Product Pathways - NF-kB Signaling
IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) (Sepharose Bead Conjugate) #4078
|IP||H M R Mk B Pg GP||Endogenous||39||Mouse IgG1|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey B=Bovine Pg=Pig GP=Guinea Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) detects endogenous levels of total IκBα protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a GST-IκBα fusion protein corresponding the amino-terminus of human IκBα.
Western blot analysis of IP reaction supernatant (10% input, lanes 1, 3, 5, and 7) and immunoprecipitate (lanes 2, 4, 6, and 8) of wild-type mouse embryonic fibroblast (WT MEF) lysate using Protein G beads alone (lanes 1 and 2) or in combination with IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) #4814 (lanes 5 and 6), Mouse IgG (Sepharose Bead Conjugate) #3420 (lanes 3 and 4), and IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) (Sepharose Bead Conjugate) #4078 (lanes 7 and 8). The blot was probed using IκBα (44D4) Rabbit mAb #4812.
This Cell Signalinling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated sepharose beads. IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) (Sepharose Bead Conjugate) is useful for the immunoprecipitation of IκBα protein.
The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).
- Baeuerle, P.A. and Baltimore, D. (1988) Science 242, 540-6.
- Beg, A.A. and Baldwin, A.S. (1993) Genes Dev 7, 2064-70.
- Finco, T.S. et al. (1994) Proc Natl Acad Sci USA 91, 11884-8.
- Brown, K. et al. (1995) Science 267, 1485-8.
- Brockman, J.A. et al. (1995) Mol Cell Biol 15, 2809-18.
- Traenckner, E.B. et al. (1995) EMBO J 14, 2876-83.
- Chen, Z.J. et al. (1996) Cell 84, 853-62.
- Karin, M. and Ben-Neriah, Y. (2000) Annu Rev Immunol 18, 621-63.
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For Research Use Only. Not For Use In Diagnostic Procedures.