bsm-70530M

DATASHEET

Host: Mouse

Target Protein: Integrin β4 (Cytoplasmic region)

Specificity: This antibody detects a 200kDa* protein corresponding to the molecular mass of Integrin β4 on SDS-PAGE immunoblots of human A431 cells. This sequence is found in all three Integrin β4 isoforms and has 90% homology with rat and mouse Integrin β4.

Clonality: Monoclonal

Isotype: IgG1

Swiss Prot: P16144

Source: Clone M126 was generated from a recombinant protein containing amino acid residues in the cytoplasmic region of human Integrin β4.

Purification: Purified by Protein A.

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

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.