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背景介绍 IL-15 has been shown to be produced by human fetal astrocytes and microglial cells in response to IL-1beta, IFN-gamma, or TNF- alpha and may thus play a role in T-cell mediated immune responses in the human central nervous system. IL-15 stimulates proliferation of the established T-cell line CTLL-2, CD8(+) memory T- cells require IL-15 for proliferation. IL-15 is also able to induce generation of cytolytic cells and LAK cells activity in vitro. IL-15 appears to function as a specific maturation factor for NK-cells and can mimic the bone marrow microenvironment in vitro, which is required for NK- cells to acquire lytic functions. IL-15 induces proliferation of mast cells in the absence of functional IL-2 receptor components and utilizes a receptor of 60-65 kDa that is distinct from known components of T-cell IL-15 receptors. The IL-15 receptor on mast cells recruits JAK2 and STAT5, instead of JAK1, JAK3, and STAT3 and STAT5 that are activated in T-cells. The alpha subunit of the IL-15 receptor (IL-15RA) is structurally related to the alpha subunit of the IL-2 receptor and confers high affinity binding of IL-15 to its receptor. IL-15 binds to the beta and gamma chains of the IL2 receptor, which are known to be required for ligand internalization and signal transduction. 产品介绍 Recombinant Interleukin-15 is a disulfide-linked homodimeric protein consisting of two 115 amino acid residues, and migrates as an approximately 13 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding human Interleukin-15 mature chain was expressed in E. coli.
询价背景介绍 IL-15 has been shown to be produced by human fetal astrocytes and microglial cells in response to IL-1beta, IFN-gamma, or TNF- alpha and may thus play a role in T-cell mediated immune responses in the human central nervous system. IL-15 stimulates proliferation of the established T-cell line CTLL-2, CD8(+) memory T- cells require IL-15 for proliferation. IL-15 is also able to induce generation of cytolytic cells and LAK cells activity in vitro. IL-15 appears to function as a specific maturation factor for NK-cells and can mimic the bone marrow microenvironment in vitro, which is required for NK- cells to acquire lytic functions. IL-15 induces proliferation of mast cells in the absence of functional IL-2 receptor components and utilizes a receptor of 60-65 kDa that is distinct from known components of T-cell IL-15 receptors. The IL-15 receptor on mast cells recruits JAK2 and STAT5, instead of JAK1, JAK3, and STAT3 and STAT5 that are activated in T-cells. The alpha subunit of the IL-15 receptor (IL-15RA) is structurally related to the alpha subunit of the IL-2 receptor and confers high affinity binding of IL-15 to its receptor. IL-15 binds to the beta and gamma chains of the IL2 receptor, which are known to be required for ligand internalization and signal transduction. 产品介绍 Recombinant Interleukin-15 is a disulfide-linked homodimeric protein consisting of two 115 amino acid residues, and migrates as an approximately 13 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding human Interleukin-15 mature chain was expressed in E. coli.
询价背景介绍 PARP1 is known to bind damaged DNA through its N-terminal zinc finger domain. After PARP1 ribosylates itself (autoribosylation), it dissociates from DNA due to the accumulated negative charge of the ribosyl polymer. Trapped PARP-DNA complexes have been shown to be cytotoxic to cancer cells. 产品介绍 The PARPtrap™ Assay Kit for PARP1 is designed to measure PARP1/DNA complex formation in a high throughput screening assay using fluorescence polarization (FP). PARP1 is known to bind damaged DNA through its DNA-binding domains. Binding to DNA activates PARP1 and in the presence of NAD+ PARP1 ribosylates itself (auto-ribosylation), what in consequence leads to PARP1 dissociation from the DNA due to the accumulated negative charge of the ribosyl polymer. In the presence of some inhibitors, however, PARP remains bound to the DNA, a phenomenon termed trapping. Trapped PARP-DNA complexes have been shown to be highly cytotoxic to cancer cells, therefore such inhibitors may be desirable for cancer treatment. The key to the PARPtrap™ Assay Kit for PARP1 is the fluorescent-labeled oligonucleotide duplex. In the absence of ribosylation, PARP1 binds to the fluorescent probe, forming a large complex and resulting in the emission of highly polarized light. However, after auto-ribosylation, PARP1 dissociates from the oligonucleotide duplex, which then rotates freely, emitting less polarized light (Fig. 1). Addition of a PARP1 inhibitor results in trapping of PARP1 to the fluorescent oligonucleotide duplex, and increases the FP signal in a dose dependent manner. The PARPtrap™ Assay Kit for PARP1 is a fluorescence polarization homogeneous assay. The FP signal is measured using a fluorescent microplate reader capable of measuring fluorescence polarization.
询价背景介绍 PARP1 is known to bind damaged DNA through its N-terminal zinc finger domain. After PARP1 ribosylates itself (autoribosylation), it dissociates from DNA due to the accumulated negative charge of the ribosyl polymer. Trapped PARP-DNA complexes have been shown to be cytotoxic to cancer cells. 产品介绍 The PARPtrap™ Assay Kit for PARP1 is designed to measure PARP1/DNA complex formation in a high throughput screening assay using fluorescence polarization (FP). PARP1 is known to bind damaged DNA through its DNA-binding domains. Binding to DNA activates PARP1 and in the presence of NAD+ PARP1 ribosylates itself (auto-ribosylation), what in consequence leads to PARP1 dissociation from the DNA due to the accumulated negative charge of the ribosyl polymer. In the presence of some inhibitors, however, PARP remains bound to the DNA, a phenomenon termed trapping. Trapped PARP-DNA complexes have been shown to be highly cytotoxic to cancer cells, therefore such inhibitors may be desirable for cancer treatment. The key to the PARPtrap™ Assay Kit for PARP1 is the fluorescent-labeled oligonucleotide duplex. In the absence of ribosylation, PARP1 binds to the fluorescent probe, forming a large complex and resulting in the emission of highly polarized light. However, after auto-ribosylation, PARP1 dissociates from the oligonucleotide duplex, which then rotates freely, emitting less polarized light (Fig. 1). Addition of a PARP1 inhibitor results in trapping of PARP1 to the fluorescent oligonucleotide duplex, and increases the FP signal in a dose dependent manner. The PARPtrap™ Assay Kit for PARP1 is a fluorescence polarization homogeneous assay. The FP signal is measured using a fluorescent microplate reader capable of measuring fluorescence polarization.
询价背景介绍 Caspase-3 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. 产品介绍 Human caspase 3 (CASP3), also known as CPP32 and apopain, a.a. 1 - 277 (end) (GenBank Accession No. NM_004346, var alpha) with C-terminal His-tag, expressed in an E. coli expression system. Procaspase-3 is self-cleaved into two subunits, MW = 17 kDa and 13 kDa, to form the active heterotetrameric complex.
询价背景介绍 Caspase-3 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. 产品介绍 Human caspase 3 (CASP3), also known as CPP32 and apopain, a.a. 1 - 277 (end) (GenBank Accession No. NM_004346, var alpha) with C-terminal His-tag, expressed in an E. coli expression system. Procaspase-3 is self-cleaved into two subunits, MW = 17 kDa and 13 kDa, to form the active heterotetrameric complex.
询价产品介绍 Human Casitas B-lineage lymphoma proto-oncogene b (CBL-B), also known as E3 ubiquitin-protein ligase CBL-B, RING finger protein 56, and SH3- binding protein CBL-B with Y363F mutation GenBank Accession No. NM_170662, a.a. 39 - 426 with N-terminal His-tag and N-terminal Avi-tag, expressed in an E. coli expression system. This protein was enzymatically biotinylated in vivo using AviTag™ technology. MW=48 kDa.
询价产品介绍 Human Casitas B-lineage lymphoma proto-oncogene b (CBL-B), also known as E3 ubiquitin-protein ligase CBL-B, RING finger protein 56, and SH3- binding protein CBL-B with Y363F mutation GenBank Accession No. NM_170662, a.a. 39 - 426 with N-terminal His-tag and N-terminal Avi-tag, expressed in an E. coli expression system. This protein was enzymatically biotinylated in vivo using AviTag™ technology. MW=48 kDa.
询价产品介绍 Human Casitas B-lineage lymphoma proto-oncogene b (CBL-B), also known as E3 ubiquitin-protein ligase CBL-B, RING finger protein 56, and SH3- binding protein CBL-B GenBank Accession No. NM_170662, a.a. 39 - 426 with N-terminal His-tag and N-terminal Avi-tag, expressed in an E. coli expression system. This protein was enzymatically biotinylated in vivo using AviTag™ technology. MW=48 kDa.
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