CAS 156251-01-3

H-GLU-ALA-ALA-GLY-ILE-GLY-ILE-LEU-THR-VAL-OH

Description:

The chemical substance with the name "H-GLU-ALA-ALA-GLY-ILE-GLY-ILE-LEU-THR-VAL-OH" and CAS number "156251-01-3" is a peptide composed of a sequence of amino acids. This peptide features a combination of hydrophilic and hydrophobic residues, which can influence its solubility and interaction with biological membranes. The presence of glutamic acid (GLU) introduces a negatively charged side chain, while the branched-chain amino acids like isoleucine (ILE) and leucine (LEU) contribute to its hydrophobic character. The terminal hydroxyl group (OH) suggests that it may have some polar characteristics, potentially enhancing its solubility in aqueous environments. Peptides like this one can play significant roles in biological processes, including signaling, enzyme activity, and structural functions in proteins. The specific sequence and composition can also affect its biological activity, stability, and potential applications in pharmaceuticals or biotechnology. Understanding the properties of such peptides is crucial for their utilization in research and therapeutic contexts.

Formula: C₄₂H₇₄N₁₀O₁₄

Synonyms:

• Glu-Ala-Ala-Gly-Ile-Gly-Ile-Leu-Thr-Val
• Eaagigiltv
• Antigen Sk29-Aa (26-35) (Human)
• Antigen Lb39-Aa (26-35) (Human)
• Mart 1 (26-35)
• Mart-1 (26-35) (Human)
• Melanoma Antigen Recognized By T-Cells 1 (26-35) (Human)

MART-1 (26-35) (human)

CAS: 156251-01-3

MART-1 (26-35) has been shown to be better recognized by a number of polyclonal and monoclonal populations of tumor-reactive HLA-A*0201-restricted cytotoxic T lymphocytes (CTL) than MART-1 (27-35) (human).

Formula: C₄₂H₇₄N₁₀O₁₄

Purity: 96.7%

Color and Shape: White

Molecular weight: 943.11

Ref: 01-4027904

MART-1 (26-35) (human)

CAS: 156251-01-3

MART-1 (26-35) (human)

Purity: ≥98%

Molecular weight: 943.1g/mol

Ref: 54-BUP21017

MART-1 (26-35) (human)

CAS: 156251-01-3

MART-1 (26-35) (human) (MART-1 (26-35) human) is a peptide fragment of MART-1 protein.

Formula: C₄₂H₇₄N₁₀O₁₄

Purity: >99.99%

Color and Shape: Solid

Molecular weight: 943.1

Ref: TM-T7489

MART-1 (26-35)

CAS: 156251-01-3

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 (EC50) is 0.01nM, whereas that of the native Melan-A (26-35) peptide is 0.25nM1. Therefore, the relative activity of Melan-A (26-35) A27L analog is 25 fold higher than that of the native Melan-A (26-35) peptide.
Furthermore, functional competition assay has shown that the concentration of Melan-A (26-35) A27L analog required to achieve 50% inhibition (IC50) of tumor lysis is 2nM, which is 10 fold lower than that of the native Melan-A (26-35) peptide. Regarding peptide stability in human serum, the half-lifes (t1/2) of the native Melan-A (26-35) peptide and the A27L analog are quite similar (45 and 40min, respectively) as measured by HPLC-ESI-MS, but much higher than that of the Melan-A (27-35) nonapeptide (5min).

Formula: C₄₂H₇₄N₁₀O₁₄

Color and Shape: Powder

Molecular weight: 943.1 g/mol

Ref: 3D-CRB1001607

MART-1 (26-35) (human)

CAS: 156251-01-3

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 (EC50) is 0.01nM, whereas that of the native Melan-A (26-35) peptide is 0.25nM1. Therefore, the relative activity of Melan-A (26-35) A27L analog is 25 fold higher than that of the native Melan-A (26-35) peptide.
Furthermore, functional competition assay has shown that the concentration of Melan-A (26-35) A27L analog required to achieve 50% inhibition (IC50) of tumor lysis is 2nM, which is 10 fold lower than that of the native Melan-A (26-35) peptide. Regarding peptide stability in human serum, the half-lifes (t1/2) of the native Melan-A (26-35) peptide and the A27L analog are quite similar (45 and 40min, respectively) as measured by HPLC-ESI-MS, but much higher than that of the Melan-A (27-35) nonapeptide (5min).

Formula: C₄₂H₇₄N₁₀O₁₄

Molecular weight: 943.11 g/mol

Ref: 3D-PP50002

MART-1 (26-35) (human) trifluoroacetate salt

CAS: 156251-01-3

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 (EC50) is 0.01nM, whereas that of the native Melan-A (26-35) peptide is 0.25nM1. Therefore, the relative activity of Melan-A (26-35) A27L analog is 25 fold higher than that of the native Melan-A (26-35) peptide.
Furthermore, functional competition assay has shown that the concentration of Melan-A (26-35) A27L analog required to achieve 50% inhibition (IC50) of tumor lysis is 2nM, which is 10 fold lower than that of the native Melan-A (26-35) peptide. Regarding peptide stability in human serum, the half-lifes (t1/2) of the native Melan-A (26-35) peptide and the A27L analog are quite similar (45 and 40min, respectively) as measured by HPLC-ESI-MS, but much higher than that of the Melan-A (27-35) nonapeptide (5min).

Formula: C₄₂H₇₄N₁₀O₁₄

Purity: Min. 95%

Molecular weight: 943.1 g/mol

Ref: 3D-FM109182