Peptides & Amino Acids

gp100 (280-288) A288V HLA-A*0201 antigen peptide – YLEPGPVTV SB-PEPTIDE offers gp100 (280-288) A288V variant peptide – YLEPGPVTV for its promising use in immunotherapy. gp100 protein: potent melanoma-specific antigen gp100 (Uniprot: P40967) 661 amino acids long type I transmembrane glycoprotein, also known as premelanosome protein (PMEL) for the gene encoding it, is primarily known for its crucial role in melanosome morphogenesis and pigmentation. Indeed, it orchestrates the maturation of these organelles, that are responsible for melanin synthesis, storage, and transport. More than its implication in melanosome maturation, melanogenesis, biogenesis, and melanin polymerization, gp100 has gained significant attention and recognition as tumor-associated antigen (TAA). Hance, its dynamic and multifaceted nature piqued the interest of researchers and immunobiologists to explore PMEL’s potential in shaping the future of cancer treatment. gp100 280-288 immunogenic epitope – YL

Biotin-PEG-Thiol (MW 2000) is an active, pegylated compound that binds to streptavidin or antibiotin with high affinity and specificity. It is capable of modifying biomolecules, proteins, peptides, and other small molecular materials. This compound is commonly utilized in agent release research and the development of novel nanomaterials [1].

MAGE (melanoma associated antigen) proteins are CT (cancer testis) antigens, and there are about 60 proteins in the MAGE family that can be subdivided into type I (present only on the X-chromosome, MAGE-A, B, and C) and type II (MAGE D-L and necdin). Under normal conditions they are mostly found in the testis and placenta. They are found at high levels in several cancer types, such as melanoma, brain, and breast cancer, and are involved in the development of resistance to chemotherapy, cell motility and cell survival. Expression of MAGE proteins tend to correlate with a poor prognosis. They are intracellular proteins, with MAGE-A1 being mostly cytosolic, making them poor targets for strategies such as CAR-T cell therapy. MAGE proteins are degraded in the proteosome, and the peptides created can then be found on the cell membrane in combination with MHC (major histocompatibility complex) I. The presentation on the cell surface in this form makes them an attractive target for TCR (T cell

MAGE (melanoma associated antigen) proteins are CT (cancer testis) antigens, and there are about 60 proteins in the MAGE family that can be subdivided into type I (present only on the X-chromosome, MAGE-A, B, and C) and type II (MAGE D-L and necdin). Under normal conditions they are mostly found in the testis and placenta. They are found at high levels in several cancer types, such as melanoma, brain, and breast cancer, and are involved in the development of resistance to chemotherapy, cell motility, and cell survival. Expression of MAGE proteins tend to correlate with a poor prognosis. They are intracellular proteins, with MAGE-A1 being mostly cytosolic, making them poor targets for strategies such as CAR-T cell therapy. MAGE proteins are degraded in the proteosome, and the peptides created can then be found on the cell membrane in combination with MHC (major histocompatibility complex) I. The presentation on the cell surface in this form makes them an attractive target for TCR (T cel

KRAS (Kirsten rat sarcoma virus) are GTPase proteins. They cycle between a GDP-bound inactive state and a GTP-bound (active) form, in a process regulated by two accessory proteins: GEF (guanine exchange factors) and GAPs (GTPase activating proteins). Once activated KRAS can bind to its effectors and regulate multiple signaling pathways, such as the RAF (rapidly accelerated fibrosarcoma)-MEK (mitogen activated protein kinase)-ERK (extracellular regulated kinase) or the PI3K (phosphoinositide 3-kinase)-AKT (protein kinase B)-mTOR (mammalian target of rapamycin) signaling pathways. KRAS mutations account for about 85% of all RAS mutations and are considered one of the main drivers of human cancer, such as in PDAC (pancreatic ductal adenocarcinoma). One of the amino acids frequently mutated is glycine 12, with the most common form being G12D. Since KRAS are intracellular proteins, they are not amenable to CAR (chimeric antigen receptor)-T cell-based therapies, and the development of inhibi

KRAS (Kirsten rat sarcoma virus) are GTPase proteins. They cycle between GDP-bound inactive state and a GTP-bound (active) form, in a process regulated by two accessory proteins: GEF (guanine exchange factors) and GAPs (GTPase activating proteins). Once activated KRAS can bind to its effectors and regulate multiple signaling pathways, such as the RAF (rapidly accelerated fibrosarcoma)-MEK (mitogen activated protein kinase)-ERK (extracellular regulated kinase) or the PI3K (phosphoinositide 3-kinase)-AKT (protein kinase B)-mTOR (mammalian target of rapamycin) signaling pathways. KRAS mutations account for about 85% of all RAS mutations and are considered one of the main drivers of human cancer, such as in PDAC (pancreatic ductal adenocarcinoma). One of the amino acids frequently mutated is glycine 12, with the most common form being G12D. Since KRAS are intracellular proteins, they are not amenable to CAR (chimeric antigen receptor)-T cell-based therapies, and the development of inhibito

KRAS (Kirsten rat sarcoma virus) are GTPase proteins. They cycle between a GDP-bound inactive state and a GTP-bound (active) form, in a process regulated by two accessory proteins: GEF (guanine exchange factors) and GAPs (GTPase activating proteins). Once activated KRAS can bind to its effectors and regulate multiple signaling pathways, such as the RAF (rapidly accelerated fibrosarcoma)-MEK (mitogen activated protein kinase)-ERK (extracellular regulated kinase) or the PI3K (phosphoinositide 3-kinase)-AKT (protein kinase B)-mTOR (mammalian target of rapamycin) signaling pathways. KRAS mutations account for about 85% of all RAS mutations and are considered one of the main drivers of human cancer, such as in PDAC (pancreatic ductal adenocarcinoma). One of the amino acids frequently mutated is glycine 12, with the most common form being G12D. Since KRAS are intracellular proteins, they are not amenable to CAR (chimeric antigen receptor)-T cell-based therapies, and the development of inhibi

KRAS (Kirsten rat sarcoma virus) are GTPase proteins. They cycle between a GDP-bound inactive state and a GTP-bound (active) form, in a process regulated by two accessory proteins: GEF (guanine exchange factors) and GAPs (GTPase activating proteins). Once activated KRAS can bind to its effectors and regulate multiple signaling pathways, such as the RAF (rapidly accelerated fibrosarcoma)-MEK (mitogen activated protein kinase)-ERK (extracellular regulated kinase) or the PI3K (phosphoinositide 3-kinase)-AKT (protein kinase B)-mTOR (mammalian target of rapamycin) signaling pathways. KRAS mutations account for about 85% of all RAS mutations and are considered one of the main drivers of human cancer, such as in PDAC (pancreatic ductal adenocarcinoma). One of the amino acids frequently mutated is glycine 12, with the most common form being G12D. Since KRAS are intracellular proteins, they are not amenable to CAR (chimeric antigen receptor)-T cell-based therapies, and the development of inhibi

MAGE (melanoma associated antigen) proteins are CT (cancer testis) antigens, and there are about 60 proteins in the MAGE family that can be subdivided into type I (present only on the X-chromosome, MAGE-A, B, and C) and type II (MAGE D-L and necdin). Under normal conditions they are mostly found in the testis and placenta. They are found at high levels in several cancer types, such as melanoma, brain, and breast cancer, and are involved in the development of resistance to chemotherapy, cell motility, and cell survival. Expression of MAGE proteins tend to correlate with a poor prognosis. They are intracellular proteins, with MAGE-A4 being found in the cytosol and nucleus, making them poor targets for strategies such as CAR-T cell therapy. MAGE proteins are degraded in the proteosome, and the peptides created can then be found on the cell membrane in combination with MHC (major histocompatibility complex) I. The presentation on the cell surface in this form makes them an attractive targe