OVA 257 264 peptide (SIINFEKL)– CAS: 138831-86-4
OVA 257-264 (H-2Kb) is an epitope of interest of the egg white albumen, ovalbumin. Ovalbumin is a glycoprotein that is sufficiently large and complex to be mildly immunogenic. Indeed, it has been demonstrated that Ovalbumin contains B-cell epitopes which are recognized by specific IgE antibodies and CD4 T cell epitopes restricted by the MHC I-Ad molecule in mice and by HLA-D molecule in human.
Applications of OVA 257-264
OVA 257-264 is used to stimulate T cells in PBMCs and to quantify peptide epitope specificity and IFN-γ releasing effector cells by ELISPOT assay. OVA 257-264 is also used to test new adjuvant in immunotherapeutic vaccine development. OVA 257-264 can form a stable hydrogel and stimulate a immune response. This reaction seems to be linked with OVA 257-264 property to self-assemble into a hydrogel.
SB-PEPTIDE offers the scrambled version of OVA 257-264 peptide (see section « OVA 257-264 scrambled »).
|Sequence : SIINFEKL|
|MW : 963.16 Da (C45H74N10O13)|
|Purity : > 95%|
|Counter-Ion : TFA Salts (see option TFA removal)|
|Delivery format : Freeze dried in propylene 2mL microtubes|
|Other names : 1p1z, 1p4l, HY-P1489, CAS: 138831-86-4|
|Peptide Solubility Guideline|
Bulk peptide quantities available – Carrier conjugation upon request
Made in France – For research use only
|Product catalog||Size||Price € HT||Price $ USD|
SB-PEPTIDE offers a wide range of antigens on catalog. Browse our antigen catalog to find out more.
Peptide pools are used as standards and controls to stimulate antigen-specific T-cells in functional T-cell assays. SB-PEPTIDE offers various control peptide pools including CEF control peptide pool, CMV pp65 peptide pool, Ovalbumin peptide pool.
SB-PEPTIDE can also prepare fully customized pools.
SB-PEPTIDE is a peptide manufacturing company offering a wide range of synthesis and engineering solutions.
SB-PEPTIDE offers non-conformational epitope mapping service. SB-PEPTIDE can synthesize the antigenic protein as a library of overlapped peptides (usually 15aa, 5aa overlap) and perform ELISA to determine the epitope.
1- Dersh D., Yewdell J. W., Wei J. Methods Mol Biol. (2019)
Antigen presentation by classical MHC class I molecules to CD8+ T cells is a central aspect of the adaptive immune response. Here, we describe methods to monitor antigen presentation using the model ovalbumin Kb-binding peptide, SIINFEKL. SIINFEKL genetically incorporated into viral or cellular source proteins can be used to precisely probe various aspects of antigen presentation, including the kinetics of peptide generation, MHC class I surface stability, and presentation efficiency following pharmacological and genetic manipulations including genome wide and high throughput drug screening.
2- Kamalov M., Kählig H., Rentenberger C., Mullner A. R. M., Peterlik H. and Becker C. F. W. Sci Rep. 9(1):2696 (2019)
Here we show that the well-known ovalbumin epitope SIINFEKL that is routinely used to stimulate ovalbumin-specific T cells and to test new vaccine adjuvants can form a stable hydrogel. We investigate properties of this hydrogel by a range of spectroscopic and imaging techniques demonstrating that the hydrogel is stabilized by self-assembly of the peptide into nanofibres via stacking of β-sheets. As peptide hydrogels are known to stimulate an immune response as adjuvants, the immunoactive properties of the SIINFEKL peptide may also originate from its propensity to self-assemble into a hydrogel. This finding requires a re-evaluation of this epitope in adjuvant testing.
3- Harms J. S., Khan M., Hall C., Splitter G. A., Homan E. J., Bremel R. D. and Smith A. J. Infect Immun. 86(7):e00281 (2018)
Brucella Peptide Cross-Reactive Major Histocompatibility Complex Class I Presentation Activates SIINFEKL-Specific T Cell Receptor-Expressing T Cells
Brucella spp. are intracellular pathogenic bacteria remarkable in their ability to escape immune surveillance and therefore inflict a state of chronic disease within the host. To enable further immune response studies, Brucella was engineered to express the well-characterized chicken ovalbumin (OVA). Surprisingly, we found that CD8 T cells bearing T cell receptors (TCR) nominally specific for the OVA peptide SIINFEKL (OT-1) reacted to parental Brucella-infected targets as well as OVA-expressing Brucella variants in cytotoxicity assays. Furthermore, splenocytes from Brucella-immunized mice produced gamma interferon (IFN-γ) and exhibited cytotoxicity in response to SIINFEKL-pulsed target cells.To determine if the SIINFEKL-reactive OT-1 TCR could be cross-reacting to Brucella peptides, we searched the Brucella proteome using an algorithm to generate a list of near-neighbor nonamer peptides that would bind to H2Kb Selecting five Brucella peptide candidates, along with controls, we verified that several of these peptides mimicked SIINFEKL, resulting in T cell activation through the « SIINFEKL-specific » TCR. Activation was dependent on peptide concentration as well as sequence. Our results underscore the complexity and ubiquity of cross-reactivity in T cell recognition. This cross-reactivity may enable microbes such as Brucella to escape immune surveillance by presenting peptides similar to those of the host and may also lead to the activation of autoreactive T cells.
4- Warger T. et al. Blood. 108(2):544-550 (2006)
Synergistic activation of dendritic cells by combined Toll-like receptor ligation induces superior CTL responses in vivo
Toll-like receptors (TLRs) are able to interact with pathogen-derived products and their signals induce the coordinated activation of innate and adaptive immune mechanisms. Dendritic cells (DCs) play a central role in these events. As the different TLRs are able to trigger MyD88/TRIF-dependent and -independent signaling pathways, we wondered if the simultaneous activation of these signaling cascades would synergize with respect to DC activation and induce superior cytotoxic T-lymphocyte (CTL) activity in vivo. We observed that indeed the combined activation of MyD88-dependent and -independent signaling induced by TLR7 and TLR3 ligands provoked a more rapid and more sustained bone marrow-derived DC (BMDC) activation with regard to the secretion of proinflammatory cytokines, like IL-6 and IL-12p70, and the expression of costimulatory molecules like CD40, CD70, and CD86. Furthermore, in the presence of combined TLR ligand-stimulated DCs, CD4(+) and CD8(+) T cells were insensitive toward the inhibitory effects of regulatory T cells. Most importantly, peptide-loaded BMDCs stimulated by TLR ligand combinations resulted in a marked increase of CTL effector functions in wild-type mice in vivo. Thus, our results provide evidence that unlocking the full potential of DCs by advanced activation protocols will boost their immunogenic potential and improve DC-based vaccination strategies.