Rabbit Recombinant Monoclonal FOXO3A antibody. Suitable for WB, Flow Cyt (Intra) and reacts with Human samples. Cited in 32 publications.
pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 9% PBS, 0.05% BSA
IP | WB | IHC-P | Flow Cyt (Intra) | |
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Human | Not recommended | Tested | Not recommended | Tested |
Rat | Not recommended | Predicted | Not recommended | Predicted |
Species | Dilution info | Notes |
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Species Human, Rat | Dilution info - | Notes - |
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Species Human | Dilution info 1/1000 - 1/10000 | Notes - |
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Species Rat | Dilution info - | Notes - |
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Species Human, Rat | Dilution info - | Notes - |
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Species Human | Dilution info - | Notes - |
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Species Rat | Dilution info - | Notes - |
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Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302).
FKHRL1, FOXO3A, FOXO3, Forkhead box protein O3, AF6q21 protein, Forkhead in rhabdomyosarcoma-like 1
Rabbit Recombinant Monoclonal FOXO3A antibody. Suitable for WB, Flow Cyt (Intra) and reacts with Human samples. Cited in 32 publications.
pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 9% PBS, 0.05% BSA
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
FOXO3A also known as FOXO3 or 1e2 is a transcription factor with a molecular weight of approximately 71 kDa. It belongs to the Forkhead box O family of proteins. This protein plays an important role in the regulation of transcription in response to oxidative stress and growth stimuli. FOXO3A is expressed in a variety of tissues including liver muscle and brain where it contributes to a wide range of cellular processes related to stress resistance and metabolism. Scientists frequently study FOXO3A using techniques like FOXO3A ELISA and apply FOXO3A anticuerpos in research to understand its function more intricately.
FOXO3A acts as a regulator of genes involved in cell cycle arrest apoptosis and DNA repair. It is not part of a simple protein complex but works closely with multiple factors to influence cellular homeostasis. Significantly FOXO3A controls the expression of Bcl-2 a protein important for cell survival and the protein p27 which is important for cell cycle control. FOXO3A's activity modulates cellular longevity and impacts stress responses highlighting its abundant biological functions.
FOXO3A integrates into the PI3K/AKT and the insulin signaling pathways both essential for cellular metabolism and proliferation control. In the PI3K/AKT pathway FOXO3A functionally links with proteins such as AKT and PTEN where its activity can be inhibited by AKT-mediated phosphorylation. In doing so it supports a balance between cell survival and apoptosis allowing the cell to adjust to growth conditions and external stressors effectively.
FOXO3A is linked to cancer and neurodegenerative diseases. In cancer alterations in FOXO3A activity or expression can affect tumor growth and resistance to oxidative stress often involving interactions with proteins like MDM2. Similarly in neurodegenerative disorders such as Alzheimer's disease FOXO3A modifies responses to oxidative damage potentially tied to proteins like Tau. Both instances highlight the role of FOXO3A as a versatile modulator that can influence the progression and management of various diseases.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
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Intracellular Flow Cytometry analysis of HeLa (human cervix adenocarcinoma) cells labeling FOXO3A with unpurified ab109629 at 1/150 dilution (10ug/ml) (red). Cells were fixed with 4% paraformaldehyde and permeabilised with 90% methanol. A Goat anti rabbit IgG (Alexa Fluorr® 488) (1/2000 dilution) was used as the secondary antibody. Rabbit monoclonal IgG (Black) was used as the isotype control, cells without incubation with primary antibody and secondary antibody (Blue) were used as the unlabeled control.
ab109629 was shown to react with FOXO3A in wild-type cells in Western blot with loss of signal observed in FOXO3 knockout cell lines. Wild-type and FOXO3 knockout cell lysates were subjected to SDS-PAGE. Membranes were blocked in 3 % milk in TBS-T (0.1 % Tween®) before incubation with ab109629 and Anti-GAPDH antibody [6C5] - Loading Control ab8245 (Mouse anti-GAPDH antibody [6C5]) overnight at 4 °C at a 1 in 1000 dilution and a 1 in 20000 dilution respectively. Blots were incubated with Goat anti-Rabbit IgG H&L (IRDye® 800CW) preabsorbed (Goat anti-Rabbit IgG H&L (IRDye® 800CW) preadsorbed ab216773) and Goat anti-Mouse IgG H&L (IRDye® 680RD) preabsorbed (Goat anti-Mouse IgG H&L (IRDye® 680RD) preadsorbed ab216776) secondary antibodies at 1 in 20000 dilution for 1 h at room temperature before imaging.
All lanes: Western blot - Anti-FOXO3A antibody [EPR1950] (ab109629) at 1/1000 dilution
Lane 1: Wild-type HEK-293T cell lysate at 20 µg
Lane 2: Western blot - Human FOXO3 (FOXO3A) knockout HEK-293T cell lysate (Human FOXO3 (FOXO3A) knockout HEK-293T cell lysate ab256922) at 20 µg
Lane 2: Western blot - Human FOXO3 (FOXO3A) knockout HEK-293T cell line (Human FOXO3 (FOXO3A) knockout HEK-293T cell line ab265069)
Lane 3: Wild-type HEK-293 cell lysate at 20 µg
Lane 4: Western blot - Human FOXO3 (FOXO3A) knockout HEK-293 cell lysate (Human FOXO3 (FOXO3A) knockout HEK-293 cell lysate ab261649) at 20 µg
Performed under reducing conditions.
Predicted band size: 71 kDa
Observed band size: 82 kDa
All lanes: Western blot - Anti-FOXO3A antibody [EPR1950] (ab109629) at 1/1000 dilution
Lane 1: MCF7 cell lysate at 10 µg
Lane 2: SH-SY5Y cell lysate at 10 µg
Predicted band size: 71 kDa
ab109629 was shown to recognize FOXO3A in wild-type HEK 293 cells as signal was lost at the expected MW in FOXO3 knockout cells. Additional cross-reactive bands were observed in the wild-type and knockout cells. Wild-type and FOXO3 knockout samples were subjected to SDS-PAGE. The membrane was blocked with 3% Milk. ab109629 and Anti-GAPDH antibody [6C5] - Loading Control ab8245 (Mouse anti-GAPDH loading control) were incubated overnight at 4°C at 1/1000 dilution and 1/20000 dilution respectively. Blots were developed with Goat anti-Rabbit IgG H&L (IRDye® 800CW) preabsorbed Goat anti-Rabbit IgG H&L (IRDye® 800CW) preadsorbed ab216773 and Goat anti-Mouse IgG H&L (IRDye® 680RD) preabsorbed Goat anti-Mouse IgG H&L (IRDye® 680RD) preadsorbed ab216776 secondary antibodies at 1/20000 dilution for 1 hour at room temperature before imaging.
All lanes: Western blot - Anti-FOXO3A antibody [EPR1950] (ab109629) at 1/1000 dilution
Lane 1: Wild-type HEK 293 whole cell lysate at 20 µg
Lane 2: FOXO3 knockout HEK-293 (Human epithelial cell line from embryonic kidney) whole cell lysate at 20 µg
Lane 2: Western blot - Human FOXO3 (FOXO3A) knockout HEK-293 cell line (Human FOXO3 (FOXO3A) knockout HEK-293 cell line ab260857)
Lane 3: HeLa (Human epithelial cell line from cervix adenocarcinoma) whole cell lysate at 20 µg
Lane 4: Jurkat (Human T cell leukemia cell line from peripheral blood) whole cell lysate at 20 µg
Predicted band size: 71 kDa
Image collected and cropped by CiteAb under a CC-BY license from the publication
FOXO3A western blot using anti-FOXO3A antibody [EPR1950] ab109629. Publication image and figure legend from Li, L., Lin, L., et al., 2020, J Cell Mol Med, PubMed 31881122.
ab109629 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab109629 please see the product overview.
Activation of p65 mediates PUMA induction in response to gilteritinib treatment. A, HCT116 cells were treated with gilteritinib for 24 h at indicated concentration. Indicated proteins were analysed by Western blot. B, HCT116 cells were treated with 50 nmol/L gilteritinib at indicated time‐points. Expression of p‐p65 (S536) and p65 was analysed by Western blot. C, HCT116 cells were transfected with either a control scrambled siRNA or a p65 siRNA for 24 h and then treated with 50 nmol/L gilteritinib for 24 h. p65 and PUMA expressions were analysed by Western blot. D, HCT116 cells were treated with 10 μmol/L BAY11‐7082 for 1 h, and then with 50 nmol/L gilteritinib for 24 h. Nuclear fractions were isolated from cells and analysed for p65 expression by Western blot. Lamin A/C and β‐actin, which are expressed in nucleus and cytoplasm, respectively, were used as controls for loading and fractionation. E, HCT116 cells were treated with 10 μmol/L BAY11‐7082 for 1 h, and then with 50 nmol/L gilteritinib for 24 h. The level of p‐p65 (S536) and PUMA was analysed by Western blot. F, Chromatin immunoprecipitation (ChIP) was performed using anti‐p65 antibody on HCT116 cells following gilteritinib (50 nmol/L) treatment for 12 h. The IgG was used to control for antibody specificity. PCR was carried out using primers surrounding the p65 binding sites in the PUMA promoter
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