The peptide Influenza NP 55-63 (HLA-A*02:01) with the amino acid sequence RLIQNSLTI is a linear peptidic epitope (epitope ID 54593) studied as part of Nucleoprotein (UniProt:P03466) from Influenza A virus.
Influenza NP 55-63 (HLA-A*02:01) has been studied for immune reactivity in publications and has been tested in T cell assays and MHC ligand assays.
The Influenza A (PR8) NP 265–274 peptide (Sequence: ILRGSVAHK) is a widely studied, immunodominant linear peptidic epitope derived from the viral Nucleoprotein (NP, UniProt ID: P03466) of Influenza A virus (strain A/PR/8/1934). Restricted to HLA-A*03:01, this epitope serves as a vital standard in immunomonitoring assays, cross-reactive T-cell profiling, and vaccine development against influenza pathogens. Key Features & ApplicationsExtensive Scientific Validation: Documented in 36 publications and rigorously evaluated across 68+ T-cell assays and 7 MHC ligand binding studies (IEDB Epitope ID: 27283). Structural Characterization: Solved 3D crystal structure available (PDB ID: 7UC5) for detailed structural biology and TCR-MHC interaction analyses. Broad Assay Compatibility: Optimized for ELISpot, Intracellular Cytokine Staining (ICS), MHC multimer staining, and cytotoxic T-lymphocyte (CTL) activation assays. Cross-Referenced Control Pools This catalog peptide is also available as a core component in the following off-the-shelf peptides&elephants control pools: Influenza control Peptide Pool (>95% HPLC)CEF control Peptide Pool (>95% HPLC, advanced)CEF (classic) Peptide Pool (>95% HPLC)
The Influenza A HA 116–131 Peptide (epitope ID 73603) is an extended 16-mer CD4+ T-cell epitope derived from the HA1 subunit of Influenza A Hemagglutinin (H3N2). Binding for this
MHC Class II ligand
has been experimentally validated for HLA-DRB1*01:01, HLA-DRB1*04:01, and HLA-DRB1*07:01. In canonical UniProt entries such as P03437 for A/Aichi/2/1968 or related H3N2 strains like A/Beijing/32/1992, the sequence YDVPDYASLRSLVASS corresponds to amino acids 116–131 of the precursor protein, which represents residues 98–113 of the mature HA1 chain following signal peptide cleavage.Encompassing the well-known core motif YDVPDYASL, this specific 16-amino-acid sequence has been evaluated in specialized immunological studies (e.g., Gelder et al., 1998) to investigate MHC Class II binding capacity and CD4+ T-cell reactivity. It serves as a targeted peptide for Influenza-specific T-cell assays and epitope characterization.
The Influenza A HA 271–286 Peptide (RGYFKMRTGKSSIMRS, IEDB Epitope ID: 54022) is a highly promiscuous, 16-mer CD4+ T-cell epitope derived from Influenza A Hemagglutinin (UniProt ID: P03437). Characterized by its broad MHC Class II binding spectrum, this linear peptide binds with high affinity to HLA-DQA1*01:02 / DQB1*06:02 as well as HLA-DRB1*10:01 and HLA-DRB1*01:01.Due to its ability to be presented across multiple common HLA class II alleles, this sequence is a key target for studying helper T-cell priming, cross-reactive CD4+ responses, and population-wide immunomonitoring. Depending on whether the numbering scheme includes the precursor signal peptide (HA0) or refers to the processed chain, this sequence is annotated as HA 271–286 or HA 255–270.
The Influenza A HA 306–318 Peptide (PKYVKQNTLKLAT) is one of the most thoroughly characterized promiscuous CD4+ T-cell epitopes in viral immunology. Derived from the HA1 subunit of Influenza A Hemagglutinin (strain A/Aichi/2/1968 H3N2; UniProt: P03437), this 13-mer sequence is a benchmark tool for studying broad MHC Class II restriction, helper T-cell activation, and cross-reactive immunity.PKYVKQNTLKLAT is also annotated as HA 322–334 when including the 16-amino-acid N-terminal signal peptide (HA0 precursor numbering). It is part of a coordinated reference panel alongside the truncated HA 322–333 (12-mer) for fine-tuned MHC Class II studies and Influenza B HA 322–334 for type-specific control assays.Indexed under IEDB Epitope ID 48237, this catalog peptide has been featured in over 130 peer-reviewed publications and structurally validated in multiple Protein Data Bank (PDB) co-crystal structures (e.g., 1DLH, 1FYT, 1HXY). It exhibits exceptionally broad binding across numerous human HLA-DR alleles, making it an ideal reference peptide for population-wide immunomonitoring, ELISPOT controls, and vaccine development assays. Key Features & Applications Highly Promiscuous Class II Target: Binds with high affinity across a broad spectrum of HLA-DR alleles, including HLA-DRB1*01:01, HLA-DRB1*04:01, HLA-DRB1*11:01, HLA-DRB1*07:01, and HLA-DRB5*01:01. Gold-Standard Reference Epitop: Extensively benchmarked in functional CD4+ T-cell activation assays (ELISPOT, ICS, proliferation) and direct MHC ligand binding studies. Structural Proof: High-resolution 3D crystal structures available in the PDB demonstrate its precise molecular interactions within the MHC Class II binding groove.
The Influenza A HA 322–333 Peptide (PKYVKQNTLKLA) is a 12-mer linear CD4+ T-cell epitope derived from the HA1 subunit of Influenza A Hemagglutinin (strain A/Aichi/2/1968 H3N2; UniProt-ID: P03437). Specifically restricted to HLA-DRA*01:01 / DRB1*01:01 (HLA-DR1), this sequence is utilized in cellular immunology to evaluate CD4+ T-cell reactivity, MHC-peptide binding dynamics, and cross-reactive recall responses against seasonal H3N2 strains.
It is indexed under IEDB Epitope ID 48231, and has been validated in peer-reviewed publications across functional T-cell activation assays and direct MHC ligand binding studies.
PKYVKQNTLKLA
serves as a targeted reference peptide for epitope mapping, immunomonitoring, and the development of T-cell-directed influenza vaccine strategies.
Corresponding to HA 306–317 in mature HA1 chain numbering, this 12-mer core sequence represents the C-terminally trimmed variant of the canonical Influenza A HA 306–318 (HA 322–334) epitope—offering a high-affinity HLA-DR1 benchmark that perfectly complements both its parent 13-mer and the lineage-matched Influenza B HA 322–334 reference peptide.
The peptide Influenza A virus 332-340 (H-2-Db) with the amino acid sequence TGLRNTPSI is a linear peptidic epitope (epitope ID 187544) studied as part of Hemagglutinin (UniProt:P03452) from Influenza A virus.Influenza A virus 332-340 (H-2-Db) has been studied for immune reactivity in publication and has been tested in T cell assays and MHC ligand assay.
LYEKVKSQL is a linear peptidic epitope (epitope ID40746) studied as part of Hemagglutinin from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
IYSTVASSL is a linear peptidic epitope studied as part of Hemagglutinin from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays, B cell assays and MHC ligand assays
The Influenza A M1 13–21 epitope (amino acid sequence: SIIPSGPLK) is a well-characterized CD8⁺ T cell epitope derived from the Matrix Protein 1 (M1) of the Influenza A virus (UniProt ID: P03485). This 9-mer linear peptide is located within the membrane-binding domain of M1 and is known to be presented on several HLA class I molecules, including:
HLA-A*11:01
HLA-A*03:01
HLA-A*31:01
HLA-A*68:01
This epitope has been referenced under IEDB Epitope ID: 58567 and has been widely studied in the context of T cell recognition, MHC class I binding, and antiviral immune responses.
Applications:
Detection of Influenza-specific CD8⁺ T cells
HLA-A-restricted antigen presentation analysis
Use in T cell activation assays (e.g., ELISPOT, ICS)
Validation of TCR transgenic systems or HLA tetramer tools
Monitoring immune responses in vaccine or infection models
Epitope Background
This epitope, SIIPSGPLK, is derived from Matrix Protein 1 (M1) of Influenza A virus, a structural protein involved in virion stability, uncoating, and regulation of transcription. The 13–21 region lies within the membrane-binding domain, which interacts with the inner side of the viral lipid bilayer.This catalog peptide is also available in the following off-the-shelf Control Pools:Influenza A M1 Peptide PoolInfluenza control Peptide Pool (>95% HPLC)CEF control Peptide Pool (>95% HPLC, advanced)
RMVLASTTAK is a linear peptidic epitope (epitope ID54953) studied as part of Matrix protein 1 from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
The Influenza A M1 58-66 peptide is a linear peptidic epitope (epitope ID 20354) that has the amino acid sequence GILGFVFTL and is located at positions 58-66 of the Matrix Protein 1 (UniProt: P03485) from Influenza A virus.
The M1 58-66 peptide is highly conserved across many strains of influenza, T cells primed to recognize this peptide can potentially recognize and respond to a variety of influenza infections. This makes the M1 58-66 peptide valuable in vaccine research and in the study of cross-protection against different strains of influenza.
This catalog peptide is also available in the following off-the-shelf Control Pools:Influenza A M1 Peptide PoolInfluenza control Peptide Pool (>95% HPLC)CEF control Peptide Pool (>95% HPLC, advanced)CEF (classic) Peptide Pool (>95% HPLC)
The Influenza A M1 58-66 peptide is well-known for its role in being presented by HLA-A*02:01 (a class I MHC molecule) to cytotoxic CD8+ T cells. It is a well-characterized epitope, making it an ideal tool for studying how T cells recognize viral peptides and initiate an immune response. It is used as a model antigen to study T cell function, activation, and the mechanics of antigen presentation. Understanding how immune cells recognize and target antigens also helps improve T cell-based therapies for cancer.
The Influenza A M1 58-66 peptide has been tested in T cell assays, B cell assays and MHC ligand assays. It is frequently used as a positive control, especially in ELISPOT and tetramer staining, ensuring that the immune cells are functioning as expected.
The M1 58-66 peptide is also a prime example of an immunodominant epitope. In people with the HLA-A*02:01 type, a significant portion of the immune response to influenza focuses on this peptide, making it a key target for understanding immune system priorities in viral infections.See also an example comparison of our prices with the prices of other peptide manufacturers.
The ILGFVFTLTV peptide (epitope ID 27066) overlaps with the well-known immunodominant epitope GILGFVFTL from Influenza A Matrix Protein 1 (M1; UniProt:P03485). Influenza A MP 59-68 is used for the development of more broadly protective influenza vaccines and as a control peptide in immunological studies.Researchers investigated the immunogenicity and protective efficacy of Modified Vaccinia Virus Ankara (MVA) vectors encoding internal influenza antigens in HLA-A2.1 transgenic mice. Following vaccination with recombinant MVAs expressing peptides derived from Influenza A Matrix Protein 1 (M1), the induced CD8⁺ T cell responses were primarily directed against the immunodominant epitope M1 58-66. However, consistent T cell responses were also observed against the overlapping peptide M1 59-68. CD8⁺ T cell activity was assessed using an IFN-γ ELISPOT assay.
KSMREEYRK is a linear peptidic epitope (epitope ID33447) studied as part of Matrix protein 2 from Influenza A virus, tested in T cell assays and MHC ligand assays
IGRFYIQM is a linear peptidic epitope studied as part of Nucleoprotein from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
Influenza peptide ASNENMETM (H-2 Db) is a single peptide for stimulation of T cells. The peptide from Influenza nucleoprotein is synthesized as it is presented by the MHC class I H-2 Db allele and can be used for targeted in vitro generation and expansion of antigen-specific CD8+ T cells.
The Influenza A NP 383–391 peptide (Sequence: SRYWAIRTR) is an exceptionally well-studied, immunodominant epitope derived from the viral Nucleoprotein (NP) of Influenza A virus (UniProt ID: P03466). Primarily presented by HLA-B*27:05, this canonical peptide is a cornerstone tool in cellular immunology for monitoring CD8+ cytotoxic T-lymphocyte (CTL) activation, investigating viral immune escape, and profiling allele-specific T-cell responses. Reactivity has additionally been reported in select studies for related alleles, including HLA-B*27:03 and HLA-B*27:04.Key Scientific Highlights Extensive Literature Validation: Supported by an exceptional scientific corpus including 58 publications, 74+ functional T-cell assays, and 75 MHC ligand binding studies (IEDB Epitope ID: 60867). High-Resolution Structural Data: Structural binding interactions are fully resolved in available 3D crystal structures (PDB ID: 2BST), facilitating structure-based TCR interaction studies. Recall Assay Reference: Widely recognized as a benchmark viral antigen for testing memory T-cell responses in HLA-B*27-positive donor samples. Cross-Referenced Control Pools Streamline your assay workflows by sourcing this epitope as an individual catalog peptide or as a verified component within our off-the-shelf peptides&elephants control panels: Influenza control Peptide Pool (>95% HPLC)CEF control Peptide Pool (>95% HPLC, advanced)CEF (classic) Peptide Pool (>95% HPLC)
CTELKLSDY is a linear peptidic epitope (epitope ID 7136) studied as part of Nucleoprotein (UniProt: P03466) from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
This catalog peptide is also available in the following off-the-shelf Control Pools:Influenza control Peptide Pool (>95% HPLC)CEF control Peptide Pool (>95% HPLC, advanced)CEF (classic) Peptide Pool (>95% HPLC)
SPIVPSFDM is a linear peptidic epitope (epitope ID60089) studied as part of Nucleoprotein from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
QPEWFRNVL is a linear peptidic epitope (epitope ID51809) studied as part of RNA-directed RNA polymerase catalytic subunit from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
VSDGGPNLY is a linear peptidic epitope (epitope ID: 70898) studied as part of RNA-directed RNA polymerase catalytic subunit (UniProt-ID: P03431) from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays.This catalog peptide is also available in the following off-the-shelf Control Pools:Influenza control Peptide Pool (>95% HPLC)CEF control Peptide Pool (>95% HPLC, advanced)CEF (classic) Peptide Pool (>95% HPLC)
KLGEFYNQMM is a linear peptidic epitope (epitope ID31880) studied as part of Nucleoprotein from Influenza B virus. This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
The Influenza B HA 322–334 Peptide (PYYTGEHAKAIGN) is a linear, 13-mer CD4+ T-cell epitope derived from the Hemagglutinin protein (UniProt: P03460) of the Influenza B virus. Restricted to HLA-DR1 (MHC Class II), this epitope serves as a validated reference peptide for studying helper T-cell responses and cross-reactive cellular immunity against type B influenza strains. PYYTGEHAKAIGN is indexed under IEDB Epitope ID 50200, and has been characterized in T-cell reactivity and MHC binding assays, making it a reliable tool for epitope profiling, immunological monitoring, and vaccine candidate evaluation.
Positioned as the type-B structural analogue to the benchmark Influenza A HA 306–318 (HA 322–334) epitope, this 13-mer peptide enables precise discrimination between Influenza A- and B-specific CD4+ helper T-cell responses; paired with the trimmed Influenza A HA 322–333 core sequence, it forms a complete reference set for differential HA immunomonitoring.
TYQRTRALV is a linear peptidic epitope studied as part of Nucleoprotein from Influenza A virus. This epitope has been studied for immune reactivity, tested in T cell assays, B cell assays, MHC ligand assays
The peptide Influenza NP 218-226 (HLA-A*02:01) with the amino acid sequence AYERMCNIL is a linear peptidic epitope (epitope ID 5757) studied as part of Nucleoprotein (UniProt:P03466) from Influenza A virus.Influenza NP 218-226 (HLA-A*02:01) has been studied for immune reactivity in publications and has been tested in T cell assays and MHC ligand assays.
