A constructs – Full- Length (FL), N-terminal (NT) and C-terminal (CT) in the Cal27 IL-1α-overexpressing cells were analyzed by RT-qPCR, <t>ELISA</t> and Western blot respectively compared to control. GAPDH was used as an endogenous control for PCR analysis (A-C); α-Tubulin was used as the loading control for whole cell lysate and cytoplasmic fraction western blots (E-F); and Lamin B1 was used as the loading control for the nuclear fraction Western blot (G). Bars represent mean ± SEM from n = 3 independent experiments. IL-1α band intensities were normalized to the respective loading controls. ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.$
Human Duo Set Elisa Kits, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 47 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/duo+set+elisas/Human+IL-1ra%2FIL-1F3+DuoSet+ELISA/pmc13122707-57-22-27
Average 94 stars, based on 47 article reviews

human duo set elisa kits - by Bioz Stars, 2026-09

94/100 stars

Images

1) Product Images from "C-terminal interleukin 1 alpha (IL-1α) overexpression drives EMT and a vulnerability to ferroptosis in HNSCC"

Article Title: C-terminal interleukin 1 alpha (IL-1α) overexpression drives EMT and a vulnerability to ferroptosis in HNSCC

Journal: Redox Biology

doi: 10.1016/j.redox.2026.104172

$Characterization of IL-1α overexpression constructs in Cal27 HNSCC cells. Gene expression (A-C), protein release (D) and protein expression (E-G) of the three IL1A constructs – Full- Length (FL), N-terminal (NT) and C-terminal (CT) in the Cal27 IL-1α-overexpressing cells were analyzed by RT-qPCR, ELISA and Western blot respectively compared to control. GAPDH was used as an endogenous control for PCR analysis (A-C); α-Tubulin was used as the loading control for whole cell lysate and cytoplasmic fraction western blots (E-F); and Lamin B1 was used as the loading control for the nuclear fraction Western blot (G). Bars represent mean ± SEM from n = 3 independent experiments. IL-1α band intensities were normalized to the respective loading controls. ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.$
Figure Legend Snippet: Characterization of IL-1α overexpression constructs in Cal27 HNSCC cells. Gene expression (A-C), protein release (D) and protein expression (E-G) of the three IL1A constructs – Full- Length (FL), N-terminal (NT) and C-terminal (CT) in the Cal27 IL-1α-overexpressing cells were analyzed by RT-qPCR, ELISA and Western blot respectively compared to control. GAPDH was used as an endogenous control for PCR analysis (A-C); α-Tubulin was used as the loading control for whole cell lysate and cytoplasmic fraction western blots (E-F); and Lamin B1 was used as the loading control for the nuclear fraction Western blot (G). Bars represent mean ± SEM from n = 3 independent experiments. IL-1α band intensities were normalized to the respective loading controls. ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.

Techniques Used: Over Expression, Construct, Gene Expression, Expressing, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay, Western Blot, Control

IL-1α overexpression alters expression of IL-1 pathway genes. Gene expression of IL1B (A), IL6 (B), IL8 (C), IL1RN (D), IL1RAP (E) and IL1R1 (F) in the three IL1A constructs – Full-Length (FL), N-terminal (NT) and C-terminal (CT) in Cal27 IL-1αoverexpressing cells were analyzed by RT-PCR using GAPDH as an endogenous control. Protein secretion of IL-1β (G), IL-6 (H), IL-8 (I), and IL1RA (J) in cell culture supernatants was quantified by ELISA with protein concentrations normalized to cell numbers. Whole cell lysates were analyzed for IL-1R1 expression by Western blot using GAPDH as a loading control (K). Bars represent mean ± SEM from n = 3 independent experiments.∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.

Figure Legend Snippet: IL-1α overexpression alters expression of IL-1 pathway genes. Gene expression of IL1B (A), IL6 (B), IL8 (C), IL1RN (D), IL1RAP (E) and IL1R1 (F) in the three IL1A constructs – Full-Length (FL), N-terminal (NT) and C-terminal (CT) in Cal27 IL-1αoverexpressing cells were analyzed by RT-PCR using GAPDH as an endogenous control. Protein secretion of IL-1β (G), IL-6 (H), IL-8 (I), and IL1RA (J) in cell culture supernatants was quantified by ELISA with protein concentrations normalized to cell numbers. Whole cell lysates were analyzed for IL-1R1 expression by Western blot using GAPDH as a loading control (K). Bars represent mean ± SEM from n = 3 independent experiments.∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.

Techniques Used: Over Expression, Expressing, Gene Expression, Construct, Reverse Transcription Polymerase Chain Reaction, Control, Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot

other:

Article Title: Deletion of NLRX1 increases fatty acid metabolism and prevents diet-induced hepatic steatosis and metabolic syndrome.
Article Snippet: Leptin, IL-1β and TNF-α were AC C EP TE D M AN U SC R IP T determined by duo set ELISAs (R&D Systems, Abingdon, UK) and performed according to the supplied protocol.

Article Title: NLRX1 Prevents M2 Macrophage Polarization and Excessive Renal Fibrosis in Chronic Obstructive Nephropathy.
Article Snippet: In homogenates and BMDM supernatants TNFα, IL-6 and active TGFβ levels were determined via duo set ELISAs (R&D Systems, Abingdon, UK) performed according to the supplied protocol.

Article Title: De novo hem- and lymphangiogenesis by endothelial progenitor and mesenchymal stem cells in immunocompetent mice.
Article Snippet: the two vessel types, whereas MSCs usually did not incorporate into the vessel wall.. Injections of each separate cell type did not, or hardly, reveal de novo angiogenesis. the release of VeGF-a by MSCs has been shown before, but its inhibitors, e.g., soluble VeGF receptors, have not been studied.. We performed qualitative and quantitative studies of the proteins released by ePCs, MSCs, and cocultures of the cells.

Clinical Proteomics:

Article Title: NLRX1 is not involved in the host defense against Escherichia coli induced pyelonephritis
Article Snippet: Bladder 5% (w/v) and kidney 10% (w/v) tissues from 24h and 48h UTI subjected WT and NLRX1 KO mice were homogenized with a tissue homogenizer (Polytron PT1300D homogenizer, Kinematica AG) in Greenberger lysis buffer (GLB) (300mM NaCl, 30mM Tris, 2mM MgCl 2 , 2mM CaCl 2 , 1% (v/v) Triton X-100, pH set at 7.4, supplemented with Protease Inhibitor Cocktail II (cat no. p8340, Sigma-Aldrich, Sigma-Aldrich, Zwijndrecht, The Netherlands). .. Levels of keratinocyte-derived chemokine (KC), macrophage inflammatory protein-2 (MIP-2), monocyte chemoattractant protein 1 (MCP-1), interleukin 1β (IL1β), interleukin 6 (IL6), tumor necrosis factor alpha (TNFα) and mouse myeloid peroxidase (MPO) were determined in bladder and kidney homogenates and whole blood plasma (KC, TNFα and IL6 only) by duo set ELISAs (cat no. MKC00B, MM200, MJE00, MLB00C, M6000B, MTA00B, DY3667, R&D Systems, Abingdon, UK), performed according to the supplied protocols. .. ELISA data measured in bladder and kidney homogenates was adjusted for total protein concentration as determined by BCA protein assay (cat no. B9643, Sigma-Aldrich, Sigma-Aldrich, Zwijndrecht, The Netherlands) developed with 4% CuSO 4 .

Article Title: NLRX1 is not involved in the host defense against Escherichia coli induced pyelonephritis
Article Snippet: Bladder 5% (w/v) and kidney 10% (w/v) tissues from 24h and 48h UTI subjected WT and NLRX1 KO mice were homogenized with a tissue homogenizer (Polytron PT1300D homogenizer, Kinematica AG) in Greenberger lysis buffer (GLB) (300mM NaCl, 30mM Tris, 2mM MgCl 2 , 2mM CaCl 2 , 1% (v/v) Triton X-100, pH set at 7.4, supplemented with Protease Inhibi- tor Cocktail II (cat no. p8340, Sigma-Aldrich, Sigma-Aldrich, Zwijndrecht, The Netherlands). .. Levels of keratinocyte-derived chemokine (KC), macrophage inflammatory protein-2 (MIP-2), monocyte chemoattractant protein 1 (MCP-1), interleukin 1β (IL1β), interleukin 6 (IL6), tumor necrosis factor alpha (TNFα) and mouse myeloid peroxidase (MPO) were determined in bladder and kidney homogenates and whole blood plasma (KC, TNFα and IL6 only) by duo set ELISAs (cat no. MKC00B, MM200, MJE00, MLB00C, M6000B, MTA00B, DY3667, R&D Systems, Abingdon, UK), performed according to the supplied protocols. .. ELISA data measured in bladder and kidney homogenates was adjusted for total protein concentration as determined by BCA protein assay (cat no. B9643, Sigma-Aldrich, Sigma-Aldrich, Zwijndrecht, The Netherlands) developed with 4% CuSO 4 .

Image Search Results

Journal: Redox Biology

Article Title: C-terminal interleukin 1 alpha (IL-1α) overexpression drives EMT and a vulnerability to ferroptosis in HNSCC

doi: 10.1016/j.redox.2026.104172

Figure Lengend Snippet: Characterization of IL-1α overexpression constructs in Cal27 HNSCC cells. Gene expression (A-C), protein release (D) and protein expression (E-G) of the three IL1A constructs – Full- Length (FL), N-terminal (NT) and C-terminal (CT) in the Cal27 IL-1α-overexpressing cells were analyzed by RT-qPCR, ELISA and Western blot respectively compared to control. GAPDH was used as an endogenous control for PCR analysis (A-C); α-Tubulin was used as the loading control for whole cell lysate and cytoplasmic fraction western blots (E-F); and Lamin B1 was used as the loading control for the nuclear fraction Western blot (G). Bars represent mean ± SEM from n = 3 independent experiments. IL-1α band intensities were normalized to the respective loading controls. ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.

Article Snippet: Cell culture media from IL-1α overexpressed Cal27 cells were collected for analyzing the levels of IL-1α, IL-1β, IL-6, IL-8 or IL-1RA using Human Duo Set ELISA kits (R&D Systems, Minneapolis, MN) according to the manufacturer's protocols.

Techniques: Over Expression, Construct, Gene Expression, Expressing, Quantitative RT-PCR, Enzyme-linked Immunosorbent Assay, Western Blot, Control

Journal: Redox Biology

Article Title: C-terminal interleukin 1 alpha (IL-1α) overexpression drives EMT and a vulnerability to ferroptosis in HNSCC

doi: 10.1016/j.redox.2026.104172

Figure Lengend Snippet: IL-1α overexpression alters expression of IL-1 pathway genes. Gene expression of IL1B (A), IL6 (B), IL8 (C), IL1RN (D), IL1RAP (E) and IL1R1 (F) in the three IL1A constructs – Full-Length (FL), N-terminal (NT) and C-terminal (CT) in Cal27 IL-1αoverexpressing cells were analyzed by RT-PCR using GAPDH as an endogenous control. Protein secretion of IL-1β (G), IL-6 (H), IL-8 (I), and IL1RA (J) in cell culture supernatants was quantified by ELISA with protein concentrations normalized to cell numbers. Whole cell lysates were analyzed for IL-1R1 expression by Western blot using GAPDH as a loading control (K). Bars represent mean ± SEM from n = 3 independent experiments.∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001; ∗∗∗∗p < 0.0001.

Techniques: Over Expression, Expressing, Gene Expression, Construct, Reverse Transcription Polymerase Chain Reaction, Control, Cell Culture, Enzyme-linked Immunosorbent Assay, Western Blot

Panx3 deficiency results in altered glucose metabolism markers. A Serum levels of glucose and insulin in mice of the indicated genotypes at 3, 7 and 14 postoperative days ( N = 6). Relative fold changes to controls were plotted. B Heatmap of 30 differentially regulated genes with highest fold changes in the callus of Panx3 +/+ ( N = 5) and Panx3 −/− ( N = 4) mice 3 days after the osteotomy. Each column represents one individual sample and gene, respectively. Z-scores were calculated based on the expression level of each gene and visualized in a color scale (blue = downregulated, red = upregulated). Genes associated with glucose metabolism were highlighted in red. C Expression of the indicated genes ( Slc = solute carrier family, C1qtnf3 = C1q tumor necrosis factor-related protein 3) in the callus of Panx3 +/+ and Panx3 −/− mice at the indicated postoperatively time points ( N = 6). D Representative alizarin red–stained images of isolated calvarial osteoblasts from Panx3 + / + and Panx3 −/− mice and quantification of extracellular matrix mineralization after 10 days of osteogenic differentiation ( N = 6). E Expression of the indicated genes ( Bglap = bone gamma-carboxylglutamic acid-containing protein, osteocalcin, Dmp1 = dentin matrix acidic matrix phosphoprotein 1, Panx3 = pannexin 3, C1qtnf3 = C1q tumor necrosis factor-related protein 3, Slc = solute carrier) in calvarial osteoblasts from Panx3 + / + and Panx3 −/− mice after 10 days of osteogenic differentiation ( N = 4). Unpaired Student’s t test was used to determine statistical differences between groups at each time point or for each gene. Data are presented as box plots that represent median with minimum and maximum whiskers

Journal: Molecular Medicine

Article Title: Panx3 deficiency in mice impairs bone fracture healing and causes transient hypoglycemia in neonatal animals

doi: 10.1186/s10020-026-01458-9

Figure Lengend Snippet: Panx3 deficiency results in altered glucose metabolism markers. A Serum levels of glucose and insulin in mice of the indicated genotypes at 3, 7 and 14 postoperative days ( N = 6). Relative fold changes to controls were plotted. B Heatmap of 30 differentially regulated genes with highest fold changes in the callus of Panx3 +/+ ( N = 5) and Panx3 −/− ( N = 4) mice 3 days after the osteotomy. Each column represents one individual sample and gene, respectively. Z-scores were calculated based on the expression level of each gene and visualized in a color scale (blue = downregulated, red = upregulated). Genes associated with glucose metabolism were highlighted in red. C Expression of the indicated genes ( Slc = solute carrier family, C1qtnf3 = C1q tumor necrosis factor-related protein 3) in the callus of Panx3 +/+ and Panx3 −/− mice at the indicated postoperatively time points ( N = 6). D Representative alizarin red–stained images of isolated calvarial osteoblasts from Panx3 + / + and Panx3 −/− mice and quantification of extracellular matrix mineralization after 10 days of osteogenic differentiation ( N = 6). E Expression of the indicated genes ( Bglap = bone gamma-carboxylglutamic acid-containing protein, osteocalcin, Dmp1 = dentin matrix acidic matrix phosphoprotein 1, Panx3 = pannexin 3, C1qtnf3 = C1q tumor necrosis factor-related protein 3, Slc = solute carrier) in calvarial osteoblasts from Panx3 + / + and Panx3 −/− mice after 10 days of osteogenic differentiation ( N = 4). Unpaired Student’s t test was used to determine statistical differences between groups at each time point or for each gene. Data are presented as box plots that represent median with minimum and maximum whiskers

Article Snippet: C1qTNF3 duo set ELISA (#DY7925-05, R&D Systems Inc., Minneapolis, USA) was used to determine the concentration in human patients.

Techniques: Expressing, Staining, Isolation

$Panx3 -deficient mice display impaired glucose homeostasis. A Body weight of Panx3 + / + ( N = 4–6) and Panx3 −/− ( N = 3–4) mice and B serum glucose of Panx3 + / + ( N = 6) and Panx3 −/− ( N = 3–5) mice at the indicated ages. C Glucose and D insulin tolerance test of adult mice of the indicated genotypes ( N = 7). Relative alterations to the baseline level were plotted. E Serum levels of insulin and C1qtnf3 in Panx3 + / + and Panx3 −/− mice at the indicated ages ( N = 3 for P3, N = 7 for P600). F Serum concentration of C1qtnf3 in healthy individuals as control ( N = 10), patients displayed adequate fracture healing (Fx, N = 16) and nonunion formation (NU, N = 19). Unpaired Student’s t test was used to determine statistical differences between groups at each time point. Data are presented as box plots that represent median with minimum and maximum whiskers$

Journal: Molecular Medicine

Article Title: Panx3 deficiency in mice impairs bone fracture healing and causes transient hypoglycemia in neonatal animals

doi: 10.1186/s10020-026-01458-9

Figure Lengend Snippet: Panx3 -deficient mice display impaired glucose homeostasis. A Body weight of Panx3 + / + ( N = 4–6) and Panx3 −/− ( N = 3–4) mice and B serum glucose of Panx3 + / + ( N = 6) and Panx3 −/− ( N = 3–5) mice at the indicated ages. C Glucose and D insulin tolerance test of adult mice of the indicated genotypes ( N = 7). Relative alterations to the baseline level were plotted. E Serum levels of insulin and C1qtnf3 in Panx3 + / + and Panx3 −/− mice at the indicated ages ( N = 3 for P3, N = 7 for P600). F Serum concentration of C1qtnf3 in healthy individuals as control ( N = 10), patients displayed adequate fracture healing (Fx, N = 16) and nonunion formation (NU, N = 19). Unpaired Student’s t test was used to determine statistical differences between groups at each time point. Data are presented as box plots that represent median with minimum and maximum whiskers

Article Snippet: C1qTNF3 duo set ELISA (#DY7925-05, R&D Systems Inc., Minneapolis, USA) was used to determine the concentration in human patients.

Techniques: Concentration Assay, Control

Posttraumatic defensive pathway activation and cellular immune response in the murine jejunum. ( A ) Proteome profiler-based pathway analysis revealed activation of immune and defense-related mechanisms. The 15 pathways with the highest degree of regulation are shown. ( B, C ) Histological quantification in jejunal tissue demonstrated a significant increase of CD3 + T lymphocytes in the trauma group relative to controls. ( D ) Gene expression profiling of S100a8 showed a significant post-traumatic upregulation in traumatized mice compared to sham animals. ( E ) In contrast, no statistically significant alteration was observed in interleukin-6 (Il6) expression. ( F ) Plasma levels of C5a were unaltered by traumatic exposure. ( G ) C5a in bronchoalveolar lavage fluid (BALF) was significantly increased in mice 24 h after AT compared to shams. C : n = 180 per group; D-G : n = 4–5 per group. Statistical analysis was performed using the Mann-Whitney U test, with significance defined as p < 0.05. Data are presented as mean ± standard error of the mean (SEM)

Journal: European Journal of Trauma and Emergency Surgery

Article Title: Multifaceted intestinal defense following experimental blunt abdominal trauma

doi: 10.1007/s00068-026-03145-0

Figure Lengend Snippet: Posttraumatic defensive pathway activation and cellular immune response in the murine jejunum. ( A ) Proteome profiler-based pathway analysis revealed activation of immune and defense-related mechanisms. The 15 pathways with the highest degree of regulation are shown. ( B, C ) Histological quantification in jejunal tissue demonstrated a significant increase of CD3 + T lymphocytes in the trauma group relative to controls. ( D ) Gene expression profiling of S100a8 showed a significant post-traumatic upregulation in traumatized mice compared to sham animals. ( E ) In contrast, no statistically significant alteration was observed in interleukin-6 (Il6) expression. ( F ) Plasma levels of C5a were unaltered by traumatic exposure. ( G ) C5a in bronchoalveolar lavage fluid (BALF) was significantly increased in mice 24 h after AT compared to shams. C : n = 180 per group; D-G : n = 4–5 per group. Statistical analysis was performed using the Mann-Whitney U test, with significance defined as p < 0.05. Data are presented as mean ± standard error of the mean (SEM)

Article Snippet: To measure the concentrations of C5a in plasma and BALF, a sandwich ELISA was performed using the C5a ELISA Kit Mouse Duo Set (R&D Systems, Minneapolis, USA).

Techniques: Activation Assay, Gene Expression, Expressing, Clinical Proteomics, MANN-WHITNEY

Review

human duo set elisa kits (R&D Systems)

Structured Review

Images

1) Product Images from "C-terminal interleukin 1 alpha (IL-1α) overexpression drives EMT and a vulnerability to ferroptosis in HNSCC"

Related Articles

other:

Clinical Proteomics:

Similar Products

Image Search Results