Ova (323-339) – ISQAVHAAHAEINEAGR – CAS 92915-79-2
Ovalbumin protein
Ova (323-339) is an epitope of interest of the egg white albumen,which is widely used in allergy research. 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 (323-339)
Ova (323-339) allows to study bindings of class II MHC-peptide and T-cell activation in PBMCs by ELISPOT assays. In fact,this method quantifies peptide epitope specificity and IFN-γ releasing effector cells. It has been shown that Ova (323-339) was responsible for 25-35% of T-cell response of isolated BALB/c mouse. An investigation has demonstrated that Ova and Ova (323-339) induced similar lung inflammation and a Th2-like dominant immune response in mouse model.
SB-PEPTIDE also offers Biotin-Ova (323-339).
Technical specification
| Sequence : ISQAVHAAHAEINEAGR | |
| MW : 1773 ,91 g/mol (C74H120N26O25) | |
| Purity : > 95% | |
| Counter-Ion : TFA Salts (see option TFA removal) | |
| Delivery format : Freeze dried in propylene 2mL microtubes | |
| Other names : Ovalbumine 323-339,CAS: 92915-79-2 | |
| Peptide Solubility Guideline | |
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Bulk peptide quantities available – Carrier conjugation in option Made in France – For research use only |
Price
| Product catalog | Size | Price € HT | Price $ HT |
| SB059-1MG | 1 mg | 99 | 124 |
| SB059-5MG | 5 mg | 347 | 433 |
| SB059-10MG | 10 mg | 594 | 743 |
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.
References
1- Sun L. Z.,Elsayed S.,Aasen T. B.,Van Do T.,Aardal N. P.,Florvaag E. and Vaali K. Scandinavian Journal of Immunology 71(5):329-335 (2010)
Comparison between Ovalbumin and Ovalbumin Peptide 323©339 Responses in Allergic Mice: Humoral and Cellular Aspects
Ovalbumin (OVA) is widely used in allergy research. OVA peptide 323©339 has been reported to be responsible for 25–35% of isolated BALB/c mouse T©cell response to intact OVA. An investigation of whether OVA and OVA 323©339 molecules can induce equivalent in vivo and in vitro immune responses was conducted. Eight©week©old BALB/c mice were randomly divided into three groups: OVA,OVA 323©339 and saline. On days 0,7,14,mice were intraperitoneally injected with 25 μg OVA or OVA 323©339 absorbed on 300 μg Alum,or saline; on days 21–23,all groups were challenged intranasally with either 20 μl of 1% OVA,1% OVA 323©339 or saline. On day 28,after killing,splenocytes were isolated and cultured under the stimulus of each allergen or medium. Evaluated by hematoxylin/eosin and major basic protein immunohistochemical stainings,OVA and OVA 323©339 induced similar lung inflammation. Interestingly,significant serum total IgE and OVA©specific IgE were observed in OVA mice when compared to saline control. OVA 323©339 mice showed higher serum OVA©specific IgE,OVA 323©339©specific IgE,IL©4 and lower IFN©γ similar to OVA mice. The proliferative response to OVA was found in cultured splenocytes of both OVA and OVA 323©339 mice,while the similar proliferative response to OVA 323©339 was only observed in the splenocytes of OVA 323©339©sensitized and challenged mice. Although OVA 323©339 induced a Th2©like response in the mouse model as did OVA,OVA 323©339 has clearly limited immunogenic potency to activate OVA©sensitized and challenged mice splenocytes,unlike OVA.
2- Zom G. G. et al. Cancer Immunol Res. 2(8):756-764 (2014).
Efficient induction of antitumor immunity by synthetic toll-like receptor ligand-peptide conjugates
Chemical conjugates comprising synthetic Toll-like receptor ligands (TLR-L) covalently bound to antigenic synthetic long peptides (SLP) are attractive vaccine modalities,which can induce robust CD8(+) T-cell immune responses. Previously,we have shown that the mechanism underlying the power of TLR-L SLP conjugates is improved delivery of the antigen together with a dendritic cell activation signal. In the present study,we have expanded the approach to tumor-specific CD4(+) as well as CD8(+) T-cell responses and in vivo studies in two nonrelated aggressive tumor models. We show that TLR2-L SLP conjugates have superior mouse CD8(+) and CD4(+) T-cell priming capacity compared with free SLPs injected together with a free TLR2-L. Vaccination with TLR2-L SLP conjugates leads to efficient induction of antitumor immunity in mice challenged with aggressive transplantable melanoma or lymphoma. Our data indicate that TLR2-L SLP conjugates are suitable to promote integrated antigen-specific CD8(+) and CD4(+) T-cell responses required for the antitumor effects. Collectively,these data show that TLR2-L SLP conjugates are promising synthetic vaccine candidates for active immunotherapy against cancer.
3- 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.