recombinant protein saa1 Search Results


90
OriGene recombinant human saa1
Recombinant Human Saa1, supplied by OriGene, 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/recombinant+protein+saa1/pmc06179936-96-0-12?v=OriGene
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91
OriGene eukarytoic recombinant human saa1 1
Amino acid sequence of naturally occurring and commercially available recombinant human A-SAA preparations discussed in the present paper.
Eukarytoic Recombinant Human Saa1 1, supplied by OriGene, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+protein+saa1/pmc09935590-9-0-5?v=OriGene
Average 91 stars, based on 1 article reviews
eukarytoic recombinant human saa1 1 - by Bioz Stars, 2026-07
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90
OriGene recombinant saa1
Human SAA and/or HDL proteins compared in this study †
Recombinant Saa1, supplied by OriGene, 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/recombinant+protein+saa1/pmc07753654-63-42-48?v=OriGene
Average 90 stars, based on 1 article reviews
recombinant saa1 - by Bioz Stars, 2026-07
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94
OriGene human recombinant saa1 protein
(A) Cell-cell communication analysis of SAA signaling pathway for the indicated depots and cells. Line colors and widths represent the sending cell and the strength of the signal, respectively. (B) Pseudobulk comparison of differentially expressed genes in epiploic vs. subcutaneous depots, highlighting the indicated signaling pathways. (C) Expression of <t>SAA1</t> mRNA upon stimulation with LPS (10 ng/mL), TNF-α (2.5 ng/mL), IL-1β (10 ng/mL), or IL-6 (10 ng/mL) for 24 h. Data are presented as fold change (FC) over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. (D) Relative expression of SAA1 (left) and SAA2 (right) mRNA in adipocytes, ASPCs, adipose-derived endothelial cells (adECs), and THP1-derived macrophages (THP1 M0). Significant (<0.05) p values compared with the cell-type-specific control from one-way ANOVA are shown. (E) Results from ELISA measurements of SAA in conditioned media from human adipocytes incubated without or with LPS for 72 h. Results are displayed as mean, error bars represent standard error of the mean, and statistical significance was calculated using Student’s t test. (F) Analyses of DNA methylation in the indicated cell classes for the promoter and gene body regions of SAA1 and SAA2 , respectively. Chromosomal localization and motifs for NFKB2/RELA/REL and STAT3 are indicated for both genes. (G) SAA1 and SAA2 mRNA expression in adipocytes treated with or without LPS in the presence or absence of different inhibitors described in the main text. Data are presented as FC over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. For (C), (D), and (G), data are displayed as geometric mean ± 95% confidence intervals with technical replicates displayed from three independent experiments. ASPC, adipose stromal and progenitor cell.
Human Recombinant Saa1 Protein, supplied by OriGene, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+protein+saa1/pmc12989110-39-0-5?v=OriGene
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human recombinant saa1 protein - by Bioz Stars, 2026-07
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93
Boster Bio saa1
(A) Cell-cell communication analysis of SAA signaling pathway for the indicated depots and cells. Line colors and widths represent the sending cell and the strength of the signal, respectively. (B) Pseudobulk comparison of differentially expressed genes in epiploic vs. subcutaneous depots, highlighting the indicated signaling pathways. (C) Expression of <t>SAA1</t> mRNA upon stimulation with LPS (10 ng/mL), TNF-α (2.5 ng/mL), IL-1β (10 ng/mL), or IL-6 (10 ng/mL) for 24 h. Data are presented as fold change (FC) over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. (D) Relative expression of SAA1 (left) and SAA2 (right) mRNA in adipocytes, ASPCs, adipose-derived endothelial cells (adECs), and THP1-derived macrophages (THP1 M0). Significant (<0.05) p values compared with the cell-type-specific control from one-way ANOVA are shown. (E) Results from ELISA measurements of SAA in conditioned media from human adipocytes incubated without or with LPS for 72 h. Results are displayed as mean, error bars represent standard error of the mean, and statistical significance was calculated using Student’s t test. (F) Analyses of DNA methylation in the indicated cell classes for the promoter and gene body regions of SAA1 and SAA2 , respectively. Chromosomal localization and motifs for NFKB2/RELA/REL and STAT3 are indicated for both genes. (G) SAA1 and SAA2 mRNA expression in adipocytes treated with or without LPS in the presence or absence of different inhibitors described in the main text. Data are presented as FC over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. For (C), (D), and (G), data are displayed as geometric mean ± 95% confidence intervals with technical replicates displayed from three independent experiments. ASPC, adipose stromal and progenitor cell.
Saa1, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ProSci Incorporated recombinant saa1 protein
The toxicity of VSMCs was determined by the MTT assay ( n = 3). Notes: The cells in control group received no treatment; to detect whether <t>SAA1</t> or the combination of SAA1 with LPS was toxic to VSMCs, cells were treated with different concentrations of SAA1 (5, 10, 15, 20 μg/ml) with/without LPS (1 μg/ml) for 24 h
Recombinant Saa1 Protein, supplied by ProSci Incorporated, 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/recombinant+protein+saa1/pmc06582534-95-2-6?v=ProSci+Incorporated
Average 90 stars, based on 1 article reviews
recombinant saa1 protein - by Bioz Stars, 2026-07
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N/A
Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Major acute phase reactant. Apolipoprotein of the HDL complex. Tissue specificity: Expressed by the liver; secreted in plasma. Disease: Note=Reactive, secondary amyloidosis is characterized by the extracellular accumulation
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Amino acid sequence of naturally occurring and commercially available recombinant human A-SAA preparations discussed in the present paper.

Journal: Frontiers in Endocrinology

Article Title: Acute-serum amyloid A and A-SAA-derived peptides as formyl peptide receptor (FPR) 2 ligands

doi: 10.3389/fendo.2023.1119227

Figure Lengend Snippet: Amino acid sequence of naturally occurring and commercially available recombinant human A-SAA preparations discussed in the present paper.

Article Snippet: Eukarytoic recombinant human SAA1.1 (erhSAA1.1; Origene) , RS FFSFL GEAFD GARDM WRAYS DMREA NYIGS DKYFH ARGNY DAAKR GPGGV WAAEA ISDAR ENIQR FFGHG AEDSL ADQAA NEWGR SGKDP NHFRP AGLPE KYEQK LISEE DL.

Techniques: Sequencing, Recombinant

Human SAA and/or HDL proteins compared in this study †

Journal: Journal of Leukocyte Biology

Article Title: Effects of serum amyloid protein A on influenza A virus replication and viral interactions with neutrophils

doi: 10.1002/JLB.4AB0220-116RR

Figure Lengend Snippet: Human SAA and/or HDL proteins compared in this study †

Article Snippet: We tested several commercially available forms of SAA1, including native human serum SAA complexed with HDL (SAAHDL; Fisher Scientific), SAA (19‐94) isolated from human serum (Abcam; Cambridge, United Kingdom, Abcam.com), recombinant SAA1 derived from E. coli (Peprotech; Rocky Hill, NJ, USA), and recombinant SAA1 derived from HEK cells (Origene, Rockville, MD, USA).

Techniques: Sequencing, Recombinant

Binding of SAA preparations to influenza A virus (IAV)—Binding of SAAs to the Phil82 strain of IAV was tested by ELISA as described in Section 2 (“Materials And Methods”) using an anti‐serum amyloid A (anti‐SAA1) antibody (panel A). Binding of SAA1 was also tested in presence of maltose (panel B) and using an anti‐DDK antibody for detection (SAA1 has a DDK tail) (panel C). HDL binding to IAV was tested as well (panel D). * = P < 0.05 and ** = P < 0.01 compared to control. Results represent mean ± sem for 3 to 5 experiments

Journal: Journal of Leukocyte Biology

Article Title: Effects of serum amyloid protein A on influenza A virus replication and viral interactions with neutrophils

doi: 10.1002/JLB.4AB0220-116RR

Figure Lengend Snippet: Binding of SAA preparations to influenza A virus (IAV)—Binding of SAAs to the Phil82 strain of IAV was tested by ELISA as described in Section 2 (“Materials And Methods”) using an anti‐serum amyloid A (anti‐SAA1) antibody (panel A). Binding of SAA1 was also tested in presence of maltose (panel B) and using an anti‐DDK antibody for detection (SAA1 has a DDK tail) (panel C). HDL binding to IAV was tested as well (panel D). * = P < 0.05 and ** = P < 0.01 compared to control. Results represent mean ± sem for 3 to 5 experiments

Article Snippet: We tested several commercially available forms of SAA1, including native human serum SAA complexed with HDL (SAAHDL; Fisher Scientific), SAA (19‐94) isolated from human serum (Abcam; Cambridge, United Kingdom, Abcam.com), recombinant SAA1 derived from E. coli (Peprotech; Rocky Hill, NJ, USA), and recombinant SAA1 derived from HEK cells (Origene, Rockville, MD, USA).

Techniques: Binding Assay, Virus, Enzyme-linked Immunosorbent Assay, Control

Neutralization of influenza A virus (IAV) by serum SAA, but not recombinant, SAA preparations—The indicated strains of IAV were pre‐incubated with SAA and or HDL preparations and then these were used to infection MDCK cell monolayers as described in Section 2 (“Materials And Methods”). Serum SAA from Abcam (panel A), SAA complexed with HDL (SAAHDL; panel B), serum HDL (panel C), and two recombinant serum amyloid A (SAA1) preparations were compared (panel D; HDL and SAAHDL included for comparison). * = P < 0.05 and ** = P < 0.01 and *** = < 0.001 compared to control. Results represent mean ± sem for 3 to 5 experiments

Journal: Journal of Leukocyte Biology

Article Title: Effects of serum amyloid protein A on influenza A virus replication and viral interactions with neutrophils

doi: 10.1002/JLB.4AB0220-116RR

Figure Lengend Snippet: Neutralization of influenza A virus (IAV) by serum SAA, but not recombinant, SAA preparations—The indicated strains of IAV were pre‐incubated with SAA and or HDL preparations and then these were used to infection MDCK cell monolayers as described in Section 2 (“Materials And Methods”). Serum SAA from Abcam (panel A), SAA complexed with HDL (SAAHDL; panel B), serum HDL (panel C), and two recombinant serum amyloid A (SAA1) preparations were compared (panel D; HDL and SAAHDL included for comparison). * = P < 0.05 and ** = P < 0.01 and *** = < 0.001 compared to control. Results represent mean ± sem for 3 to 5 experiments

Article Snippet: We tested several commercially available forms of SAA1, including native human serum SAA complexed with HDL (SAAHDL; Fisher Scientific), SAA (19‐94) isolated from human serum (Abcam; Cambridge, United Kingdom, Abcam.com), recombinant SAA1 derived from E. coli (Peprotech; Rocky Hill, NJ, USA), and recombinant SAA1 derived from HEK cells (Origene, Rockville, MD, USA).

Techniques: Neutralization, Virus, Recombinant, Incubation, Infection, Comparison, Control

Stimulation of neutrophil hydrogen peroxide production by SAA and or HDL—Neutrophil H 2 O 2 generation was measured through decline in scopoletin fluorescence as described in Section 2 (“Materials And Methods”). Influenza A virus (IAV; Phil82 strain) was pre‐incubated with the indicated concentrations of SAA and/or HDL preparations and added to suspensions of neutrophils at time 0. Results of unstimulated cells (PBS) are included for comparison. Instances where serum amyloid A (SAA1) proteins increased IAV‐induced H 2 O 2 production are noted by * or ** in in legend, where * = P < 0.05 and ** = P < 0.01 compared to control. Results represent mean ± sem for 3 to 5 experiments

Journal: Journal of Leukocyte Biology

Article Title: Effects of serum amyloid protein A on influenza A virus replication and viral interactions with neutrophils

doi: 10.1002/JLB.4AB0220-116RR

Figure Lengend Snippet: Stimulation of neutrophil hydrogen peroxide production by SAA and or HDL—Neutrophil H 2 O 2 generation was measured through decline in scopoletin fluorescence as described in Section 2 (“Materials And Methods”). Influenza A virus (IAV; Phil82 strain) was pre‐incubated with the indicated concentrations of SAA and/or HDL preparations and added to suspensions of neutrophils at time 0. Results of unstimulated cells (PBS) are included for comparison. Instances where serum amyloid A (SAA1) proteins increased IAV‐induced H 2 O 2 production are noted by * or ** in in legend, where * = P < 0.05 and ** = P < 0.01 compared to control. Results represent mean ± sem for 3 to 5 experiments

Article Snippet: We tested several commercially available forms of SAA1, including native human serum SAA complexed with HDL (SAAHDL; Fisher Scientific), SAA (19‐94) isolated from human serum (Abcam; Cambridge, United Kingdom, Abcam.com), recombinant SAA1 derived from E. coli (Peprotech; Rocky Hill, NJ, USA), and recombinant SAA1 derived from HEK cells (Origene, Rockville, MD, USA).

Techniques: Fluorescence, Virus, Incubation, Comparison, Control

Effect of SAA and or HDL on neutrophil IL‐8 production or caspase activity—In panel A, IL‐8 production by neutrophils was measured by ELISA as described in Section 2 (“Materials And Methods”). ** = P < 0.01 compared to control. Results represent mean ± sem for 3 to 5 experiments. Panel B shows IL‐8 production in response to influenza A virus (IAV) alone or IAV combined with Apo‐serum amyloid A (Apo‐SAA1). Panel C shows caspase 3 activation by IAV alone or IAV combined with Apo‐SAA1, SAAHDL (SAA complexed with HDL), SAA1, or HDL. * = P < 0.05 compared to results with neutrophils in media alone. Results are mean ± sem of 4 experiments

Journal: Journal of Leukocyte Biology

Article Title: Effects of serum amyloid protein A on influenza A virus replication and viral interactions with neutrophils

doi: 10.1002/JLB.4AB0220-116RR

Figure Lengend Snippet: Effect of SAA and or HDL on neutrophil IL‐8 production or caspase activity—In panel A, IL‐8 production by neutrophils was measured by ELISA as described in Section 2 (“Materials And Methods”). ** = P < 0.01 compared to control. Results represent mean ± sem for 3 to 5 experiments. Panel B shows IL‐8 production in response to influenza A virus (IAV) alone or IAV combined with Apo‐serum amyloid A (Apo‐SAA1). Panel C shows caspase 3 activation by IAV alone or IAV combined with Apo‐SAA1, SAAHDL (SAA complexed with HDL), SAA1, or HDL. * = P < 0.05 compared to results with neutrophils in media alone. Results are mean ± sem of 4 experiments

Article Snippet: We tested several commercially available forms of SAA1, including native human serum SAA complexed with HDL (SAAHDL; Fisher Scientific), SAA (19‐94) isolated from human serum (Abcam; Cambridge, United Kingdom, Abcam.com), recombinant SAA1 derived from E. coli (Peprotech; Rocky Hill, NJ, USA), and recombinant SAA1 derived from HEK cells (Origene, Rockville, MD, USA).

Techniques: Activity Assay, Enzyme-linked Immunosorbent Assay, Control, Virus, Activation Assay

Effects of TLR2 blocking antibodies, pertussis toxin (PT), and wortmannin of neutrophil responses to Apo‐serum amyloid A  (Apo‐SAA1)

Journal: Journal of Leukocyte Biology

Article Title: Effects of serum amyloid protein A on influenza A virus replication and viral interactions with neutrophils

doi: 10.1002/JLB.4AB0220-116RR

Figure Lengend Snippet: Effects of TLR2 blocking antibodies, pertussis toxin (PT), and wortmannin of neutrophil responses to Apo‐serum amyloid A (Apo‐SAA1)

Article Snippet: We tested several commercially available forms of SAA1, including native human serum SAA complexed with HDL (SAAHDL; Fisher Scientific), SAA (19‐94) isolated from human serum (Abcam; Cambridge, United Kingdom, Abcam.com), recombinant SAA1 derived from E. coli (Peprotech; Rocky Hill, NJ, USA), and recombinant SAA1 derived from HEK cells (Origene, Rockville, MD, USA).

Techniques: Blocking Assay, Control, Virus

(A) Cell-cell communication analysis of SAA signaling pathway for the indicated depots and cells. Line colors and widths represent the sending cell and the strength of the signal, respectively. (B) Pseudobulk comparison of differentially expressed genes in epiploic vs. subcutaneous depots, highlighting the indicated signaling pathways. (C) Expression of SAA1 mRNA upon stimulation with LPS (10 ng/mL), TNF-α (2.5 ng/mL), IL-1β (10 ng/mL), or IL-6 (10 ng/mL) for 24 h. Data are presented as fold change (FC) over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. (D) Relative expression of SAA1 (left) and SAA2 (right) mRNA in adipocytes, ASPCs, adipose-derived endothelial cells (adECs), and THP1-derived macrophages (THP1 M0). Significant (<0.05) p values compared with the cell-type-specific control from one-way ANOVA are shown. (E) Results from ELISA measurements of SAA in conditioned media from human adipocytes incubated without or with LPS for 72 h. Results are displayed as mean, error bars represent standard error of the mean, and statistical significance was calculated using Student’s t test. (F) Analyses of DNA methylation in the indicated cell classes for the promoter and gene body regions of SAA1 and SAA2 , respectively. Chromosomal localization and motifs for NFKB2/RELA/REL and STAT3 are indicated for both genes. (G) SAA1 and SAA2 mRNA expression in adipocytes treated with or without LPS in the presence or absence of different inhibitors described in the main text. Data are presented as FC over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. For (C), (D), and (G), data are displayed as geometric mean ± 95% confidence intervals with technical replicates displayed from three independent experiments. ASPC, adipose stromal and progenitor cell.

Journal: Cell metabolism

Article Title: Cytoarchitectural multi-depot profiling reveals immune-metabolic crosstalk in human colon-associated adipose tissue

doi: 10.1016/j.cmet.2025.12.008

Figure Lengend Snippet: (A) Cell-cell communication analysis of SAA signaling pathway for the indicated depots and cells. Line colors and widths represent the sending cell and the strength of the signal, respectively. (B) Pseudobulk comparison of differentially expressed genes in epiploic vs. subcutaneous depots, highlighting the indicated signaling pathways. (C) Expression of SAA1 mRNA upon stimulation with LPS (10 ng/mL), TNF-α (2.5 ng/mL), IL-1β (10 ng/mL), or IL-6 (10 ng/mL) for 24 h. Data are presented as fold change (FC) over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. (D) Relative expression of SAA1 (left) and SAA2 (right) mRNA in adipocytes, ASPCs, adipose-derived endothelial cells (adECs), and THP1-derived macrophages (THP1 M0). Significant (<0.05) p values compared with the cell-type-specific control from one-way ANOVA are shown. (E) Results from ELISA measurements of SAA in conditioned media from human adipocytes incubated without or with LPS for 72 h. Results are displayed as mean, error bars represent standard error of the mean, and statistical significance was calculated using Student’s t test. (F) Analyses of DNA methylation in the indicated cell classes for the promoter and gene body regions of SAA1 and SAA2 , respectively. Chromosomal localization and motifs for NFKB2/RELA/REL and STAT3 are indicated for both genes. (G) SAA1 and SAA2 mRNA expression in adipocytes treated with or without LPS in the presence or absence of different inhibitors described in the main text. Data are presented as FC over vehicle. Significant (<0.05) p values compared with the vehicle from one-way ANOVA are shown. For (C), (D), and (G), data are displayed as geometric mean ± 95% confidence intervals with technical replicates displayed from three independent experiments. ASPC, adipose stromal and progenitor cell.

Article Snippet: Human recombinant SAA1 protein , OriGene , Cat#TP310664.

Techniques: Comparison, Protein-Protein interactions, Expressing, Derivative Assay, Control, Enzyme-linked Immunosorbent Assay, Incubation, DNA Methylation Assay

(A) Top Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways based on differentially expressed genes from comparisons of SAA1- or LPS-treated vs. control-treated adipose-derived stromal-vascular cells. (B) Network view of the six common SAA1- and LPS-regulated pathways showing shared and treatment-specific genes. (C) Expression scores for SAA1- (left) and LPS-responsive (right) genes following a 6-h incubation with either ligand in stromal-vascular cells from subcutaneous human WAT. Results are displayed on the uniform manifold approximation and projection panel from and violin plots for each indicated cell class. Note that adipocytes and mesothelial cells were removed as these are not present in the stromal-vascular fraction from the subcutaneous depot. (D) Representative immunostaining of epiploic adipose tissue using antibodies directed against markers for Adipo SAA (CES1) and macrophages (CD68). Hoechst33342 was used as the counterstain for nuclei. Scale bar, 100 μm. ASPC, adipose stromal and progenitor cell; NES, normalized enrichment score.

Journal: Cell metabolism

Article Title: Cytoarchitectural multi-depot profiling reveals immune-metabolic crosstalk in human colon-associated adipose tissue

doi: 10.1016/j.cmet.2025.12.008

Figure Lengend Snippet: (A) Top Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways based on differentially expressed genes from comparisons of SAA1- or LPS-treated vs. control-treated adipose-derived stromal-vascular cells. (B) Network view of the six common SAA1- and LPS-regulated pathways showing shared and treatment-specific genes. (C) Expression scores for SAA1- (left) and LPS-responsive (right) genes following a 6-h incubation with either ligand in stromal-vascular cells from subcutaneous human WAT. Results are displayed on the uniform manifold approximation and projection panel from and violin plots for each indicated cell class. Note that adipocytes and mesothelial cells were removed as these are not present in the stromal-vascular fraction from the subcutaneous depot. (D) Representative immunostaining of epiploic adipose tissue using antibodies directed against markers for Adipo SAA (CES1) and macrophages (CD68). Hoechst33342 was used as the counterstain for nuclei. Scale bar, 100 μm. ASPC, adipose stromal and progenitor cell; NES, normalized enrichment score.

Article Snippet: Human recombinant SAA1 protein , OriGene , Cat#TP310664.

Techniques: Control, Derivative Assay, Expressing, Incubation, Immunostaining

The toxicity of VSMCs was determined by the MTT assay ( n = 3). Notes: The cells in control group received no treatment; to detect whether SAA1 or the combination of SAA1 with LPS was toxic to VSMCs, cells were treated with different concentrations of SAA1 (5, 10, 15, 20 μg/ml) with/without LPS (1 μg/ml) for 24 h

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: The toxicity of VSMCs was determined by the MTT assay ( n = 3). Notes: The cells in control group received no treatment; to detect whether SAA1 or the combination of SAA1 with LPS was toxic to VSMCs, cells were treated with different concentrations of SAA1 (5, 10, 15, 20 μg/ml) with/without LPS (1 μg/ml) for 24 h

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: MTT Assay, Control

Effects of LPS on SAA1 protein expression in VSMCs detected by Western blotting ( n = 3). Notes: a - b , The SAA1 protein expression in VSMCs induced by LPS with different concentrations (0, 0.01, 0.1, 1, 10 μg/ml) for 24 h; c - d , Detection of SAA1 protein expression in VSMCs induced by LPS (1 μg/ml) at different time points (6, 12, 24, 48 h). The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Effects of LPS on SAA1 protein expression in VSMCs detected by Western blotting ( n = 3). Notes: a - b , The SAA1 protein expression in VSMCs induced by LPS with different concentrations (0, 0.01, 0.1, 1, 10 μg/ml) for 24 h; c - d , Detection of SAA1 protein expression in VSMCs induced by LPS (1 μg/ml) at different time points (6, 12, 24, 48 h). The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: Expressing, Western Blot

Effects of different concentrations of recombinant SAA1 protein on NOX4/ROS pathway in LPS-induced VSMCs ( n = 3) . Notes: The levels of superoxide anion (O 2 − ) production ( a ), NADPH oxidase activity ( b ), and NOX-4 protein expression ( c - d ) in VSMCs after pre-incubation with different concentrations of SAA (5, 10, 15, 20 μg/ml) for 24 h followed by the addition with 1 μg/ml LPS for 24 h; Some VSMCs were treated with SAA (20 μg/ml) alone for 24 h. The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Effects of different concentrations of recombinant SAA1 protein on NOX4/ROS pathway in LPS-induced VSMCs ( n = 3) . Notes: The levels of superoxide anion (O 2 − ) production ( a ), NADPH oxidase activity ( b ), and NOX-4 protein expression ( c - d ) in VSMCs after pre-incubation with different concentrations of SAA (5, 10, 15, 20 μg/ml) for 24 h followed by the addition with 1 μg/ml LPS for 24 h; Some VSMCs were treated with SAA (20 μg/ml) alone for 24 h. The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: Recombinant, Activity Assay, Expressing, Incubation

Effects of recombinant SAA1 protein treatment for different time points on NOX4/ROS pathway in LPS-induced VSMCs ( n = 3). Notes: The levels of O 2 − production ( a ), NADPH oxidase activity ( b ) and NOX-4 protein ( c - d ) in VSMC after pre-incubation with 20 μg/ml SAA1 for different time points (0, 24, 48, 72 h) followed by the addition with 1 μg/ml LPS for 24 h. The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Effects of recombinant SAA1 protein treatment for different time points on NOX4/ROS pathway in LPS-induced VSMCs ( n = 3). Notes: The levels of O 2 − production ( a ), NADPH oxidase activity ( b ) and NOX-4 protein ( c - d ) in VSMC after pre-incubation with 20 μg/ml SAA1 for different time points (0, 24, 48, 72 h) followed by the addition with 1 μg/ml LPS for 24 h. The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: Recombinant, Activity Assay, Incubation

Effects of recombinant SAA1 protein on inflammatory factors in LPS-induced VSMCs detected by qRT-PCR ( n = 3). Notes: a , The mRNA expressions of inflammatory factors ( IL-1β , IL-6 , IL-8 , IL-17 , TNF-α , MCP-1 and bFGF ) in VSMCs after pre-incubation with different concentrations of SAA (5, 10, 15, 20 μg/ml) for 24 h followed by the addition with 1 μg/ml LPS for 24 h; Some VSMCs were treated with SAA (20 μg/ml) alone for 24 h; b , The mRNA expressions of inflammatory factors in VSMCs ( IL-1β , IL-6 , IL-8 , IL-17 , TNF-α , MCP-1 and bFGF ) after pre-incubation with 20 μg/ml SAA for different time points (0, 24, 48, 72 h) and addition with 1 μg/ml LPS for 24 h. The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Effects of recombinant SAA1 protein on inflammatory factors in LPS-induced VSMCs detected by qRT-PCR ( n = 3). Notes: a , The mRNA expressions of inflammatory factors ( IL-1β , IL-6 , IL-8 , IL-17 , TNF-α , MCP-1 and bFGF ) in VSMCs after pre-incubation with different concentrations of SAA (5, 10, 15, 20 μg/ml) for 24 h followed by the addition with 1 μg/ml LPS for 24 h; Some VSMCs were treated with SAA (20 μg/ml) alone for 24 h; b , The mRNA expressions of inflammatory factors in VSMCs ( IL-1β , IL-6 , IL-8 , IL-17 , TNF-α , MCP-1 and bFGF ) after pre-incubation with 20 μg/ml SAA for different time points (0, 24, 48, 72 h) and addition with 1 μg/ml LPS for 24 h. The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: Recombinant, Quantitative RT-PCR, Incubation

Inhibitory effect of SAA1 siRNA on the levels of O 2 − production ( a ), NADPH oxidase activity ( b ) and NOX-4 protein ( c - d ) in LPS (1 μg/ml) -induced VSMCs via suppressing NOX4/ROS pathway ( n = 3). Notes: The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Inhibitory effect of SAA1 siRNA on the levels of O 2 − production ( a ), NADPH oxidase activity ( b ) and NOX-4 protein ( c - d ) in LPS (1 μg/ml) -induced VSMCs via suppressing NOX4/ROS pathway ( n = 3). Notes: The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: Activity Assay

Inhibitory effect of SAA1 siRNA on inflammatory factors ( IL-1β , IL-6 , IL-8 , IL-17 , TNF-α and MCP-1 ) in LPS (1 μg/ml) -induced VSMCs via suppressing NOX4/ROS pathway detected by qRT-PCR ( n = 3). Notes: The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Inhibitory effect of SAA1 siRNA on inflammatory factors ( IL-1β , IL-6 , IL-8 , IL-17 , TNF-α and MCP-1 ) in LPS (1 μg/ml) -induced VSMCs via suppressing NOX4/ROS pathway detected by qRT-PCR ( n = 3). Notes: The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: Quantitative RT-PCR

Inhibitory effect of SAA1 siRNA on p38MAPK/NF-κB signaling pathway via suppressing NOX4/ROS pathway in LPS (1 μg/ml) -induced VSMCs ( n = 3). Notes: The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Journal: BMC Molecular and Cell Biology

Article Title: SAA1 increases NOX4/ROS production to promote LPS-induced inflammation in vascular smooth muscle cells through activating p38MAPK/NF-κB pathway

doi: 10.1186/s12860-019-0197-0

Figure Lengend Snippet: Inhibitory effect of SAA1 siRNA on p38MAPK/NF-κB signaling pathway via suppressing NOX4/ROS pathway in LPS (1 μg/ml) -induced VSMCs ( n = 3). Notes: The same letters represented no significant differences, P > 0.05; and different letters indicated significant differences, P < 0.05

Article Snippet: We purchased recombinant SAA1 protein from ProSci incorporated (Poway, CA, USA).

Techniques: