Viral Vectors & Particles

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 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-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 target

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 target

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

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

Tumor necrosis factor (TNF, also known as TNFα) is a cytokine produced predominantly by activated macrophages and T lymphocytes. It has been identified as a key regulator in inflammatory and immune responses. TNF signaling pathways are triggered by binding to one of two distinct receptors, designated TNFR1 (TNF receptor 1) and TNFR2, which are differentially regulated on various cell types in normal and diseased tissues. TNFα exists in both a trimeric membrane-bound form (mTNFα) and as a soluble protein.  TNFα is synthetized in a precursor form, a cell surface type II transmembrane protein, which is cleaved by metalloproteinases such as TACE (TNFα converting enzyme) into a soluble peptide. Soluble TNFα can then bind to its receptors and activate downstream signaling pathways. Transmembrane TNFα can also bind to TNFα receptors and induce cellular responses. For instance,  it can enhance cytotoxicity in NK cells, while in the liver it can trigger hepatitis. Anti-TNFα antibodies can bind