Influenza Hemagglutinin (HA) peptide is a synthetic peptide that corresponds to amino acids 98-106 of the human influenza virus hemagglutinin. The HA Peptide is used for competing out the anti-HA antibody binding to HA-tagged fusion proteins in immunoassays. attaching the virus to cell receptors and for initiating infection.
CAT No: R1854
CAS No:92000-76-5
Synonyms/Alias:HA Peptide;92000-76-5;Influenza Hemagglutinin (HA) Peptide;(3S)-3-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-carboxypropanoyl]amino]-3-methylbutanoyl]pyrrolidine-2-carbonyl]amino]-4-[[(2S)-1-[[(1S)-1-carboxyethyl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;HA tag peptide;hemagglutinin tag;HA tag;HA-tag;hemagglutinin peptide;YPYDVPDYA;Tyr-Pro-Tyr-Asp-Val-Pro-Asp-Tyr-Ala;hemagglutinin (HA) tag;hemagglutinin (HA) peptide;CHEBI:80171;EX-A8013H;DTXSID00437019;HVLSXIKZNLPZJJ-TXZCQADKSA-N;AKOS040763949;Influenza Hemagglutinin (HA) Peptide?;DA-74485;H-Tyr-Pro-Tyr-Asp-Val-Pro-Asp-Tyr-Ala-OH;A12940;Influenza Hemagglutinin (HA) Peptide, >=97% (HPLC);L-Tyr-L-Pro-L-Tyr-L-Asp-L-Val-L-Pro-L-Asp-L-Tyr-L-Ala;H-L-Tyr-L-Pro-L-Tyr-L-Asp-L-Val-L-Pro-L-Asp-L-Tyr-L-Ala-OH;(3S)-3-{[(2S)-1-[(2S)-2-[(2S)-2-[(2S)-2-{[(2S)-1-[(2S)-2-AMINO-3-(4-HYDROXYPHENYL)PROPANOYL]PYRROLIDIN-2-YL]FORMAMIDO}-3-(4-HYDROXYPHENYL)PROPANAMIDO]-3-CARBOXYPROPANAMIDO]-3-METHYLBUTANOYL]PYRROLIDIN-2-YL]FORMAMIDO}-3-{[(1S)-1-{[(1S)-1-CARBOXYETHYL]CARBAMOYL}-2-(4-HYDROXYPHENYL)ETHYL]CARBAMOYL}PROPANOIC ACID;L-tyrosyl-L-prolyl-L-tyrosyl-L-alpha-aspartyl-L-valyl-L-prolyl-L-alpha-aspartyl-L-tyrosyl-L-alanine;
Chemical Name:(3S)-3-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-carboxypropanoyl]amino]-3-methylbutanoyl]pyrrolidine-2-carbonyl]amino]-4-[[(2S)-1-[[(1S)-1-carboxyethyl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoic acid
Influenza Hemagglutinin (HA) Peptide is a synthetic peptide fragment derived from the hemagglutinin glycoprotein found on the surface of influenza viruses. As a key component in viral entry and host-cell recognition, hemagglutinin plays a central role in the infectivity and immunogenicity of influenza strains. The peptide form offers a highly defined and reproducible tool for investigating antigenic determinants, protein-protein interactions, and immune recognition events. Its biochemical relevance makes it indispensable for researchers studying viral mechanisms, host-pathogen interactions, and the molecular basis of influenza virus infectivity.
Epitope Mapping: HA peptide fragments are widely utilized in epitope mapping studies to identify and characterize antigenic regions recognized by antibodies. By enabling precise delineation of linear and conformational epitopes, these peptides support the development of monoclonal antibodies and facilitate the assessment of immune responses to different influenza strains. Such mapping is crucial for understanding the antigenic drift and shift phenomena that underlie influenza virus evolution and vaccine escape.
Immunoassay Development: Synthetic hemagglutinin peptides serve as essential reagents in the development and optimization of immunoassays, including ELISA and western blot protocols. Their well-defined sequence and structural features allow for consistent detection of anti-influenza antibodies in serum samples, supporting serological surveillance, vaccine efficacy studies, and diagnostics research. The use of HA peptides as assay standards or capture antigens ensures reproducibility and specificity in immunological analyses.
Vaccine Research: In the context of vaccine design and evaluation, HA peptides are instrumental for dissecting immune responses at the molecular level. They are employed to assess T-cell and B-cell reactivity, enabling researchers to identify immunodominant regions and optimize epitope-based vaccine candidates. The use of defined peptide sequences aids in the rational design of next-generation vaccines targeting conserved regions of the hemagglutinin protein, potentially broadening the scope of protective immunity.
Protein-Protein Interaction Studies: HA-derived peptides provide a valuable platform for investigating the molecular interactions between influenza hemagglutinin and host cell receptors, such as sialic acid-containing glycoproteins. By mimicking key functional domains, these peptides facilitate biophysical and structural studies aimed at elucidating the mechanisms of viral attachment, membrane fusion, and entry. Such insights are critical for antiviral drug discovery and the development of novel therapeutic strategies targeting early steps in influenza infection.
Peptide-Based Biosensor Development: The unique binding properties of hemagglutinin peptides make them attractive candidates for the design of biosensors and analytical devices for influenza virus detection. By incorporating HA-derived sequences as recognition elements, researchers can create sensitive and selective platforms for rapid virus identification in research, surveillance, and quality control settings. The robust and customizable nature of synthetic peptides supports their integration into diverse biosensing technologies, enhancing the detection capabilities for influenza and related viral pathogens.
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