Peptides & Amino Acids

Universal Major Histocompatibility Complex (MHC) H2 I-Ab epitope for CD4+ T-cell recruitment and activation SB-PEPTIDE offers I-Ab restricted PADRE peptide ak(Cha)VAAWTLKAAa-Ahx-C. Pan DR-binding epitope (PADRE) is a universal synthetic peptide binding Major Histocompatibility Complex (MHC)-II receptors, of which H2 complex (mouse MHC), present on specific immune cells. 4 class II loci exist in the region I of the H2 complex gene (see image below), known as Aa & Ea loci (α encoded) and Ab & Eb loci (β encoded), that are similar to the DR, DP and DQ loci of the Human Leukocyte Antigen (HLA) complex. I-Ab restricted PADRE peptide interacts specifically with mouse H2-I-Ab receptors that activate antigen specific CD4+ T-cells in the same way as PADRE peptide’s interaction with HLA-DR receptors. This feature places I-Ab restricted PADRE as promising adjuvant for immunotherapeutic vaccines against chronicle diseases such as infections, Alzheimer or cancer. Similarly to the original PADRE pep

Universal Major Histocompatibility Complex (MHC) H2 I-Ab epitope for CD4+ T-cell recruitment and activation SB-PEPTIDE offers I-Ab restricted PADRE peptide ak(Cha)VAAWTLKAAa-Ahx-C. Pan DR-binding epitope (PADRE) is a universal synthetic peptide binding Major Histocompatibility Complex (MHC)-II receptors, of which H2 complex (mouse MHC), present on specific immune cells. 4 class II loci exist in the region I of the H2 complex gene (see image below), known as Aa & Ea loci (α encoded) and Ab & Eb loci (β encoded), that are similar to the DR, DP and DQ loci of the Human Leukocyte Antigen (HLA) complex. I-Ab restricted PADRE peptide interacts specifically with mouse H2-I-Ab receptors that activate antigen specific CD4+ T-cells in the same way as PADRE peptide’s interaction with HLA-DR receptors. This feature places I-Ab restricted PADRE as promising adjuvant for immunotherapeutic vaccines against chronicle diseases such as infections, Alzheimer or cancer. Similarly to the original PADRE pep

Universal Major Histocompatibility Complex (MHC) H2 I-Ab epitope for CD4+ T-cell recruitment and activation SB-PEPTIDE offers I-Ab restricted PADRE peptide ak(Cha)VAAWTLKAAa-Ahx-C. Pan DR-binding epitope (PADRE) is a universal synthetic peptide binding Major Histocompatibility Complex (MHC)-II receptors, of which H2 complex (mouse MHC), present on specific immune cells. 4 class II loci exist in the region I of the H2 complex gene (see image below), known as Aa & Ea loci (α encoded) and Ab & Eb loci (β encoded), that are similar to the DR, DP and DQ loci of the Human Leukocyte Antigen (HLA) complex. I-Ab restricted PADRE peptide interacts specifically with mouse H2-I-Ab receptors that activate antigen specific CD4+ T-cells in the same way as PADRE peptide’s interaction with HLA-DR receptors. This feature places I-Ab restricted PADRE as promising adjuvant for immunotherapeutic vaccines against chronicle diseases such as infections, Alzheimer or cancer. Similarly to the original PADRE pep

Analog of the native Melan-A (26-35) decapeptide derives from the melanocyte lineage-specific protein Melan-A/MART-1, which is expressed in almost 75-100% of primary and metastatic melanomas. The region 26-35 of Melan-A protein acts as an antigenic peptide that is recognized by CD8+ tumor-reactive cytolytic T lymphocytes (CTLs) for designing antigen-specific cancer vaccines1. It has been shown that CD8+ Melan-A-specific CTLs isolated from melanoma patients efficiently lyse the Melan-A-expressing HLA-A*0201+ melanoma cell line. However, CTLs preferentially recognize the Melan-A (26-35) peptide as compared with the Melan-A (27-35) peptide. Moreover, the Melan-A (26-35) A27L analog (ELAGIGILTV) has a higher binding affinity to HLA-A*0201 than the native Melan-A (26-35) peptide (EAAGIGILTV), and consequently displays more potent antigenicity and immunogenicity. It has been reported that the concentration of Melan-A (26-35) A27L analog required to obtain 50% of maximal antigenic activity (E

Analog of the native Melan-A (26-35) decapeptide derives from the melanocyte lineage-specific protein Melan-A, MART-1, which is expressed in almost 75-100% of primary and metastatic melanomas. The region 26-35 of Melan-A protein acts as an antigenic peptide that is recognized by CD8+ tumor-reactive cytolytic T lymphocytes (CTLs) for designing antigen-specific cancer vaccines1. It has been shown that CD8+ Melan-A-specific CTLs isolated from melanoma patients efficiently lyse the Melan-A-expressing HLA-A*0201+ melanoma cell line. However, CTLs preferentially recognize the Melan-A (26-35) peptide as compared with the Melan-A (27-35) peptide. Moreover, the Melan-A (26-35) A27L analog (ELAGIGILTV) has a higher binding affinity to HLA-A*0201 than the native Melan-A (26-35) peptide (EAAGIGILTV), and consequently displays more potent antigenicity and immunogenicity. It has been reported that the concentration of Melan-A (26-35) A27L analog required to obtain 50% of maximal antigenic activity (

Analog of the native Melan-A (26-35) decapeptide derives from the melanocyte lineage-specific protein Melan-A, MART-1, which is expressed in almost 75-100% of primary and metastatic melanomas. The region 26-35 of Melan-A protein acts as an antigenic peptide that is recognized by CD8+ tumor-reactive cytolytic T lymphocytes (CTLs) for designing antigen-specific cancer vaccines1. It has been shown that CD8+ Melan-A-specific CTLs isolated from melanoma patients efficiently lyse the Melan-A-expressing HLA-A*0201+ melanoma cell line. However, CTLs preferentially recognize the Melan-A (26-35) peptide as compared with the Melan-A (27-35) peptide. Moreover, the Melan-A (26-35) A27L analog (ELAGIGILTV) has a higher binding affinity to HLA-A*0201 than the native Melan-A (26-35) peptide (EAAGIGILTV), and consequently displays more potent antigenicity and immunogenicity. It has been reported that the concentration of Melan-A (26-35) A27L analog required to obtain 50% of maximal antigenic activity (

Analog of the native Melan-A (26-35) decapeptide derives from the melanocyte lineage-specific protein Melan-A, MART-1, which is expressed in almost 75-100% of primary and metastatic melanomas. The region 26-35 of Melan-A protein acts as an antigenic peptide that is recognized by CD8+ tumor-reactive cytolytic T lymphocytes (CTLs) for designing antigen-specific cancer vaccines1. It has been shown that CD8+ Melan-A-specific CTLs isolated from melanoma patients efficiently lyse the Melan-A-expressing HLA-A*0201+ melanoma cell line. However, CTLs preferentially recognize the Melan-A (26-35) peptide as compared with the Melan-A (27-35) peptide. Moreover, the Melan-A (26-35) A27L analog (ELAGIGILTV) has a higher binding affinity to HLA-A*0201 than the native Melan-A (26-35) peptide (EAAGIGILTV), and consequently displays more potent antigenicity and immunogenicity. It has been reported that the concentration of Melan-A (26-35) A27L analog required to obtain 50% of maximal antigenic activity (

Biotin-MOG (35-55) peptide is the biotinylated version of Mouse MOG (35-55) peptide which is used to induce the Experimental Autoimmune Encephalomyelitis (EAE) mouse model for T-cell-mediated inflammatory demyelinating autoimmune diseases of the CNS.

Overlaping peptide library of Human MOG protein, 15 amino acids per peptide with offset 11. Purity around 70%. All peptides are pooled in a single tube.