Ikappa B alpha (pSer32,pSer36) antibody
Western Blotting (WB), Immunoprecipitation (IP)
|6 references available|
|Quantity||50 µg (0.5 mg/ml)|
|Price||Product not available in this region.|
|Immunogen||Phosphorylated Human IkappaBalpha aa. 32, 36|
|Description||NF-kappaB is a transcription factor which is a member of the mammalian NF-kappaB/Rel family of proteins. Members of this family are involved in the regulation of cell proliferation, immune function, as well as development. NF-kappaB is normally found in the cytoplasm and remains in an inactive state by its association with an inhibitory protein, IkappaB. Stimulation of NF-kappaB by a variety of inducers causes the degradation of IkappaBs and translocation of NF-kappaB to the nucleus and activation of the target gene. IkappaBalpha is a member of the IkappaB family of proteins including IkappaBbeta, IkappaBgamma, IkappaBepsilon, Bcl-3, and the precursors of NF-kappaB1 (p105), and NF-kappaB2 (p100). IkappaBalpha is the best characterized member of the family and has been shown to contain three different structural domains: an N-terminal region, an amino acid internal region containing ankyrin repeats, and a C-terminal region containing a PEST domain. In resting cells, IkappaBalpha binds to and maintains NF-kappaB in the cytoplasm by blocking the nuclear localization sequences of NF-kappaB. In the response to an extracellular signal, IkappaBalpha is phosphorylated and subsequently degraded via the ubiquination-proteasome pathway, allowing NF-kappaB to translocate to the nucleus. Once in the nucleus, NF-kappaB can induce the transcription of IkappaBalpha thereby renewing the cycle so that IkappaBalpha can form a complex with NF-kappaB and maintains it in its cytoplasmic location. IkappaBalpha -/- mice have been shown to die soon after birth and show an increased level of NF-kappaB activity. Furthermore, in Hodgekin's lymphoma (HL) a high constitutive level of NF-kappaB has been reported in samples in which clonal deleterious mutations were detected in the IkappaBalpha gene. The exact role that IkappaBalpha plays in the pathogenic process which leads to HL remains to be elucidated. IkappaBalpha migrates at ~42 kDa in SDS/PAGE, while the deduced molecular weight based upon its cDNA sequence is ~36 kDa (SWISS PROT Accession number P25963). The antibody specifically recognizes the phosphorylated form of human IkappaBalpha, it does not recognize the unphosphorylated form. A synthetic peptide containing phosphorylated serines at amino acid residues of 32 and 36 of human IkappaBalpha was used as the immunogen.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Related Products: ABIN967389
|Application Notes||Applications include western blot analysis (0.5-2.0 µg/ml). Additional applications not tested include immunoprecipitation. Treatment of Jurkat T cells with TNF-alpha is recommended as a positive control.|
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at 4°C.|
|Restrictions||For Research Use only|
Beg, Sha, Bronson et al.: "Constitutive NF-kappa B activation, enhanced granulopoiesis, and neonatal lethality in I kappa B alpha-deficient mice." in: Genes & development, Vol. 9, Issue 22, pp. 2736-46, 1995 (PubMed).
Klement, Rice, Car et al.: "IkappaBalpha deficiency results in a sustained NF-kappaB response and severe widespread dermatitis in mice." in: Molecular and cellular biology, Vol. 16, Issue 5, pp. 2341-9, 1996 (PubMed).
Baldwin: "The NF-kappa B and I kappa B proteins: new discoveries and insights." in: Annual review of immunology, Vol. 14, Issue 8, pp. 649-83, 1996 (PubMed).
Verma, Stevenson: "IkappaB kinase: beginning, not the end." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 22, pp. 11758-60, 1997 (PubMed).
Jungnickel, Staratschek-Jox, Bräuninger et al.: "Clonal deleterious mutations in the IkappaBalpha gene in the malignant cells in Hodgkin's lymphoma." in: The Journal of experimental medicine, Vol. 191, Issue 2, pp. 395-402, 2000 (PubMed).
Karin, Ben-Neriah: "Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity." in: Annual review of immunology, Vol. 18, Issue 8, pp. 621-63, 2000 (PubMed).