Pool of 27 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Latent membrane protein 2A (LMP2A) (UniProt ID: A8CDV5) of Epstein-Barr virus (HHV4) for T cell assays.
One unit allows the stimulation of 2,5 x 108 cells.
TechData
Gene:
LMP2A
Delivery:
1-3 days
Counterion:
TFA
Length:
118 amino acids
No. Peptides:
27 peptides
Amount/Aliquote:
15 nmol (approx. 25µg)/peptide for stimulation of 2,5 x 108 cells
Solubility:
Dissolve in a minimum amount of pure DMSO (40µl) and dilute with water to the desired concentration. Please pay attention that the final concentration of DMSO must be below 1% (v/v) to avoid toxicity in the biological system.
Pool of 59 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Trans-activator protein BZLF1 (UniProt ID: P03206) of Epstein-Barr virus (HHV4) for T cell assays.
One unit allows the stimulation of 2,5 x 108cells.
Pool of 234 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Epstein-Barr nuclear antigen 3 (EBNA3a) (UniProt ID: P12977) of Epstein-Barr virus (HHV4) for T cell assays.
One unit allows the stimulation of 2,5 x 108 cells.
Pool of 234 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Epstein-Barr nuclear antigen 4 (EBNA3b) (UniProt ID: Q1HVG4) of Epstein-Barr virus (HHV4) for T cell assays.
One unit allows the stimulation of 2,5 x 108 cells.
Peptide pool of 224 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Envelope glycoprotein GP350/GP340 (UniProt ID: P03200) of Epstein-Barr virus (EBV, Humanes Herpesvirus 4, HHV4).
One unit allows the stimulation of 2,5 x 108 cells.
gp350/gp340 versus gp350/220
The EBV envelope glycoprotein gp350/gp340 (or gp350/220) is encoded by the BLLF1 gene and represents one of the most abundant surface proteins of the virion. The protein exists in multiple isoforms generated by alternative splicing. While gp350 denotes the full-length form, gp340 and gp220 refer to truncated isoforms of the same glycoprotein, which retain identical biological function. Differences in naming (gp340 vs. gp220) arise from historical nomenclature, experimental detection methods, and variations in glycosylation state.
Initial attachment and endocytosis
Gp350/gp340 belongs to the core set of EBV glycoproteins that define viral tropism and host cell interaction – together with gp42, BMRF2, gH/gL, and gB. Gp350/gp340 plays a central role in viral attachment and entry into B lymphocytes. Through molecular mimicry of complement components, gp350/gp340 specifically recognizes complement receptor 1 (CR1/CD35) and complement receptor 2 (CR2/CD21) on B cells. This interaction mediates the initial attachment of EBV particles and triggers endocytosis of the immobilized virion, marking the first step of EBV infection in B lymphocytes.
Major target of immune responses
Due to its surface exposure, high abundance, and essential role in viral entry, gp350/gp340 represents a major target of humoral and cellular immune responses. Peptides derived from gp350/gp340 are widely used to study EBV-specific T cell immunity, epitope recognition, and immune monitoring in the context of EBV infection, EBV-associated malignancies, and vaccine development.
The EBV (gp350/gp340) Peptide Pool from peptides&elephants provides comprehensive sequence coverage of this key viral glycoprotein and is ideally suited for applications such as T cell stimulation assays, epitope mapping, and immunological profiling in EBV research.
Pool of 94 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Latent membrane protein 1 (LMP1) (UniProt ID: P03230) of Epstein-Barr virus (HHV4) for T cell assays.
One unit allows the stimulation of 2,5 x 108 cells.
Peptide pool of 53 overlapping peptides derived from a peptide scan (15mers with 11 aa overlap) through Secreted protein BARF1 (UniProt: P03225) of Homo sapiens Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
One unit allows the stimulation of 2,5 x 108 cells.
This pool consists of 26 peptides, each corresponding to a defined HLA class I-restricted T cell epitope from Epstein-Barr virus (EBV).
One unit allows the stimulation of 2,5 x 108 cells.
The EBV EBNA-2 Peptide Pool from peptides&elephants is designed for reliable stimulation and detection of EBV-specific T-cell responses in immunological research. The pool consists of 119 overlapping peptides (15-mers with an 11-amino-acid overlap) spanning Epstein–Barr nuclear antigen 2 (EBNA2) from Epstein–Barr virus strain B95-8 (UniProt ID: P12978). The Epstein-Barr virus is also known as Human herpesvirus 4 (HHV-4).
EBNA2 is one of the earliest viral proteins expressed after infection of B cells and acts as a central transcriptional regulator that reprograms host and viral gene expression. Through interactions with numerous sites in the host genome, EBNA2 cooperates with EBNA-LP to activate key cellular pathways, including transient activation of the MYC proto-oncogene, which drives early B-cell proliferation and supports survival during the establishment of EBV latency.
EBNA2 activity also contributes to the transition from the initial Wp promoter–driven transcription toward the Cp promoter–controlled latency program IIb, in which multiple EBV nuclear antigens are expressed from a polycistronic transcript. This shift allows the virus to balance rapid proliferation with controlled persistence.
Learn more about EBNA2-mediated transcriptional reprogramming and MYC regulation during early EBV infection in the Peptide Insights section of peptides&elephants.
Applications
Suitable for multiple T-cell–based assays, including:
ELISpot assays
Intracellular cytokine staining (ICS)
FluoroSpot assays
T-cell proliferation assays
Immune monitoring in EBV research
Capacity
One unit allows the stimulation of 2.5 × 10⁸ cells.
The EBV EBNA-2 Peptide Pool provides a comprehensive tool for studying EBV-specific immune responses, latency establishment, and virus-host interactions in basic and translational research.
SSCSSCPLSK is a linear peptidic epitope (epitope ID60930) studied as part of Latent membrane protein 2 from Human herpesvirus 4 (Epstein Barr virus). This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
Antigen Peptide EBV LMP-2 419-427 (HLA-A*24:02) TYGPVFMCL for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays.
EBV LMP-2 426-434 (HLA-A*02:01) CLGGLLTMV for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays.
Single peptide (PYLFWLAAI) for stimulation of human EBV LMP2(131-139)-specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*2402 allele.
IEDPPFNSL is a linear peptidic epitope (epitope ID 25756) studied as part of Latent membrane protein 2 from Human herpesvirus 4 (Epstein Barr virus). This epitope has been studied for immune reactivity, tested in T cell assays and MHC ligand assays
Antigen Peptide EBV LMP2 HLA-A*0201 (FLYALALLL) for stimulation of human EBV LMP2(356-364)-specific CD8+ T-cells. The peptide is synthesised as it is presented by the MHC class I HLA-A*0201 allele. LYALALLL is a linear peptidic epitope studied as part of Latent membrane protein 2 from Human herpesvirus 4 (Epstein Barr virus).
The EBV LMP2 419-427 mutant 426S (HLA-A*24:02) peptide with the amino acid sequence TYGPVFMSL is a linear peptidic epitope (epitope ID 67350) studied as part of Latent membrane protein 2 (UniProt:P13285) from Human herpesvirus 4 (Epstein Barr virus).EBV LMP2 419-427 mutant 426S (HLA-A*24:02) has been studied for immune reactivity in publications and has been tested in T cell assays and MHC ligand assays.