Active, pure human recombinant enzyme
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NF-κB (p50) (human, recombinant)

Item No. 10009818

Technical Information
Synonyms
  • NF-κB1
  • Nuclear Factor-κB (p50)
Purity
≥55%
Source
Human recombinant GST-tagged protein expressed in E. coli
Amino Acids
1-433 (full length)
MW
74.5 kDa
A solution in PBS, pH 7.4, containing 5 mM DTT and 20% glycerol
Applications
(+) WB
UniProt Accession №
P19838
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    The NF-κB/Rel family of transcription factors is comprised of several structurally-related proteins that form homodimers and heterodimers and include p50/p105, p52/p100, RelA (p65), and c-Rel/NF-κB 1. Members of this family are responsible for regulating over 150 target genes, including the expression of inflammatory cytokines, chemokines, immunoreceptors, and cell adhesion molecules. Because of this, NF-κB has often been called a 'central mediator of the human immune response.2 Acting as dimers, these transcription factors bind to 10 base pair DNA sequences, collectively called κB sites thereby regulating expression of target genes. The most common Rel/NF-κB dimer in mammals contains (p50)-RelA (p50/p65) heterodimers and is called NF-κB. The importance of Rel/NF-κB transcription factors in human inflammation and certain diseases makes them attractive targets for potential therapeutics.3,4,5

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Gilmore, T.D. The Rel/NF-κB signal transduction pathway: Introduction. Oncogene 18, 6842-6844 (1999).

    2. Pahl, H.L. Activators and target genes of Rel/NF-κB transcription factors. Oncogene 18, 6853-6866 (1999).

    3. Gilroy, D.W., Lawrence, T., Perretti, M., et alInflammatory resolution: New opportunities for drug discovery. Nat. Rev. Drug Discov. 3, 401-416 (2004).

    4. Maeda, S., Hsu, L.C., Liu, H., et alNod2 mutation in Crohn’s disease potentiates NF-κB activity and IL-1β processing. Science 307, 734-738 (2005).

    5. Clark, A.G., and Debnam, P. Inhibition of glutathione S-transferases from rat liver by S-nitroso-L-glutathione. Biochem. Pharmacol. 37, 3199-3201 (1988).