SN50, also named NF-KB inhibitor, is a synthetic peptide corresponding to the nuclear localization sequence of NF-KB p105 subunit (also known as p50) appended to a hydrophobic sequence to facilitate import into living cells. It blocks the nuclear import of p105 in cells treated with activators of NF-KB signaling, including LPS and TNF-Alpha.
CAT No: R1845
CAS No:213546-53-3
Synonyms/Alias:SN50;213546-53-3;NFkappaB Inhibitor;NF-kappaB Inhibitor, SN50;H-ALA-ALA-VAL-ALA-LEU-LEU-PRO-ALA-VAL-LEU-LEU-ALA-LEU-LEU-ALA-PRO-VAL-GLN-ARG-LYS-ARG-GLN-LYS-LEU-MET-PRO-OH;NF-kappaB SN50;SN50 trifluoroacetate salt;AAVALLPAVLLALLAPVQRKRQKLMP;CHEBI:195371;SN 50;SN-50;H-AAVALLPAVLLALLAPVQRKRQKLMP-OH;AKOS040738511;DA-57948;FN109704;G12952;Nuclear Factor NF-KB Inhibitor SN50 trifluoroacetate salt;H-Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu-Ala-Pro-Val-Gln- Arg-Lys-Arg-Gln-Lys-Leu-Met-Pro-OH; H-AAVALLPAVLLALLAPVQR KRQKLMP-OH;L-Ala-L-Ala-L-Val-L-Ala-L-Leu-L-Leu-L-Pro-L-Ala-L-Val-L-Leu-L-Leu-L-Ala-L-Leu-L-Leu-L-Ala-L-Pro-L-Val-L-Gln-L-Arg-L-Lys-L-Arg-L-Gln-L-Lys-L-Leu-L-Met-L-Pro;L-alanyl-L-alanyl-L-valyl-L-alanyl-L-leucyl-L-leucyl-L-prolyl-L-alanyl-L-valyl-L-leucyl-L-leucyl-L-alanyl-L-leucyl-L-leucyl-L-alanyl-L-prolyl-L-valyl-L-glutaminyl-L-arginyl-L-lysyl-L-arginyl-L-glutaminyl-L-lysyl-L-leucyl-L-methionyl-L-proline;
SN50 is a synthetic peptide inhibitor derived from the nuclear localization sequence of the NF-κB p50 subunit, recognized for its capacity to selectively block the nuclear translocation of NF-κB. As a cell-permeable peptide, SN50 has become a pivotal molecular tool in the study of NF-κB signaling pathways, enabling researchers to dissect the regulatory mechanisms underlying inflammation, immune responses, and gene expression. Its biochemical design allows for targeted interference with protein-protein interactions critical to the activation of transcription factors, making it highly relevant in molecular and cellular biology research focused on intracellular signaling dynamics.
Signal transduction studies: SN50 is widely utilized to investigate NF-κB-mediated signal transduction pathways. By competitively inhibiting the nuclear import of NF-κB complexes, it provides a precise means to evaluate the downstream effects of pathway inhibition in response to various stimuli. Researchers employ this peptide to dissect the temporal dynamics and specificity of NF-κB activation in diverse cell types, thereby clarifying the role of this transcription factor in cellular responses to stress, cytokines, and pathogenic challenges.
Gene regulation analysis: The peptide is instrumental in experiments designed to elucidate the impact of NF-κB on gene transcription. By impeding the nuclear entry of NF-κB, SN50 enables the assessment of transcriptional changes and the identification of NF-κB-dependent genes. Its use facilitates detailed studies on promoter activity, chromatin remodeling, and the interplay between transcription factors, supporting the mapping of complex gene regulatory networks in inflammation, apoptosis, and differentiation.
Immunological research: SN50 serves as a valuable tool in studies exploring immune cell activation and cytokine production. The selective blockade of NF-κB nuclear translocation allows for the examination of specific signaling events that govern immune responses. This approach is particularly relevant in the context of macrophage, lymphocyte, and dendritic cell function, where the peptide helps delineate the contribution of NF-κB to immune modulation and the development of inflammatory phenotypes.
Cellular stress and apoptosis investigations: Researchers leverage SN50 to interrogate the role of NF-κB in cellular stress responses and programmed cell death. By modulating NF-κB activity, the peptide aids in distinguishing between pro-survival and pro-apoptotic signaling cascades under conditions such as oxidative stress, DNA damage, or exposure to cytotoxic agents. These studies provide crucial insights into cell fate decisions and the molecular determinants of stress resistance.
Peptide-based inhibitor studies: As a model cell-permeable peptide inhibitor, SN50 is frequently employed in the development and validation of novel peptide-based tools targeting intracellular protein interactions. Its well-characterized mechanism of action serves as a benchmark for designing next-generation inhibitors that modulate transcription factor activity or disrupt nuclear transport processes. This application supports advances in chemical biology and the rational design of molecular probes for intracellular signaling research.
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