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Rabbit Polyclonal Phospho-AIRE-1 (S156) antibody (STJ90618)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:5000;
Recommended protocols: check protocols
Click or hover above images to see image description for AIRE-1 (phospho Ser156) Polyclonal Antibody.
Check alternative names for the antibodyExpand
AIRE antibody, APECED antibody,|AIRE antibody|AIRE_HUMAN antibody|AIRE1 antibody|APECED antibody|APECED protein antibody|APS1 antibody|APSI antibody|Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein antibody|Autoimmune regulator antibody|Autoimmune regulator protein antibody|PGA1 antibody|Anti-AIRE antibody – ChIP Grade (ab13573)
SCBT cat No: sc-17986|sc-33188|sc-33189|sc-17985|
AIRE-1 (phospho Ser156) Polyclonal Antibody
|Catalogue No.|| |
Phospho-AIRE-1 (S156) Polyclonal Antibody detects endogenous levels of AIRE-1 protein only when phosphorylated at S156.
Synthesized phospho-peptide derived from AIRE-1 (phospho Ser156) at AA range 100-180
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:5000;
|Molecular weight|| |
AIRE-1 (phospho Ser156) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
AIRE-1 (phospho Ser156) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Autoimmune regulator antibody, Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein antibody, APECED protein antibody
|Protein names|| |
Autoimmune regulator , Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein , APECED protein
|Protein function|| |
Transcriptional regulator that binds to DNA as a dimer or as a tetramer, but not as a monomer. Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5′-. ATTGGTTA-3′ combined with a 5′-TTATTA-3′ box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at ‘Lys-4’, not phosphorylated at ‘Thr-3’ and not methylated at ‘Arg-2’. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Functions as a transcriptional activator and promotes the expression of otherwise tissue-specific self-antigens in the thymus, which is important for self tolerance and the avoidance of autoimmune reactions.
|Protein tissue specificity|| |
Widely expressed. Expressed at higher level in thymus (medullary epithelial cells and monocyte-dendritic cells), pancreas, adrenal cortex and testis. Expressed at lower level in the spleen, fetal liver and lymph nodes. Isoform 2 and isoform 3 seem to be less frequently expressed than isoform 1, if at all.
|Involvement in disease|| |
Autoimmune polyendocrine syndrome 1, with or without reversible metaphyseal dysplasia (APS1) [MIM:240300]: A rare disease characterized by the combination of chronic mucocutaneous candidiasis, hypoparathyroidism and Addison disease. Symptoms of mucocutaneous candidiasis manifest first, followed by hypotension or fatigue occurring as a result of Addison disease. APS1 is associated with other autoimmune disorders including diabetes mellitus, vitiligo, alopecia, hepatitis, pernicious anemia and primary hypothyroidism. . Note: The disease is caused by mutations affecting the gene represented in this entry. Most of the mutations alter the nucleus-cytoplasm distribution of AIRE and disturb its association with nuclear dots and cytoplasmic filaments. Most of the mutations also decrease transactivation of the protein. The HSR domain is responsible for the homomultimerization activity of AIRE. All the missense mutations of the HSR and the SAND domains decrease this activity, but those in other domains do not. The AIRE protein is present in soluble high-molecular-weight complexes. Mutations in the HSR domain and deletion of PHD zinc fingers disturb the formation of these complexes (PubMed:14974083). .
|Protein sequence and domain|| |
The L-X-X-L-L repeats may be implicated in binding to nuclear receptors. / The HSR domain is required for localization on tubular structures (N-terminal part) and for homodimerization. / Interacts via the first PHD domain with the N-terminus of histone H3 that is not methylated at ‘Lys-4’. Disruption of the first PHD domain has been shown to lead to reduced transcriptional activity and to localization of the protein mainly in the cytoplasm in small granules. While the PHD zinc fingers are necessary for the transactivation capacity of the protein, other regions also modulate this function. / Contains 1 HSR domain. / Contains 2 PHD-type zinc fingers. / Contains 1 SAND domain.
|Protein post-translational modifications|| |
Phosphorylated. Phosphorylation could trigger oligomerization.
|Protein cellular localization|| |
Nucleus / Cytoplasm
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St John’s Laboratory Ltd.
|Product type|| |
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