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Cat.No.: F3889
| Dilution |
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| Application |
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| WB, IHC, IF, FCM |
| Reactivity |
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| Human |
| Source |
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| Mouse Monoclonal Antibody |
| Storage Buffer |
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| PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 |
| Storage (from the date of receipt) |
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| -20°C (avoid freeze-thaw cycles), 2 years |
| Predicted MW Observed MW |
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| 100 kDa 150 kDa,62 kDa |
| *Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. |
| Positive Control | Human spleen tissue; Human colon carcinoma tissues; Human tonsil; Jurkat cells; HeLa cells; HeLa cells (staurosporine, 1uM, 3 h); U251 Cells; MCF-7 cells |
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| Negative Control | HeLa cells |
| Specificity |
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| NFAT1 Antibody [L23B6] detects endogenous levels of total NFAT1 protein. |
| Clone |
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| L23B6 |
| Synonym(s) |
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| NFAT1; NFATP; NFATC2; NF-ATc2; NFATc2; NFAT pre-existing subunit; T-cell transcription factor NFAT1; NF-ATp |
| Background |
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| NFAT1, also known as Nuclear Factor of Activated T-cells 1 or NFATc2, is a transcription factor from the NFAT family (NFAT1-5) predominantly found in immune cells such as T lymphocytes, as well as in neuronal tissues. It regulates gene expression in response to calcium signaling. NFAT1 contains an intrinsically disordered N-terminal regulatory domain with serine-rich regions for phosphorylation, a central Rel-homology DNA-binding domain with an immunoglobulin-like fold that recognizes GGAAA consensus sequences, and a C-terminal transactivation domain that enables cooperative interactions with partners like AP-1 and GATA. In its resting state, NFAT1 remains hyperphosphorylated in the cytoplasm. Upon antigen receptor engagement or calcium influx, the phosphatase calcineurin dephosphorylates NFAT1 at key serine residues, exposing nuclear localization signals. This allows NFAT1 to translocate to the nucleus, bind DNA, and activate transcription of genes such as IL-2 and TNF-α. NFAT1 is central to the Ca2+/calcineurin-NFAT signaling pathway, driving T-cell activation, Th1/Th2 differentiation, cytokine production, and T-cell proliferation and differentiation. In neurons, NFAT1 contributes to axon growth and survival. NFAT1 also forms complexes with AP-1 (c-Fos/Jun) on composite promoter elements, allowing for fine-tuned control of immune responses. Deficiency in NFAT1 leads to hyperproliferation, autoimmunity, and reduced IL-2 expression in animal models. Dysregulated NFAT1 activity is implicated in autoimmune diseases such as rheumatoid arthritis due to excessive cytokine production, and in cancers like lymphomas and diffuse large B-cell lymphoma, where it promotes proliferation through cyclin deregulation. |
| References |
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