IkappaBalpha (phospho-Tyr-42) Blocking Peptide
€155.00
In stock
SKU
ECM-IX1035
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.
Sequence: Phospho-IκBα (Tyr-42) synthetic peptide corresponds to amino acid residues around tyrosine 42 of human IκBα. This peptide sequence has low homology to other IκB proteins, but does have some homology to unrelated proteins that may have a conserved tyrosine phosphorylation motif.
Specificity: The peptide is specifically recognized by IκBα (Tyr-42) phospho-specific antibody (IP1031) in ELISA, and has been shown to block the reactivity of IP1031 during Western blot. In addition, the peptide is recommended for use in blocking IP1031 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Sequence: Phospho-IκBα (Tyr-42) synthetic peptide corresponds to amino acid residues around tyrosine 42 of human IκBα. This peptide sequence has low homology to other IκB proteins, but does have some homology to unrelated proteins that may have a conserved tyrosine phosphorylation motif.
Specificity: The peptide is specifically recognized by IκBα (Tyr-42) phospho-specific antibody (IP1031) in ELISA, and has been shown to block the reactivity of IP1031 during Western blot. In addition, the peptide is recommended for use in blocking IP1031 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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