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ova peptide sequence OVA257-264 peptide

Published October Oct 17, 2026 7:47 PM

In the realm of biochemical research and model antigen studies, the OVA peptide sequence stands out as a fundamental tool for those exploring cellular responses. As someone who frequently interacts with high-purity laboratory reagents, I have found that understanding the structural nuances of ovalbumin-derived peptides is essential for precise experimental design. Whether you are working with the classic SIINFEKL epitope or longer sequences, the specificity of these molecules is what makes them indispensable in modern laboratory settings.

The Significance of OVA (257-264)

Perhaps the most recognized sequence in this category is the OVA peptide (257-264), often referred to as SIINFEKL. This octameric peptide is a primary example of a class I (Kb)-restricted peptide epitope of OVA. When I evaluate these reagents, I look for high-purity synthesis, typically provided as H-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu-OH, which is essential for ensuring consistent results.

The OVA257-264 peptide (or SL8) is frequently used as an H-2Kb-restricted OVA class I epitope. Its molecular formula, C45H74N10O13, and a mo OVA Antigens | InvivoGen lecular weight of approximately 963.13 g/mol, define its chemical profile. This is a class I (Kb)-restricted peptide epitope of OVA, an octameric peptide from ovalbumin presented by the class I MHC molecule, H-2Kb. Because SIINFEKL is one peptide sequence of the OVA used frequently in standardized assays, it is often the first point of reference for researchers investigating antigen presentation kinetic OVA, HEL, and HA peptides were expressed on human IgG3 molecules by substituting the L6 loop in the CH1 domain. The loops in the domain are numbered  s.

Exploring the OVA (323-339) Peptide

While the 257-264 fragment is dominant for class I studies, the OVA 323-339 peptide serves a different, equally critical role as a key H-2b-restricted OVA class II epitope. This longer sequence, represented by the amino acids ISQAVHAAHAEINEAGR, is widely cited in literature regarding Ovalbumin protein Ova (323-339).

When sourcing this OVA peptide (323-339), ovalbumin reagent, I prioritize products with a purity level of >95%. The molecular weight for this specific chain is approximately 1773.9 Ovalbumin 1 g/mol, with a formula of C74H120N26O25. It is fascinating to note that researchers often utilize ISQAVHAAHAEINEAGR-NH2 variants to adjust solubility and stability for specific OVA (323-339) experimental architectures.

Comparative Analysis and Biological Context

The versatility of the OVA protein, which constitutes about 55% of egg white protein, allows for the extraction of various epitopes. Beyond the primary two discussed, other regions such as aa 243-248, aa 127-136, and even the OVA peptide of amino acid numbers 55-62 are documented in specialized studies.

It is also noteworthy that Ovalbumin displays sequence and structural homology to the serpin superfamily, though it does not function as a serine protease inhibitor. This unique structural nature explains why OVA, HEL, and HA peptides were expressed on human IgG3 molecul OVA peptide es in various structural biology studies to further probe the functionality of these epitopes.

Practical Considerations for Researchers

When selecting these reagents, Identification of epitopes in ovalbumin that provide insights for I always verify the sequence and the specific epitope ID (such as ID 28676 for the 323-339 variant). Whether you are analyzing OVA (ovalbumin) peptide residues 257 to 280 or looking into OVA peptide 36–43 for comparative protein analysis, the precision of the peptide synthesis is paramount.

For those conducting experiments involving Ova peptide (257-264) or the Ova (323-339) variant, it is highly recommended to consult the UniProt ID (P01012) to ensure the alignment of the peptide sequence with the target protein structure. Proper storage and handling of these peptide sequences—usually at -20°C in lyophilized form—will maintain the integrity of the ovalbumin epitopes throughout your research lifecycle.

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