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The pan HLA DR-binding epitope (PADRE) has been proposed as a simple carrier epitope suitable for use in the development of synthetic and recombinant vaccines.
T cell epitopes are presented on the surface of antigen-presenting cells by MHC molecules. T cell epitopes presented by MHC class I molecules are typically peptides between 8 and 11 amino acids in length and exhibiting MHC-specific sequence motifs. These antigenic peptides are derived from non-structural and structural proteins through proteolysis in the cytosolic compartment. Peptide-MHC-I complexes are then transported to the cell surface of antigen presenting cells and are recognised by CD8+ cytotoxic T lymphocytes (CTL). This interaction induces the differentiation of CTLs. Activated CTL lyse the infected cell, secrete cytokines, and proliferate. This mechanism ensures that cells infected by viruses or intracellular bacteria or cancer cells can be detected, since pathogen or cancer-specific MHC peptide complexes are displayed on the cell surface. CTL can recognise such abnormal cells and eliminate them. The genes of MHC I and II molecules are polymorphic. Each MHC allele has a distinct peptide binding motif which favours certain amino acid anchor residues at defined sequence positions.
Purity: >95% (HPLC, ESI-MS)
Lyophilized white powder
Sicherheits Hinweise / Safety
Klassifizierungen / Classificationeclass-Nr: 34-16-04-90
Dokumente - Protokolle - Downloads
Here you will find information and further literature on PADRE - AKFVAAWTLKAAA. For further documents (certificates with additional lot numbers, safety data sheets in other languages, further product information) please contact Genaxxon biosience at: firstname.lastname@example.org or phone: +49 731 3608 123.