NFAT2 Antibody (Mouse mAb) [P20K6]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:1000 FCM1:1000

Application
WB, IHC, FCM

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
101 kDa 75, 80, 90 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Human normal Hodgkin's lymphoma; Human normal tonsil tissue; HeLa cells; HAP1 cells; Jurkat cells; Recombinant Human NFAT2 protein (GST tag N-Terminus)
Negative Control

Datasheet & SDS

Biological Description

Specificity
NFAT2 Antibody (Mouse mAb) [P20K6] detects endogenous levels of total NFAT2 protein.

Clone
P20K6

Synonym(s)
NFAT2, NFATC, NFATC1, NF-ATc1, NFATc1, NFAT transcription complex cytosolic component, NF-ATc, NFATc

Background
NFAT2, also known as NFATc1, belongs to the calcium-regulated nuclear factor of activated T cells family alongside NFAT1, NFAT3, and NFAT4, sharing a conserved Rel-homology DNA-binding domain with these family members while carrying a distinct N-terminal regulatory domain containing calcineurin-docking motifs. NFAT2 resides in the cytoplasm in a heavily phosphorylated, transcriptionally inactive state under resting conditions, held there through interactions that mask its nuclear localization signal. Receptor engagement that triggers a sustained rise in intracellular calcium activates calmodulin, which in turn activates the calcium/calmodulin-dependent phosphatase calcineurin, composed of a catalytic calcineurin A subunit and a calcium-binding calcineurin B subunit. Calcineurin binds directly to NFAT2 and dephosphorylates multiple serine residues within its regulatory domain, exposing the nuclear localization signal and driving nuclear translocation. Within the nucleus, NFAT2 binds specific DNA motifs independently but achieves high-affinity, cooperative binding at composite regulatory elements through direct association with AP-1 (Fos-Jun) proteins, forming NFAT-AP-1 complexes that coordinately activate cytokine gene transcription, including interleukin-2, during antigen receptor-driven lymphocyte activation. NFAT2 and NFAT1 together are required for full T and B cell activation and cytokine production, with genetic loss of both factors abolishing this response. Continuous nuclear NFAT activity in the absence of AP-1 partner engagement instead drives an alternative transcriptional program associated with T cell anergy and functional exhaustion, distinguishing NFAT2 signaling outcomes based on cofactor availability rather than calcineurin activity alone. NFAT2 additionally regulates gene expression programs in osteoclast differentiation and cardiac hypertrophic growth, reflecting the pathway's broader tissue distribution beyond lymphocytes. Calcineurin-NFAT2 signaling is pharmacologically targeted by the immunosuppressants cyclosporine A and FK506, which block calcineurin phosphatase activity and prevent NFAT2 dephosphorylation. Dysregulated calcineurin-NFAT2 signaling is implicated in autoimmune disease pathogenesis, pathological cardiac remodeling, and tumor cell migration and invasion in select cancer contexts.

Background

NFAT2, also known as NFATc1, belongs to the calcium-regulated nuclear factor of activated T cells family alongside NFAT1, NFAT3, and NFAT4, sharing a conserved Rel-homology DNA-binding domain with these family members while carrying a distinct N-terminal regulatory domain containing calcineurin-docking motifs. NFAT2 resides in the cytoplasm in a heavily phosphorylated, transcriptionally inactive state under resting conditions, held there through interactions that mask its nuclear localization signal. Receptor engagement that triggers a sustained rise in intracellular calcium activates calmodulin, which in turn activates the calcium/calmodulin-dependent phosphatase calcineurin, composed of a catalytic calcineurin A subunit and a calcium-binding calcineurin B subunit. Calcineurin binds directly to NFAT2 and dephosphorylates multiple serine residues within its regulatory domain, exposing the nuclear localization signal and driving nuclear translocation. Within the nucleus, NFAT2 binds specific DNA motifs independently but achieves high-affinity, cooperative binding at composite regulatory elements through direct association with AP-1 (Fos-Jun) proteins, forming NFAT-AP-1 complexes that coordinately activate cytokine gene transcription, including interleukin-2, during antigen receptor-driven lymphocyte activation. NFAT2 and NFAT1 together are required for full T and B cell activation and cytokine production, with genetic loss of both factors abolishing this response. Continuous nuclear NFAT activity in the absence of AP-1 partner engagement instead drives an alternative transcriptional program associated with T cell anergy and functional exhaustion, distinguishing NFAT2 signaling outcomes based on cofactor availability rather than calcineurin activity alone. NFAT2 additionally regulates gene expression programs in osteoclast differentiation and cardiac hypertrophic growth, reflecting the pathway's broader tissue distribution beyond lymphocytes. Calcineurin-NFAT2 signaling is pharmacologically targeted by the immunosuppressants cyclosporine A and FK506, which block calcineurin phosphatase activity and prevent NFAT2 dephosphorylation. Dysregulated calcineurin-NFAT2 signaling is implicated in autoimmune disease pathogenesis, pathological cardiac remodeling, and tumor cell migration and invasion in select cancer contexts.

References
https://pubmed.ncbi.nlm.nih.gov/15928679/ https://pubmed.ncbi.nlm.nih.gov/32210952/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%