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Ovalbumin (OVA) is a phosphoglucoprotein with a molecular weight of 45 kDa, which is one of the most plentiful proteins (up to 54% w/w) and is deemed to be one of the major anaphylactogens. Its sequence (containing 385 amino acids) contains 6 cysteines. There is a disulfide bond between Cys73 and Cys120. Asn292 has glycosylation sites. Ser68 and Ser344 have two phosphorylation sites. Like many other sensitized proteins, OVA partly oppose the hydrolysis of pepsinum and trypsin, which may be conducive to its ability to sensibilization or induce anaphylactic reactions. OVA (323-339) peptide sequence is H-2b restricted OVA class II epitope. OVA peptide (257-264) is a class I (Kb) restrictive peptide epitope of OVA. OVA is an octamer peptide from ovalbumin presented by class I MHC molecule H-2Kb.
Mechanism of action
The great majority of the residues required to combine chicken OVA (323-339) peptide to I-A (d) MHC II protein are included in the shorter 325-336 peptide. Two OVA peptides, OVA (323-335) and OVA (325-336), were found to disaggregate from I-A (d) in diverse kinetics. When asparagine was used to replace the His 81 residue of MHC beta chain, the dissociation rates of both peptides increased. In this structure, the residue of beta H81 forms hydrogen bonds with the main carbonyl group of I323. If the OVA (325-336) peptide is also combined with the temporary storage, there is no comparable hydrogen-bonded receptor in the side chain of beta H81 to explain the susceptibility of the peptide to beta H81 substitution. The OVA (323-335) peptide bound in the temporary storage does not activate T-cell hybridoma activated by OVA (325-336) bound in the alternating temporary storage. A single peptide can bind MHC peptides in alternating temporary storages to produce different T cell responses.
Application of OVA peptide
OVA peptide (323-339) delegates a T and B cell epitope of OVA, which is significant in the production and development of forthwith hypersensitivity responses in BALB/c mouse. OVA (323-339) peptide showed that causing death CPXV communication decreased the proliferation of DO11.10 T cells in lung-associated lymph nodes, but still cell multiplication during sublethal infection.
1. Mine, Y., & Yang, M. (2008). Recent advances in the understanding of egg allergens: basic, industrial, and clinical perspectives. Journal of Agricultural and Food Chemistry, 56 (13), 4874-4900.
2. Ruiter, B., & Shreffler, W. G. (2012, September). Innate immunostimulatory properties of allergens and their relevance to food allergy. In Seminars in immunopathology (Vol. 34, No. 5, pp. 617-632). Springer-Verlag.