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R&D Systems human fgf1 elisa kit

Effect of introducing point mutations on the biological activity of <t>FGF1.</t> a Serum-starved NIH 3T3 cells were treated with 10 ng/mL FGF1 variants for 15 min in the presence of heparin (10 U/mL). Activation of the downstream cascade was detected by immunoblotting using the following antibodies: anti-phospho-FRS2 (pFRS2) and anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2 and anti-vinculin antibodies were used to confirm equal loading. Representative results are shown (n ≥ 3). The vertical lines in the last WB panel show the deleted wells. The original membranes, together with the method of trimming, are presented in Fig. S2. Densitometric analysis of pERK/ERK is presented in Fig. S3. b Effect of 20-h FGF1 variants stimulation (20 ng/mL) in the presence of 10 U/mL heparin on glucose uptake by 3T3-L1 adipocytes. Data are presented as mean ± SEM, n = 4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Human Fgf1 Elisa Kit, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human fgf1 elisa kit - by Bioz Stars, 2026-08

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1) Product Images from "Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes"

Article Title: Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes

Journal: Molecular Biomedicine

doi: 10.1186/s43556-025-00398-w

Effect of introducing point mutations on the biological activity of FGF1. a Serum-starved NIH 3T3 cells were treated with 10 ng/mL FGF1 variants for 15 min in the presence of heparin (10 U/mL). Activation of the downstream cascade was detected by immunoblotting using the following antibodies: anti-phospho-FRS2 (pFRS2) and anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2 and anti-vinculin antibodies were used to confirm equal loading. Representative results are shown (n ≥ 3). The vertical lines in the last WB panel show the deleted wells. The original membranes, together with the method of trimming, are presented in Fig. S2. Densitometric analysis of pERK/ERK is presented in Fig. S3. b Effect of 20-h FGF1 variants stimulation (20 ng/mL) in the presence of 10 U/mL heparin on glucose uptake by 3T3-L1 adipocytes. Data are presented as mean ± SEM, n = 4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Figure Legend Snippet: Effect of introducing point mutations on the biological activity of FGF1. a Serum-starved NIH 3T3 cells were treated with 10 ng/mL FGF1 variants for 15 min in the presence of heparin (10 U/mL). Activation of the downstream cascade was detected by immunoblotting using the following antibodies: anti-phospho-FRS2 (pFRS2) and anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2 and anti-vinculin antibodies were used to confirm equal loading. Representative results are shown (n ≥ 3). The vertical lines in the last WB panel show the deleted wells. The original membranes, together with the method of trimming, are presented in Fig. S2. Densitometric analysis of pERK/ERK is presented in Fig. S3. b Effect of 20-h FGF1 variants stimulation (20 ng/mL) in the presence of 10 U/mL heparin on glucose uptake by 3T3-L1 adipocytes. Data are presented as mean ± SEM, n = 4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Techniques Used: Activity Assay, Activation Assay, Western Blot

Impaired activation of signaling pathways by FGF1 variants due to reduced affinity for the FGFR1 (IIIc) receptor. a Serum-starved NIH 3T3 cells were stimulated with 10 ng/mL FGF1 variants in the presence of heparin (10 U/mL) for 15 min, and activation of downstream signaling cascades was detected by immunoblotting using the following antibodies: anti-phospho-FGFR (pFGFR), anti-phospho-PLCγ (pPLCγ), anti-phosphoFRS2 (pFRS2), anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2, anti-FGFR1, anti-PLCγ and anti-γTubulin antibodies were used to confirm equal loading. Representative results are shown. Densitometric analysis is presented as mean ± SEM, n = 3/4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001. b BLI analysis of the affinity of FGF1 variants for FGFR1-Fc (IIIc isoform). FGFR1-Fc was immobilized on a Protein A sensor and its interactions (association and dissociation) with selected FGF1 mutants were analyzed in the concentration range of 100–800 nM. Curves obtained by global fitting are marked in red. Representative results are shown (n ≥ 3). The equilibrium dissociation constant (K D ) was calculated from the saturation binding curve

Figure Legend Snippet: Impaired activation of signaling pathways by FGF1 variants due to reduced affinity for the FGFR1 (IIIc) receptor. a Serum-starved NIH 3T3 cells were stimulated with 10 ng/mL FGF1 variants in the presence of heparin (10 U/mL) for 15 min, and activation of downstream signaling cascades was detected by immunoblotting using the following antibodies: anti-phospho-FGFR (pFGFR), anti-phospho-PLCγ (pPLCγ), anti-phosphoFRS2 (pFRS2), anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2, anti-FGFR1, anti-PLCγ and anti-γTubulin antibodies were used to confirm equal loading. Representative results are shown. Densitometric analysis is presented as mean ± SEM, n = 3/4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001. b BLI analysis of the affinity of FGF1 variants for FGFR1-Fc (IIIc isoform). FGFR1-Fc was immobilized on a Protein A sensor and its interactions (association and dissociation) with selected FGF1 mutants were analyzed in the concentration range of 100–800 nM. Curves obtained by global fitting are marked in red. Representative results are shown (n ≥ 3). The equilibrium dissociation constant (K D ) was calculated from the saturation binding curve

Techniques Used: Activation Assay, Protein-Protein interactions, Western Blot, Concentration Assay, Binding Assay

Effect of introduced mutations on the long-term activity of FGF1. a Induction of Glut1 expression after stimulation with FGF1 variants. 3T3-L1 cells were treated with 100 ng/mL FGF1 muteins in the presence of 10 U/mL heparin for 24 h, followed by WB analysis with anti-Glut1 and anti-γTubulin antibodies, data are presented as mean ± SEM, n = 6. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001. b Normalized thermal denaturation curves of FGF1 variants monitored by ellipticity changes (λ = 227 nm). c Degradation of FGF1 variants in the presence of adipocytes. Serum-starved 3T3-L1 adipocytes were incubated with 1 µg/mL FGF1 variants. The progress of proteolysis on subsequent days was monitored by immunoblotting with anti-FGF1 antibody. Representative results are shown ( n = 5). Densitometric analysis of proteolysis of FGF1 variants is presented as the ratio the intensity of the upper band to the intensity of the whole amount of protein. Mean ± SEM are shown, n = 5. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Figure Legend Snippet: Effect of introduced mutations on the long-term activity of FGF1. a Induction of Glut1 expression after stimulation with FGF1 variants. 3T3-L1 cells were treated with 100 ng/mL FGF1 muteins in the presence of 10 U/mL heparin for 24 h, followed by WB analysis with anti-Glut1 and anti-γTubulin antibodies, data are presented as mean ± SEM, n = 6. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001. b Normalized thermal denaturation curves of FGF1 variants monitored by ellipticity changes (λ = 227 nm). c Degradation of FGF1 variants in the presence of adipocytes. Serum-starved 3T3-L1 adipocytes were incubated with 1 µg/mL FGF1 variants. The progress of proteolysis on subsequent days was monitored by immunoblotting with anti-FGF1 antibody. Representative results are shown ( n = 5). Densitometric analysis of proteolysis of FGF1 variants is presented as the ratio the intensity of the upper band to the intensity of the whole amount of protein. Mean ± SEM are shown, n = 5. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Techniques Used: Activity Assay, Expressing, Incubation, Western Blot

Mitogenic activity of selected FGF1 variants in different cell types. Mitogenic activity of selected FGF1 variants was assessed by stimulating serum-starved C2C12, MCF7 or 4MBr-5 cells with FGF1 mutants in the concentration range 0.1–100 ng/ml in the presence of 10 U/ml heparin for 48 h, 72 h or 96 h, respectively. Cell viability was assessed by PrestoBlue cell viability assay a or by CellTiter-Fluor cell viability assay b . Cell number was determined by counting NucBlue-stained nuclei using an Opera Phenix Plus High-Content Screening System c . Data are presented as mean ± SEM, n = 3. Multiple t-test; statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Figure Legend Snippet: Mitogenic activity of selected FGF1 variants in different cell types. Mitogenic activity of selected FGF1 variants was assessed by stimulating serum-starved C2C12, MCF7 or 4MBr-5 cells with FGF1 mutants in the concentration range 0.1–100 ng/ml in the presence of 10 U/ml heparin for 48 h, 72 h or 96 h, respectively. Cell viability was assessed by PrestoBlue cell viability assay a or by CellTiter-Fluor cell viability assay b . Cell number was determined by counting NucBlue-stained nuclei using an Opera Phenix Plus High-Content Screening System c . Data are presented as mean ± SEM, n = 3. Multiple t-test; statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Techniques Used: Activity Assay, Concentration Assay, Viability Assay, Staining, High Content Screening

Metabolic activity of FGF1 variants in vivo. a , b Change in blood glucose levels in db/db mice after a single administration of FGF1 variants (measurements at 0, 6, 18, 24, 30, 48, 72, 96 and 168 h after protein administration). FGF1 variants were administered at a dose of 1 mg/kg body weight. Data were normalized to glucose levels before protein administration and presented as mean ± SEM, n = 7/6. Statistical significance * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001; (*) indicates comparison with vehicle; (#) indicates comparison with wild-type protein. c Analysis of mouse body weight 96 h after administration. d Pharmacokinetics of FGF1 variants after a single subcutaneous administration in Wistar Han rats. FGF1 variants were administered subcutaneously at a dose 0.5 mg/kg, and blood samples were collected before injection and at 5 min, 15 min, 30 min and 1, 2, 4, 7, 12, 24, 48 h after injection and protein levels were analyzed by ELISA. Data are presented as mean ± SEM, n = 5

Figure Legend Snippet: Metabolic activity of FGF1 variants in vivo. a , b Change in blood glucose levels in db/db mice after a single administration of FGF1 variants (measurements at 0, 6, 18, 24, 30, 48, 72, 96 and 168 h after protein administration). FGF1 variants were administered at a dose of 1 mg/kg body weight. Data were normalized to glucose levels before protein administration and presented as mean ± SEM, n = 7/6. Statistical significance * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001; (*) indicates comparison with vehicle; (#) indicates comparison with wild-type protein. c Analysis of mouse body weight 96 h after administration. d Pharmacokinetics of FGF1 variants after a single subcutaneous administration in Wistar Han rats. FGF1 variants were administered subcutaneously at a dose 0.5 mg/kg, and blood samples were collected before injection and at 5 min, 15 min, 30 min and 1, 2, 4, 7, 12, 24, 48 h after injection and protein levels were analyzed by ELISA. Data are presented as mean ± SEM, n = 5

Techniques Used: Activity Assay, In Vivo, Comparison, Drug discovery, Injection, Enzyme-linked Immunosorbent Assay

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Journal: Molecular Biomedicine

Article Title: Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes

doi: 10.1186/s43556-025-00398-w

Figure Lengend Snippet: Effect of introducing point mutations on the biological activity of FGF1. a Serum-starved NIH 3T3 cells were treated with 10 ng/mL FGF1 variants for 15 min in the presence of heparin (10 U/mL). Activation of the downstream cascade was detected by immunoblotting using the following antibodies: anti-phospho-FRS2 (pFRS2) and anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2 and anti-vinculin antibodies were used to confirm equal loading. Representative results are shown (n ≥ 3). The vertical lines in the last WB panel show the deleted wells. The original membranes, together with the method of trimming, are presented in Fig. S2. Densitometric analysis of pERK/ERK is presented in Fig. S3. b Effect of 20-h FGF1 variants stimulation (20 ng/mL) in the presence of 10 U/mL heparin on glucose uptake by 3T3-L1 adipocytes. Data are presented as mean ± SEM, n = 4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Article Snippet: Human FGF1 ELISA Kit was purchased from R&D Systems (#DFA00B).

Techniques: Activity Assay, Activation Assay, Western Blot

Journal: Molecular Biomedicine

Article Title: Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes

doi: 10.1186/s43556-025-00398-w

Figure Lengend Snippet: Impaired activation of signaling pathways by FGF1 variants due to reduced affinity for the FGFR1 (IIIc) receptor. a Serum-starved NIH 3T3 cells were stimulated with 10 ng/mL FGF1 variants in the presence of heparin (10 U/mL) for 15 min, and activation of downstream signaling cascades was detected by immunoblotting using the following antibodies: anti-phospho-FGFR (pFGFR), anti-phospho-PLCγ (pPLCγ), anti-phosphoFRS2 (pFRS2), anti-phospho-ERK1/2 (pERK1/2). Anti-ERK1/2, anti-FGFR1, anti-PLCγ and anti-γTubulin antibodies were used to confirm equal loading. Representative results are shown. Densitometric analysis is presented as mean ± SEM, n = 3/4. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001. b BLI analysis of the affinity of FGF1 variants for FGFR1-Fc (IIIc isoform). FGFR1-Fc was immobilized on a Protein A sensor and its interactions (association and dissociation) with selected FGF1 mutants were analyzed in the concentration range of 100–800 nM. Curves obtained by global fitting are marked in red. Representative results are shown (n ≥ 3). The equilibrium dissociation constant (K D ) was calculated from the saturation binding curve

Article Snippet: Human FGF1 ELISA Kit was purchased from R&D Systems (#DFA00B).

Techniques: Activation Assay, Protein-Protein interactions, Western Blot, Concentration Assay, Binding Assay

Journal: Molecular Biomedicine

Article Title: Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes

doi: 10.1186/s43556-025-00398-w

Figure Lengend Snippet: Effect of introduced mutations on the long-term activity of FGF1. a Induction of Glut1 expression after stimulation with FGF1 variants. 3T3-L1 cells were treated with 100 ng/mL FGF1 muteins in the presence of 10 U/mL heparin for 24 h, followed by WB analysis with anti-Glut1 and anti-γTubulin antibodies, data are presented as mean ± SEM, n = 6. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001. b Normalized thermal denaturation curves of FGF1 variants monitored by ellipticity changes (λ = 227 nm). c Degradation of FGF1 variants in the presence of adipocytes. Serum-starved 3T3-L1 adipocytes were incubated with 1 µg/mL FGF1 variants. The progress of proteolysis on subsequent days was monitored by immunoblotting with anti-FGF1 antibody. Representative results are shown ( n = 5). Densitometric analysis of proteolysis of FGF1 variants is presented as the ratio the intensity of the upper band to the intensity of the whole amount of protein. Mean ± SEM are shown, n = 5. Statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Article Snippet: Human FGF1 ELISA Kit was purchased from R&D Systems (#DFA00B).

Techniques: Activity Assay, Expressing, Incubation, Western Blot

Journal: Molecular Biomedicine

Article Title: Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes

doi: 10.1186/s43556-025-00398-w

Figure Lengend Snippet: Mitogenic activity of selected FGF1 variants in different cell types. Mitogenic activity of selected FGF1 variants was assessed by stimulating serum-starved C2C12, MCF7 or 4MBr-5 cells with FGF1 mutants in the concentration range 0.1–100 ng/ml in the presence of 10 U/ml heparin for 48 h, 72 h or 96 h, respectively. Cell viability was assessed by PrestoBlue cell viability assay a or by CellTiter-Fluor cell viability assay b . Cell number was determined by counting NucBlue-stained nuclei using an Opera Phenix Plus High-Content Screening System c . Data are presented as mean ± SEM, n = 3. Multiple t-test; statistical significance: * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001

Article Snippet: Human FGF1 ELISA Kit was purchased from R&D Systems (#DFA00B).

Techniques: Activity Assay, Concentration Assay, Viability Assay, Staining, High Content Screening

Journal: Molecular Biomedicine

Article Title: Engineered fibroblast growth factor 1 variants uncouple glucose-lowering effects from mitogenic activity with therapeutic potential for type 2 diabetes

doi: 10.1186/s43556-025-00398-w

Figure Lengend Snippet: Metabolic activity of FGF1 variants in vivo. a , b Change in blood glucose levels in db/db mice after a single administration of FGF1 variants (measurements at 0, 6, 18, 24, 30, 48, 72, 96 and 168 h after protein administration). FGF1 variants were administered at a dose of 1 mg/kg body weight. Data were normalized to glucose levels before protein administration and presented as mean ± SEM, n = 7/6. Statistical significance * p ≤ 0.05; ** p ≤ 0.01 and *** p ≤ 0.001; (*) indicates comparison with vehicle; (#) indicates comparison with wild-type protein. c Analysis of mouse body weight 96 h after administration. d Pharmacokinetics of FGF1 variants after a single subcutaneous administration in Wistar Han rats. FGF1 variants were administered subcutaneously at a dose 0.5 mg/kg, and blood samples were collected before injection and at 5 min, 15 min, 30 min and 1, 2, 4, 7, 12, 24, 48 h after injection and protein levels were analyzed by ELISA. Data are presented as mean ± SEM, n = 5

Article Snippet: Human FGF1 ELISA Kit was purchased from R&D Systems (#DFA00B).

Techniques: Activity Assay, In Vivo, Comparison, Drug discovery, Injection, Enzyme-linked Immunosorbent Assay

NgBR deficiency leads to the downregulation of FGF1 expression and secretion. A Expression clustering heatmap analysis of differentially expressed genes related to the PI3K-AKT pathway shown in Fig. B. B‒D SH-SY5Y cells were transfected with the indicated siRNAs for 48 h. Then, the samples were subjected to qRT‒PCR ( B ) or immunoblotting ( C ). The relative protein level of FGF1 to that of β-actin in ( C ) was analyzed as shown in D. n = 3, * P < 0.05, ** P < 0.01, *** P < 0.001. E SH-SY5Y cells were transfected with Flag or Flag-NgBR for 48 h, after which the cell lysates were subjected to immunoblot analysis. F The protein levels of FGF1 relative to those of β-actin in ( E ) were analyzed. n = 3, ** P < 0.01. G N2a cells were transfected with the indicated siRNAs for 48 h. Then, the cell lysates were subjected to immunoblot analysis. H The protein level of FGF1 relative to that of β-actin in ( G ) was analyzed. n = 3, * P < 0.05, ** P < 0.01. I MES23.5 cells were transfected with the indicated siRNAs for 48 h. Then, the cell lysates were subjected to immunoblot analysis. J The protein level of FGF1 relative to that of β-actin in ( I ) was analyzed. n = 3, * P < 0.05. K Nus1 flox/flox primary cortical neurons were infected with LV-Ctrl or LV-Cre and cultured for 6 days. Then, the cell lysates were subjected to immunoblot analysis. L The protein level of FGF1 relative to that of β-actin in ( K ) was analyzed. n = 3, ** P < 0.01. M-N SH-SY5Y cells were transfected with the indicated siRNAs for 24 h. Then, the cells were cultured with serum-free medium for 24 h, and the FGF1 content in the culture medium ( M ) and cell lysate ( N ) was detected via an ELISA kit. n = 3, * P < 0.05, ** P < 0.01, *** P < 0.001

Journal: Cellular and Molecular Life Sciences: CMLS

Article Title: Loss of NgBR causes neuronal damage through decreasing KAT7-mediated RFX1 acetylation and FGF1 expression

doi: 10.1007/s00018-025-05660-6

Figure Lengend Snippet: NgBR deficiency leads to the downregulation of FGF1 expression and secretion. A Expression clustering heatmap analysis of differentially expressed genes related to the PI3K-AKT pathway shown in Fig. B. B‒D SH-SY5Y cells were transfected with the indicated siRNAs for 48 h. Then, the samples were subjected to qRT‒PCR ( B ) or immunoblotting ( C ). The relative protein level of FGF1 to that of β-actin in ( C ) was analyzed as shown in D. n = 3, * P < 0.05, ** P < 0.01, *** P < 0.001. E SH-SY5Y cells were transfected with Flag or Flag-NgBR for 48 h, after which the cell lysates were subjected to immunoblot analysis. F The protein levels of FGF1 relative to those of β-actin in ( E ) were analyzed. n = 3, ** P < 0.01. G N2a cells were transfected with the indicated siRNAs for 48 h. Then, the cell lysates were subjected to immunoblot analysis. H The protein level of FGF1 relative to that of β-actin in ( G ) was analyzed. n = 3, * P < 0.05, ** P < 0.01. I MES23.5 cells were transfected with the indicated siRNAs for 48 h. Then, the cell lysates were subjected to immunoblot analysis. J The protein level of FGF1 relative to that of β-actin in ( I ) was analyzed. n = 3, * P < 0.05. K Nus1 flox/flox primary cortical neurons were infected with LV-Ctrl or LV-Cre and cultured for 6 days. Then, the cell lysates were subjected to immunoblot analysis. L The protein level of FGF1 relative to that of β-actin in ( K ) was analyzed. n = 3, ** P < 0.01. M-N SH-SY5Y cells were transfected with the indicated siRNAs for 24 h. Then, the cells were cultured with serum-free medium for 24 h, and the FGF1 content in the culture medium ( M ) and cell lysate ( N ) was detected via an ELISA kit. n = 3, * P < 0.05, ** P < 0.01, *** P < 0.001

Article Snippet: SH-SY5Y cells were inoculated into 24-well plates and treated with siRNAs against NUS1 for 24 h. Then, the cells were cultured with serum-free medium for 24 h, and 100 μL of the FGF1 content in the culture medium or in cell lysate was measured with an ELISA kit (EK0339, BOSTER, Wuhan, China).

Techniques: Expressing, Transfection, Western Blot, Infection, Cell Culture, Enzyme-linked Immunosorbent Assay

Clinical characteristics of individuals with undetectable and detectable serum FGF1 levels.

Journal: Frontiers in Endocrinology

Article Title: Serum fibroblast growth factor 1 and its association with pancreatic beta cell function and insulin sensitivity in adults with glucose intolerance

doi: 10.3389/fendo.2023.1198311

Figure Lengend Snippet: Clinical characteristics of individuals with undetectable and detectable serum FGF1 levels.

Article Snippet: Serum FGF1 levels were examined using an enzyme-linked immunosorbent assay (catalog no. DFA00B; R&D Systems, Inc., Minneapolis, MN USA).

Techniques:

Metabolic parameters of individuals with undetectable (group 1), low (group 2), and high (group 3) serum FGF1 levels.

Journal: Frontiers in Endocrinology

Article Title: Serum fibroblast growth factor 1 and its association with pancreatic beta cell function and insulin sensitivity in adults with glucose intolerance

doi: 10.3389/fendo.2023.1198311

Figure Lengend Snippet: Metabolic parameters of individuals with undetectable (group 1), low (group 2), and high (group 3) serum FGF1 levels.

Article Snippet: Serum FGF1 levels were examined using an enzyme-linked immunosorbent assay (catalog no. DFA00B; R&D Systems, Inc., Minneapolis, MN USA).

Techniques:

Metabolic parameters of individuals with undetectable (group 1), low (group 2), and high (group 3) serum FGF1 levels. DI, disposition index; IGI, insulinogenic index; ISI, Matsuda insulin sensitivity index.

Journal: Frontiers in Endocrinology

Article Title: Serum fibroblast growth factor 1 and its association with pancreatic beta cell function and insulin sensitivity in adults with glucose intolerance

doi: 10.3389/fendo.2023.1198311

Figure Lengend Snippet: Metabolic parameters of individuals with undetectable (group 1), low (group 2), and high (group 3) serum FGF1 levels. DI, disposition index; IGI, insulinogenic index; ISI, Matsuda insulin sensitivity index.

Article Snippet: Serum FGF1 levels were examined using an enzyme-linked immunosorbent assay (catalog no. DFA00B; R&D Systems, Inc., Minneapolis, MN USA).

Techniques:

Univariable and multivariable analysis of the association between serum FGF1 levels and metabolic parameters using a Tobit regression model.

Journal: Frontiers in Endocrinology

Article Title: Serum fibroblast growth factor 1 and its association with pancreatic beta cell function and insulin sensitivity in adults with glucose intolerance

doi: 10.3389/fendo.2023.1198311

Figure Lengend Snippet: Univariable and multivariable analysis of the association between serum FGF1 levels and metabolic parameters using a Tobit regression model.

Article Snippet: Serum FGF1 levels were examined using an enzyme-linked immunosorbent assay (catalog no. DFA00B; R&D Systems, Inc., Minneapolis, MN USA).

Techniques:

Box plot of the estimated log-transformed serum FGF1 level according to the quartile of each parameter using a Tobit regression model adjusted by age and sex. DI, disposition index; IGI, insulinogenic index; ISI, Matsuda insulin sensitivity index.

Journal: Frontiers in Endocrinology

Article Title: Serum fibroblast growth factor 1 and its association with pancreatic beta cell function and insulin sensitivity in adults with glucose intolerance

doi: 10.3389/fendo.2023.1198311

Figure Lengend Snippet: Box plot of the estimated log-transformed serum FGF1 level according to the quartile of each parameter using a Tobit regression model adjusted by age and sex. DI, disposition index; IGI, insulinogenic index; ISI, Matsuda insulin sensitivity index.

Article Snippet: Serum FGF1 levels were examined using an enzyme-linked immunosorbent assay (catalog no. DFA00B; R&D Systems, Inc., Minneapolis, MN USA).

Techniques: Transformation Assay

A Schematic diagram of the RNAseq experiments performed. PC9 cells were transfected with control or STYK1 siRNAs. Forty-eight hours post-transfection, cells were treated with DMSO (control) or afatinib (5 nM) for an additional 24 h. Differentially expressed genes between STYK1 siRNA + afatinib versus control siRNA + afatinib were determined (|log2FoldChange | = 2, p adj. <0.05) from the RNAseq data. B Heatmap of DEG for STYK1 siRNA + afatinib versus control siRNA + afatinib based on Z-scores. C Expression of top DEG between STYK1 siRNA + afatinib relative to control siRNA + afatinib as determined by RNAseq. D , E Validation by qRT-PCR in PC9 ( D ) and HCC827 ( E ) cells of the RNAseq results for FGF1. Data are presented as mean ± SEM from two independent experiments. F Validation at the protein level of the differential expression of FGF1, in the experimental conditions of the RNAseq screen, as determined by ELISA. The graph represents mean ± SEM from three independent experiments. G PC9 cells were transfected with empty vector (EV) or STYK1 and incubated for 48 h. FGF1 mRNA levels were determined by qRT-PCR and plotted as mean ± SEM ( n = 2). H PC9 cells were reverse transfected with non-targeting control or FGF1 siRNAs. 48 h after transfection, cells were treated with control (DMSO), afatinib (5 nM) or osimertinib (10 nM). Cell viability was measured after an additional 48 h of incubation. Data are presented as mean ± SEM from four independent experiments. Statistics are shown for FGF1 siRNA compared to control siRNA for the respective treatments.

Journal: Cell Death & Disease

Article Title: The EGFR-STYK1-FGF1 axis sustains functional drug tolerance to EGFR inhibitors in EGFR-mutant non-small cell lung cancer

doi: 10.1038/s41419-022-04994-4

Figure Lengend Snippet: A Schematic diagram of the RNAseq experiments performed. PC9 cells were transfected with control or STYK1 siRNAs. Forty-eight hours post-transfection, cells were treated with DMSO (control) or afatinib (5 nM) for an additional 24 h. Differentially expressed genes between STYK1 siRNA + afatinib versus control siRNA + afatinib were determined (|log2FoldChange | = 2, p adj. <0.05) from the RNAseq data. B Heatmap of DEG for STYK1 siRNA + afatinib versus control siRNA + afatinib based on Z-scores. C Expression of top DEG between STYK1 siRNA + afatinib relative to control siRNA + afatinib as determined by RNAseq. D , E Validation by qRT-PCR in PC9 ( D ) and HCC827 ( E ) cells of the RNAseq results for FGF1. Data are presented as mean ± SEM from two independent experiments. F Validation at the protein level of the differential expression of FGF1, in the experimental conditions of the RNAseq screen, as determined by ELISA. The graph represents mean ± SEM from three independent experiments. G PC9 cells were transfected with empty vector (EV) or STYK1 and incubated for 48 h. FGF1 mRNA levels were determined by qRT-PCR and plotted as mean ± SEM ( n = 2). H PC9 cells were reverse transfected with non-targeting control or FGF1 siRNAs. 48 h after transfection, cells were treated with control (DMSO), afatinib (5 nM) or osimertinib (10 nM). Cell viability was measured after an additional 48 h of incubation. Data are presented as mean ± SEM from four independent experiments. Statistics are shown for FGF1 siRNA compared to control siRNA for the respective treatments.

Article Snippet: The FGF1 ELISA was performed with the Quantikine FGF1 ELISA kit (DFA00B, R&D systems, Minneapolis, MN, USA) according to the manufacturer’s instructions.

Techniques: Transfection, Control, Expressing, Biomarker Discovery, Quantitative RT-PCR, Quantitative Proteomics, Enzyme-linked Immunosorbent Assay, Plasmid Preparation, Incubation

Journal: Cell Death & Disease

Article Title: The EGFR-STYK1-FGF1 axis sustains functional drug tolerance to EGFR inhibitors in EGFR-mutant non-small cell lung cancer

doi: 10.1038/s41419-022-04994-4

Article Snippet: The FGF1 ELISA was performed with the Quantikine FGF1 ELISA kit (DFA00B, R&D systems, Minneapolis, MN, USA) according to the manufacturer’s instructions.

Techniques: Transfection, Control, Expressing, Biomarker Discovery, Quantitative RT-PCR, Quantitative Proteomics, Enzyme-linked Immunosorbent Assay, Plasmid Preparation, Incubation

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