OVA (323-339), biotin-labeled

Product Name: OVA (323-339), biotin-labeled

Sequence One Letter Code: Biotin-ISQAVHAAHAEINEAGR

Sequence Three Letter Code: Biotin-Ile-Ser-Gln-Ala-Val-His-Ala-Ala-His-Ala-Glu-Ile-Asn-Glu-Ala-Gly-Arg-OH

Chemical Formula:C84H134N28O27S1

Molecular Weight: 2000.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Inflammation and Immunology Research

Source / Species: chicken

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: Biotin-OVA (323–339) is a synthetic peptide corresponding to a well-characterized ovalbumin-derived epitope recognized in H-2b–restricted antigen presentation systems. This peptide is commonly used in immunology research to study antigen processing, MHC class II presentation, and CD4⁺ T-cell activation. The ovalbumin 323–339 sequence is a classical model antigen widely applied in experimental systems investigating adaptive immune responses, immune tolerance, and antigen-specific T-cell signaling. The N-terminal biotin label enables convenient detection, immobilization, and affinity capture in a variety of assay platforms, including ELISA-based assays and protein interaction studies. Biotin-OVA (323–339) is particularly useful for investigating antigen presentation pathways, T-cell receptor recognition, and immune regulation in both in vitro and in vivo models.

Current Research: Understanding how the immune system recognizes and responds to antigens is fundamental to immunology research. Among the many model systems used to study adaptive immunity, peptides derived from ovalbumin (OVA) have become widely adopted tools. Biotin-OVA (323–339) is a synthetic peptide representing the well-characterized ovalbumin epitope spanning amino acids 323 to 339. This sequence is extensively used in H-2b–restricted antigen presentation systems and has become a classical model antigen for studying MHC class II presentation, CD4⁺ T-cell activation, and antigen-specific immune signaling. By incorporating a biotin tag at the N-terminus, this peptide provides additional versatility for experimental applications, allowing convenient detection, immobilization, and affinity capture across multiple assay platforms. As a result, Biotin-OVA (323–339) is widely used in studies investigating antigen processing, T-cell receptor recognition, and mechanisms regulating adaptive immune responses. The OVA (323–339) Epitope in Immunology Research The ovalbumin peptide OVA (323–339) is one of the most extensively studied model epitopes in immunology. It is recognized by CD4⁺ T cells when presented by MHC class II molecules, particularly within murine H-2b genetic backgrounds. Because of its well-defined immunological properties, the peptide has been widely used to explore how antigen presentation leads to T-cell activation and immune signaling. In experimental models, antigen-presenting cells (APCs) process proteins into peptide fragments that are loaded onto MHC class II molecules. These peptide–MHC complexes are then displayed on the cell surface, where they are recognized by T-cell receptors (TCRs) on CD4⁺ helper T cells. The OVA (323–339) sequence serves as a reliable antigenic determinant in this process, enabling researchers to monitor and manipulate immune responses under controlled conditions. Because the peptide’s interaction with the immune system is well characterized, it has become a cornerstone reagent in studies examining antigen-specific T-cell responses and immune regulation. Design and Features of Biotin-OVA (323–339) The Biotin-OVA (323–339) peptide preserves the immunologically relevant epitope while incorporating an N-terminal biotin modification. Biotin is a small molecule that binds with extremely high affinity to streptavidin and avidin proteins, enabling efficient capture and detection of labeled biomolecules. This design offers several advantages in experimental workflows. The biotin tag allows the peptide to be immobilized on streptavidin-coated plates, beads, or biosensors, making it compatible with a wide range of analytical techniques. Additionally, biotinylation facilitates sensitive detection in assays where labeled peptides must be tracked or isolated. Because the biotin group is positioned outside the core epitope sequence, it generally does not interfere with T-cell receptor recognition or MHC class II binding, preserving the peptide’s biological relevance. Studying Antigen Presentation and T-Cell Activation Biotin-OVA (323–339) is particularly valuable for examining the steps involved in antigen presentation and CD4⁺ T-cell activation. Researchers frequently use this peptide in systems designed to analyze how APCs process antigens and present them to T cells. By introducing the peptide into experimental cultures or model organisms, investigators can observe how antigen-specific T cells respond to defined stimuli. This approach has been widely used to study: MHC class II peptide presentation pathways T-cell receptor recognition of antigenic peptides Activation and proliferation of CD4⁺ T cells Cytokine production and immune signaling Mechanisms of immune tolerance and regulation These studies help clarify how the immune system distinguishes between self and non-self antigens and how immune responses are initiated or suppressed. Applications in Immunological Assays The incorporation of a biotin label significantly expands the range of assays in which the peptide can be used. In particular, Biotin-OVA (323–339) is compatible with techniques that rely on streptavidin-based detection systems. Common applications include: ELISA-based assays for monitoring antigen–antibody or antigen–receptor interactions Affinity capture experiments using streptavidin-coated beads or plates Protein interaction studies involving antigen presentation complexes T-cell activation assays using defined antigenic stimulation Flow cytometry and immunodetection methods for analyzing immune responses Because the peptide can be easily immobilized or detected, it supports highly controlled experimental setups in both biochemical and cellular assays. Investigating Immune Regulation and Tolerance In addition to studying antigen recognition, the OVA (323–339) model system is widely used to investigate immune tolerance and regulatory pathways. By exposing immune cells to a defined antigen under different conditions, researchers can explore how immune responses are amplified, suppressed, or redirected. This model has contributed significantly to our understanding of T-cell differentiation, regulatory T-cell activity, and immune homeostasis. It also provides a platform for examining how environmental signals, co-stimulatory molecules, or cytokines influence antigen-specific responses. A Versatile Tool for Adaptive Immunity Research Biotin-OVA (323–339) combines a well-established model antigen with the practical advantages of biotin labeling. This combination makes it a versatile reagent for investigating key processes in adaptive immunity, including antigen presentation, T-cell receptor recognition, and immune signaling pathways. As immunology research continues to explore the complexities of antigen-specific responses, peptides like Biotin-OVA (323–339) remain essential experimental tools. Their defined structure and compatibility with multiple assay platforms enable researchers to study the molecular mechanisms that shape immune recognition and regulation in both in vitro and in vivo experimental systems.