Gp100 (25-33), mouse

Gp100 (25-33), mouse sequence is found in residues 25 to 33 of the mouse self/tumor antigen glycoprotein (mgp100). Mgp100 is an enzyme involved in pigment synthesis, and the epitope fragment is expressed in both normal melanocytes and melanoma cells.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Gp100 (25-33), mouse(CAS 212370-36-0)

CAT No: R1928

CAS No:212370-36-0

Synonyms/Alias:Gp100 (25-33), mouse;212370-36-0;Mgp100 (25-33) (TFA);HY-P2506;AKOS040757308;DA-63868;CS-0135050;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-amino-4-carboxybutanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-4-oxobutanoyl]amino]-5-oxopentanoyl]amino]-3-carboxypropanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoic acid;

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M.F/Formula
C46H69N15O17
M.W/Mr.
1104.1
Sequence
One Letter Code:EGSRNQDWL
Three Letter Code:H-Glu-Gly-Ser-Arg-Asn-Gln-Asp-Trp-Leu-OH
Application
Cancer

Gp100 (25-33), mouse is a synthetic peptide fragment derived from the mouse glycoprotein 100 (gp100) antigen, a transmembrane protein highly expressed in melanocytes and melanoma cells. As a nonapeptide corresponding to residues 25 to 33 of the gp100 sequence, it serves as a defined epitope recognized by immune cells, particularly in the context of antigen presentation and T cell activation studies. Its precise sequence and molecular characteristics make it a valuable reagent for exploring antigen-specific immune responses, peptide-MHC binding, and the functional dynamics of tumor-associated antigens in murine models. The relevance of this peptide in immunological research is underscored by its utility in dissecting the mechanisms of melanoma recognition, tolerance, and immune modulation.

Antigen presentation research: Utilization of Gp100 (25-33), mouse as a model epitope enables in-depth investigation into the molecular mechanisms of antigen processing and presentation by major histocompatibility complex (MHC) class I molecules. Researchers employ this peptide to load antigen-presenting cells, such as dendritic cells or macrophages, to evaluate peptide-MHC complex formation, stability, and surface expression. These studies are fundamental for understanding how immune surveillance is orchestrated at the cellular level, particularly in the context of tumor immunology and the development of immune evasion strategies by malignant cells.

T cell activation assays: The peptide serves as a critical tool for stimulating gp100-specific cytotoxic T lymphocytes (CTLs) in vitro and ex vivo. By pulsing target cells with the peptide, investigators can quantitatively assess T cell receptor (TCR) recognition, cytokine production, cytotoxic activity, and proliferation. Such assays are essential for characterizing T cell specificity, functionality, and avidity, providing insights into immune tolerance, cross-reactivity, and the potential for antigen-driven immunotherapies in preclinical mouse models.

Vaccine development research: Gp100 (25-33), mouse is frequently employed in the design and evaluation of peptide-based vaccines targeting melanoma-associated antigens. By incorporating this epitope into immunization protocols, researchers can analyze the induction of antigen-specific T cell responses, the magnitude and quality of immune memory, and the potential for breaking tolerance against self-antigens. These studies inform the rational design of next-generation cancer vaccines and adjuvant strategies for augmenting anti-tumor immunity.

Peptide-MHC binding studies: The defined sequence and immunogenic properties of this peptide make it an ideal substrate for quantitative assays measuring binding affinity and stability with various murine MHC class I alleles. Such investigations utilize in vitro binding assays, structural analyses, and computational modeling to elucidate the determinants of peptide-MHC interactions. Insights gained from these studies contribute to the broader understanding of antigen presentation, epitope selection, and the prediction of immunodominant peptides in the context of cancer and autoimmunity.

Immunological assay development: The availability of a well-characterized peptide epitope like Gp100 (25-33), mouse supports the optimization and validation of diverse immunological assays, including ELISPOT, intracellular cytokine staining, and flow cytometric detection of antigen-specific T cells. By serving as a positive control or experimental stimulus, the peptide enhances assay sensitivity, specificity, and reproducibility, thereby facilitating robust immune monitoring in basic and translational research settings. The use of such defined peptide reagents is critical for standardizing experimental protocols and ensuring the reliability of immunological data across laboratories.

Shipping Condition
Room temperature in continental US; may vary elsewhere.
InChI
InChI=1S/C46H69N15O17/c1-21(2)14-31(45(77)78)61-41(73)28(15-22-18-53-25-7-4-3-6-23(22)25)58-43(75)30(17-37(68)69)60-40(72)27(10-11-33(48)63)57-42(74)29(16-34(49)64)59-39(71)26(8-5-13-52-46(50)51)56-44(76)32(20-62)55-35(65)19-54-38(70)24(47)9-12-36(66)67/h3-4,6-7,18,21,24,26-32,53,62H,5,8-17,19-20,47H2,1-2H3,(H2,48,63)(H2,49,64)(H,54,70)(H,55,65)(H,56,76)(H,57,74)(H,58,75)(H,59,71)(H,60,72)(H,61,73)(H,66,67)(H,68,69)(H,77,78)(H4,50,51,52)/t24-,26-,27-,28-,29-,30-,31-,32-/m0/s1
InChI Key
NPNKXFJFJDAUNM-OAXMMLDDSA-N
References
1. Gal Cafri, et al. Production of LacZ inducible T cell hybridoma specific for human and mouse gp100₂₅₋₃₃ peptides. PLoS One. 2013;8(2):e55583.

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