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Anti-IκBα (Tyr-305), Phosphospecific Antibody

     
  •  - Anti-IκBα (Tyr-305), Phosphospecific Antibody AN1817
    Western blot analysis of A431 cells treated with pervanadate (1 mM) for 30 min. Blots were probed with anti-IκBα (lane 1), anti-IκBα (Tyr-42) (IP1031; lanes 2-5), or anti-IκBα (Tyr-305) (IP1041; lanes 6-9). In some lanes, the antibodies were used in the absence (lane 2 & 6) or presence of IκBα (Tyr-42) (lane 3 & 8) or IκBα (Tyr-305) (lane 4 & 7) blocking peptides, or BSA conjugated to phospho-tyrosine (lane 5 & 9).
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Product Information
Primary Accession P25963
Reactivity Bovine
Host Rabbit
Clonality Rabbit Polyclonal
Isotype IgG
Calculated MW 35609 Da
Additional Information
Gene ID 4792
Other Names IkB, MAD3, IkappaBalpha, NFkappaB inhibitor IkBa
Target/Specificity The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins. Activation of IκBα occurs through both serine and tyrosine phosphorylation events. Activation through phosphorylation at Ser-32 and Ser-36 is followed by proteasome-mediated degradation, resulting in the release and nuclear translocation of active NF-κB. This pathway of IκBα regulation occurs in response to various NF-κB-activating agents, such as TNFα, interleukins, LPS, and irradiation. An alternative pathway for IκBα regulation occurs through tyrosine phosphorylation of Tyr-42 and Tyr-305. Tyr-42 is phosphorylated in response to oxidative stress and growth factors. This phosphorylation can lead to degradation of IκBα and NF-κB-activation. In contrast, Tyr-305 phosphorylation by c-Abl has been implicated in IκBα nuclear translocation and inhibition of NF-κB-activation. Thus, tyrosine phosphorylation of IκBα may be an important regulatory mechanism in NF-κB signaling.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-IκBα (Tyr-305), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
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Background

The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins. Activation of IκBα occurs through both serine and tyrosine phosphorylation events. Activation through phosphorylation at Ser-32 and Ser-36 is followed by proteasome-mediated degradation, resulting in the release and nuclear translocation of active NF-κB. This pathway of IκBα regulation occurs in response to various NF-κB-activating agents, such as TNFα, interleukins, LPS, and irradiation. An alternative pathway for IκBα regulation occurs through tyrosine phosphorylation of Tyr-42 and Tyr-305. Tyr-42 is phosphorylated in response to oxidative stress and growth factors. This phosphorylation can lead to degradation of IκBα and NF-κB-activation. In contrast, Tyr-305 phosphorylation by c-Abl has been implicated in IκBα nuclear translocation and inhibition of NF-κB-activation. Thus, tyrosine phosphorylation of IκBα may be an important regulatory mechanism in NF-κB signaling.

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$ 329.00
Cat# AN1817
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