|Other Names||NF-kappa-B inhibitor alpha, I-kappa-B-alpha, IkB-alpha, IkappaBalpha, Major histocompatibility complex enhancer-binding protein MAD3, NFKBIA, IKBA, MAD3, NFKBI|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||IKBA, MAD3, NFKBI|
|Function||Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.|
|Cellular Location||Cytoplasm. Nucleus. Note=Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export.|
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Provided below are standard protocols that you may find useful for product applications.
NFKB1 or NFKB2 is bound to REL, RELA, or RELB to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, IKBKB) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).
Szamosi,T., Dig. Dis. Sci. (2008)Fan,C., J. Biol. Chem. 278 (3), 2072-2080 (2003)Tojima,Y., Nature 404 (6779), 778-782 (2000)Gil,J., Oncogene 19 (11), 1369-1378 (2000)Hay,R.T., Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354 (1389), 1601-1609(1999)
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