| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-90302-25ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF1563-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF1184-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-90303-25ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB1184-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF7510-SP | |||
![N/A Fetuin A/AHSG [HRP]](http://images.novusbio.com/fullsize/elisa/DATA_Fetuin_A_DFTA00_ELISA_684.jpg "N/A Fetuin A/AHSG [HRP]")
![N/A Fetuin A/AHSG [HRP]](http://images.novusbio.com/fullsize/elisa/DATA_Fetuin_A_DFTA00_ELISA_685.jpg)
![N/A Fetuin A/AHSG [HRP]](http://images.novusbio.com/fullsize/elisa/Fetuin_A_DFTA00_ELISA_99.jpg)
![<b>Independent Antibodies Validation. </b>Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human bone marrow, cerebral cortex, liver and lymph node using Anti-AHSG antibody NBP1-90302 (A) shows similar protein distribution across tissues to independent antibody NBP1-90303 (B).](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0009.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human bone marrow.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0014.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human liver.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0012.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human cerebellum shows moderate cytoplasmic positivity in a subset of Purkinje cells.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0015.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human cerebral cortex.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0010.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human kidney shows moderate extra-cellular positivity and moderate cytoplasmic positivity in cells in tubules.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0011.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90302] - Staining of human lymph node.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90302-img0013.jpg)
![Activation of AMPK downregulates high glucose-induced Fet-A expression in HepG2 cells.[A] HepG2 cells were incubated in a media containing either mannitol, low glucose or high glucose for 12 hours, and cell lysates/media were subjected to immunoblotting for Fet-A and pFet-A (n = 3). [B] HepG2 cells were incubated with either low- or high-glucose in the absence or presence of AICAR for 12 h and cell lysates were analyzed by Western blotting. The blots were analyzed with antibodies against Fet-A (n = 4). [C] HepG2 cells were incubated with increasing concentrations (0.5, 1, 2 mM) of AICAR for 12 h. Cell lysate or media were analyzed by Western blotting for indicated proteins (n = 3) and [D] level of Fet-A and pFet-A in media, as a ratio of GAPDH were expressed. [E] HepG2 cells were incubated in low or high glucose in the absence or presence of AICAR/metformin for 12 hours, and media was used to detect Fet-A by ELISA technique (n = 4). [F] Real-time gene expression analysis was carried out for Fet-A after AICAR and metformin treatment (n = 4). [G] HepG2 cells were incubated with AICAR/metformin in the presence or absence of Compound C, an AMPK inhibitor. Cell lysates were immunoblotted for pAMPK, Fet-A as well as p-Fet-A and [H] Fet-A levels, as a ratio to GAPDH are depicted (n = 4). Data are shown as Means ± SEM. P values were determined by one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). Data are representative of at least three independent experiments performed in replicates. * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-1212202581712.jpg "Activation of AMPK downregulates high glucose-induced Fet-A expression in HepG2 cells.[A] HepG2 cells were incubated in a media containing either mannitol, low glucose or high glucose for 12 hours, and cell lysates/media were subjected to immunoblotting for Fet-A and pFet-A (n = 3). [B] HepG2 cells were incubated with either low- or high-glucose in the absence or presence of AICAR for 12 h and cell lysates were analyzed by Western blotting. The blots were analyzed with antibodies against Fet-A (n = 4). [C] HepG2 cells were incubated with increasing concentrations (0.5, 1, 2 mM) of AICAR for 12 h. Cell lysate or media were analyzed by Western blotting for indicated proteins (n = 3) and [D] level of Fet-A and pFet-A in media, as a ratio of GAPDH were expressed. [E] HepG2 cells were incubated in low or high glucose in the absence or presence of AICAR/metformin for 12 hours, and media was used to detect Fet-A by ELISA technique (n = 4). [F] Real-time gene expression analysis was carried out for Fet-A after AICAR and metformin treatment (n = 4). [G] HepG2 cells were incubated with AICAR/metformin in the presence or absence of Compound C, an AMPK inhibitor. Cell lysates were immunoblotted for pAMPK, Fet-A as well as p-Fet-A and [H] Fet-A levels, as a ratio to GAPDH are depicted (n = 4). Data are shown as Means ± SEM. P values were determined by one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). Data are representative of at least three independent experiments performed in replicates. * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.")
![Activation of AMPK downregulates high glucose-induced Fet-A expression in HepG2 cells.[A] HepG2 cells were incubated in a media containing either mannitol, low glucose or high glucose for 12 hours, and cell lysates/media were subjected to immunoblotting for Fet-A and pFet-A (n = 3). [B] HepG2 cells were incubated with either low- or high-glucose in the absence or presence of AICAR for 12 h and cell lysates were analyzed by Western blotting. The blots were analyzed with antibodies against Fet-A (n = 4). [C] HepG2 cells were incubated with increasing concentrations (0.5, 1, 2 mM) of AICAR for 12 h. Cell lysate or media were analyzed by Western blotting for indicated proteins (n = 3) and [D] level of Fet-A and pFet-A in media, as a ratio of GAPDH were expressed. [E] HepG2 cells were incubated in low or high glucose in the absence or presence of AICAR/metformin for 12 hours, and media was used to detect Fet-A by ELISA technique (n = 4). [F] Real-time gene expression analysis was carried out for Fet-A after AICAR and metformin treatment (n = 4). [G] HepG2 cells were incubated with AICAR/metformin in the presence or absence of Compound C, an AMPK inhibitor. Cell lysates were immunoblotted for pAMPK, Fet-A as well as p-Fet-A and [H] Fet-A levels, as a ratio to GAPDH are depicted (n = 4). Data are shown as Means ± SEM. P values were determined by one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). Data are representative of at least three independent experiments performed in replicates. * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025825324.jpg)
![Activation of AMPK downregulates high glucose-induced Fet-A expression in HepG2 cells.[A] HepG2 cells were incubated in a media containing either mannitol, low glucose or high glucose for 12 hours, and cell lysates/media were subjected to immunoblotting for Fet-A and pFet-A (n = 3). [B] HepG2 cells were incubated with either low- or high-glucose in the absence or presence of AICAR for 12 h and cell lysates were analyzed by Western blotting. The blots were analyzed with antibodies against Fet-A (n = 4). [C] HepG2 cells were incubated with increasing concentrations (0.5, 1, 2 mM) of AICAR for 12 h. Cell lysate or media were analyzed by Western blotting for indicated proteins (n = 3) and [D] level of Fet-A and pFet-A in media, as a ratio of GAPDH were expressed. [E] HepG2 cells were incubated in low or high glucose in the absence or presence of AICAR/metformin for 12 hours, and media was used to detect Fet-A by ELISA technique (n = 4). [F] Real-time gene expression analysis was carried out for Fet-A after AICAR and metformin treatment (n = 4). [G] HepG2 cells were incubated with AICAR/metformin in the presence or absence of Compound C, an AMPK inhibitor. Cell lysates were immunoblotted for pAMPK, Fet-A as well as p-Fet-A and [H] Fet-A levels, as a ratio to GAPDH are depicted (n = 4). Data are shown as Means ± SEM. P values were determined by one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). Data are representative of at least three independent experiments performed in replicates. * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-121220258152611.jpg)
![Effect of fetuin-A (Fet-A) on insulin signaling and insulin mediated suppression of gluconeogenesis and glucose production in HepG2.[A] HepG2 cells were pre-treated with recombinant Fet-A in the presence or absence of insulin, and cell lysates were subjected to immunoblotting for AKT and GSK3 phosphorylation status (n = 3). [B] Quantified data of the ratio of cellular pAKT/GAPDH immunoblots (n = 3) and C] ratio of cellular pGSK/GAPDH immunoblots (n = 3) are shown. [D] HepG2 cells were serum-starved for 6 h, followed by treatment with dexamethasone (Dexa), insulin, or insulin and Fet-A for 12 h. Real-time gene expression of Pepck were analyzed (n = 4). [E] To analyze glucose production, HepG2 cells (n = 4) were treated with 0.5 μM dexamethasone and 0.1 mM 8-CTP-cAMP (Dex/cAMP), various concentrations of Fet-A or 100 nM insulin (Ins) in glucose free DMEM medium (pH 7.4 supplied with 20 mM sodium lactate and 2 mM sodium pyruvate) for 5 h. Glucose production was assayed by measuring glucose concentration in the medium as described previously [33]. Data are shown as Means ± SEM. P values were determined by one-way ANOVA followed by Tukey’s multiple comparison tests (A-C). Data are representative of at least three independent experiments performed in replicates. * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-1212202581185.jpg)
![AMPK activation downregulates Fet-A expression through p38 MAPK.[A] HepG2 were incubated with either low- or high-glucose in the absence or presence of AICAR for 12hr & used for WB analysis for ERK1/2 phosphorylation expression (n = 3). [B] HepG2 were incubated with different concentration of AICAR for 12 h & cell lysates were analyzed by WBting for ERK1/2, p38MAPK & JNK phosphorylation (n = 3). [C] were treated with p38 MAPK inhibitor [SB202190, n = 4] before treatment of AICAR for 12 hr. Cell lysate or media were analyzed by WBting for indicated proteins & [D] Fet-A levels, as a ratio to GAPDH were determined. [E] were treated with AMPK inhibitor [Comp C, n = 4] before treatment of AICAR for 12hr. Cell lysates were analyzed by WBting for phosphorylated p38 MAPK (pP38MAPK) & [F] pP38MAPK levels, as a ratio to GAPDH were determined. [G] Knockdown of p38 MAPK was performed using MAPK14 [p38 MAPK] small interfering RNA [siRNA] in HepG2 . Following AICAR treatment for 12 h, cell lysates were analyzed by WBting for expression of p38 MAPK, phosphorylated p38 MAPK, Fet-A, & pAMPK. [H] Efficiency of p38MAPK siRNA in HepG2 were determined by immunoblotting transfected for p38MAPK & levels were expressed as a ratio to GAPDH. [I] Effect of AICAR on Fet-A expression in scrambled or p38MAPK siRNA transfected were determined by expressing Fet-A levels, as a ratio to GAPDH (n = 4). [J] Effect of protein synthesis inhibitors, cycloheximide & puromycin, were compared with anisomycin, also a protein synthesis inhibitor, for effects on Fet-A & phosphorylated p38 MAPK expression (n = 3). Data are shown as Means ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). * Indicates p < 0.05. Image collected & cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-121220258141120.jpg)
![Activation of AMPK downregulates high glucose-induced Fet-A expression in HepG2 cells.[A] HepG2 cells were incubated in a media containing either mannitol, low glucose or high glucose for 12 hours, and cell lysates/media were subjected to immunoblotting for Fet-A and pFet-A (n = 3). [B] HepG2 cells were incubated with either low- or high-glucose in the absence or presence of AICAR for 12 h and cell lysates were analyzed by Western blotting. The blots were analyzed with antibodies against Fet-A (n = 4). [C] HepG2 cells were incubated with increasing concentrations (0.5, 1, 2 mM) of AICAR for 12 h. Cell lysate or media were analyzed by Western blotting for indicated proteins (n = 3) and [D] level of Fet-A and pFet-A in media, as a ratio of GAPDH were expressed. [E] HepG2 cells were incubated in low or high glucose in the absence or presence of AICAR/metformin for 12 hours, and media was used to detect Fet-A by ELISA technique (n = 4). [F] Real-time gene expression analysis was carried out for Fet-A after AICAR and metformin treatment (n = 4). [G] HepG2 cells were incubated with AICAR/metformin in the presence or absence of Compound C, an AMPK inhibitor. Cell lysates were immunoblotted for pAMPK, Fet-A as well as p-Fet-A and [H] Fet-A levels, as a ratio to GAPDH are depicted (n = 4). Data are shown as Means ± SEM. P values were determined by one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). Data are representative of at least three independent experiments performed in replicates. * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-1212202582410.jpg)
![AMPK activation downregulates Fet-A expression through p38 MAPK.[A] HepG2 were incubated with either low- or high-glucose in the absence or presence of AICAR for 12hr & used for WB analysis for ERK1/2 phosphorylation expression (n = 3). [B] HepG2 were incubated with different concentration of AICAR for 12 h & cell lysates were analyzed by WBting for ERK1/2, p38MAPK & JNK phosphorylation (n = 3). [C] were treated with p38 MAPK inhibitor [SB202190, n = 4] before treatment of AICAR for 12 hr. Cell lysate or media were analyzed by WBting for indicated proteins & [D] Fet-A levels, as a ratio to GAPDH were determined. [E] were treated with AMPK inhibitor [Comp C, n = 4] before treatment of AICAR for 12hr. Cell lysates were analyzed by WBting for phosphorylated p38 MAPK (pP38MAPK) & [F] pP38MAPK levels, as a ratio to GAPDH were determined. [G] Knockdown of p38 MAPK was performed using MAPK14 [p38 MAPK] small interfering RNA [siRNA] in HepG2 . Following AICAR treatment for 12 h, cell lysates were analyzed by WBting for expression of p38 MAPK, phosphorylated p38 MAPK, Fet-A, & pAMPK. [H] Efficiency of p38MAPK siRNA in HepG2 were determined by immunoblotting transfected for p38MAPK & levels were expressed as a ratio to GAPDH. [I] Effect of AICAR on Fet-A expression in scrambled or p38MAPK siRNA transfected were determined by expressing Fet-A levels, as a ratio to GAPDH (n = 4). [J] Effect of protein synthesis inhibitors, cycloheximide & puromycin, were compared with anisomycin, also a protein synthesis inhibitor, for effects on Fet-A & phosphorylated p38 MAPK expression (n = 3). Data are shown as Means ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). * Indicates p < 0.05. Image collected & cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025822246.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-1212202596163.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025963916.jpg)
![AMPK activation downregulates Fet-A expression through p38 MAPK.[A] HepG2 were incubated with either low- or high-glucose in the absence or presence of AICAR for 12hr & used for WB analysis for ERK1/2 phosphorylation expression (n = 3). [B] HepG2 were incubated with different concentration of AICAR for 12 h & cell lysates were analyzed by WBting for ERK1/2, p38MAPK & JNK phosphorylation (n = 3). [C] were treated with p38 MAPK inhibitor [SB202190, n = 4] before treatment of AICAR for 12 hr. Cell lysate or media were analyzed by WBting for indicated proteins & [D] Fet-A levels, as a ratio to GAPDH were determined. [E] were treated with AMPK inhibitor [Comp C, n = 4] before treatment of AICAR for 12hr. Cell lysates were analyzed by WBting for phosphorylated p38 MAPK (pP38MAPK) & [F] pP38MAPK levels, as a ratio to GAPDH were determined. [G] Knockdown of p38 MAPK was performed using MAPK14 [p38 MAPK] small interfering RNA [siRNA] in HepG2 . Following AICAR treatment for 12 h, cell lysates were analyzed by WBting for expression of p38 MAPK, phosphorylated p38 MAPK, Fet-A, & pAMPK. [H] Efficiency of p38MAPK siRNA in HepG2 were determined by immunoblotting transfected for p38MAPK & levels were expressed as a ratio to GAPDH. [I] Effect of AICAR on Fet-A expression in scrambled or p38MAPK siRNA transfected were determined by expressing Fet-A levels, as a ratio to GAPDH (n = 4). [J] Effect of protein synthesis inhibitors, cycloheximide & puromycin, were compared with anisomycin, also a protein synthesis inhibitor, for effects on Fet-A & phosphorylated p38 MAPK expression (n = 3). Data are shown as Means ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). * Indicates p < 0.05. Image collected & cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-121220259172019.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025855417.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025915564.jpg)
![AMPK activation downregulates Fet-A expression through p38 MAPK.[A] HepG2 were incubated with either low- or high-glucose in the absence or presence of AICAR for 12hr & used for WB analysis for ERK1/2 phosphorylation expression (n = 3). [B] HepG2 were incubated with different concentration of AICAR for 12 h & cell lysates were analyzed by WBting for ERK1/2, p38MAPK & JNK phosphorylation (n = 3). [C] were treated with p38 MAPK inhibitor [SB202190, n = 4] before treatment of AICAR for 12 hr. Cell lysate or media were analyzed by WBting for indicated proteins & [D] Fet-A levels, as a ratio to GAPDH were determined. [E] were treated with AMPK inhibitor [Comp C, n = 4] before treatment of AICAR for 12hr. Cell lysates were analyzed by WBting for phosphorylated p38 MAPK (pP38MAPK) & [F] pP38MAPK levels, as a ratio to GAPDH were determined. [G] Knockdown of p38 MAPK was performed using MAPK14 [p38 MAPK] small interfering RNA [siRNA] in HepG2 . Following AICAR treatment for 12 h, cell lysates were analyzed by WBting for expression of p38 MAPK, phosphorylated p38 MAPK, Fet-A, & pAMPK. [H] Efficiency of p38MAPK siRNA in HepG2 were determined by immunoblotting transfected for p38MAPK & levels were expressed as a ratio to GAPDH. [I] Effect of AICAR on Fet-A expression in scrambled or p38MAPK siRNA transfected were determined by expressing Fet-A levels, as a ratio to GAPDH (n = 4). [J] Effect of protein synthesis inhibitors, cycloheximide & puromycin, were compared with anisomycin, also a protein synthesis inhibitor, for effects on Fet-A & phosphorylated p38 MAPK expression (n = 3). Data are shown as Means ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (C-F). * Indicates p < 0.05. Image collected & cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025920296.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-1212202595219.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-121220259191717.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-121220259155621.jpg)
![Effect of AICAR or anisomycin treatment on Fet-A expression in Hep3B cells and primary rat hepatocytes.[A] Hep3B cells were incubated in low or high glucose media with or without AICAR for 12 hours, and cell lysates were subjected to immunoblotting for Fet-A and phosphorylated Fet-A (n = 4). [B] High glucose-mediated changes in Fet-A level in Hep3B cells was expressed as a ratio to GAPDH. [C] Hep3B cells were incubated with different concentration of AICAR for 12 h and cell lysates were analyzed by Western blotting for indicated proteins (n = 3). [D] Effect of AICAR on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH. [E] Hep3B cells were treated with various concentrations of anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK) and Fet-A expression (n = 3). [F] Effect of anisomycin on Fet-A level in Hep3B cells was expressed as a ratio of GAPDH [G] Primary rat hepatocytes were incubated with different concentration of AICAR for 12 h and cell lysate or media were analyzed by Western blotting for indicated proteins (n = 4). [H] Effect of AICAR in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH [I] primary rat hepatocytes were treated with anisomycin for 0.5 h to analyze phosphorylated p38 MAPK (pP38MAPK), Fet-A and p38MAPK expression (n = 4). [J] Effect of anisomycin in primary rat hepatocytes on Fet-A levels were expressed as ratio to GAPDH (n = 4). Data are shown as mean ± SEM. P values were determined accordingly by either by unpaired two-tailed test (E) or one-way ANOVA followed by Tukey’s multiple comparison tests (A-D). * Indicates p < 0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35522655), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/af1563_mouse-fetuin-a-ahsg-affinity-purified-polyclonal-ab-western-blot-12122025971811.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human bone marrow, cerebral cortex, liver and lymph node using Anti-AHSG antibody NBP1-90303 (A) shows similar protein distribution across tissues to independent antibody NBP1-90302 (B).](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0007.jpg "<b>Independent Antibodies Validation. </b>Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human bone marrow, cerebral cortex, liver and lymph node using Anti-AHSG antibody NBP1-90303 (A) shows similar protein distribution across tissues to independent antibody NBP1-90302 (B).")
![<b>Independent Antibodies Validation. </b>Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human cerebral cortex.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0014.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human kidney shows moderate extra-cellular positivity and moderate cytoplasmic positivity in cells in tubules.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0008.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human bone marrow.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0009.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human liver.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0010.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human stomach shows moderate positivity in extracellular matrix.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0011.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human skeletal muscle shows no positivity in myocytes as expected.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0012.jpg)
![Immunohistochemistry-Paraffin: Fetuin A/AHSG Antibody [NBP1-90303] - Staining of human lymph node.](http://images.novusbio.com/fullsize/Fetuin-A-AHSG-Antibody-Immunohistochemistry-Paraffin-NBP1-90303-img0013.jpg)
![N/A Fetuin A/AHSG [Biotin]](http://images.novusbio.com/fullsize/elisa/DATA_Fetuin_A_DY1563_ELISA_1675.jpg "N/A Fetuin A/AHSG [Biotin]")
![N/A Fetuin A/AHSG [Biotin]](http://images.novusbio.com/fullsize/elisa/DATA_Fetuin_A_DY1184_ELISA_1596.jpg "N/A Fetuin A/AHSG [Biotin]")
![N/A Fetuin A/AHSG [HRP]](http://images.novusbio.com/fullsize/elisa/DATA_Fetuin_A_MFTA00_ELISA_978.jpg "N/A Fetuin A/AHSG [HRP]")
![N/A Fetuin A/AHSG [HRP]](http://images.novusbio.com/fullsize/elisa/Fetuin_A_MFTA00_ELISA_422.jpg)
