Elisa Assay For Hbv

Description: HBV(+) and HBV(-) noncancerous liver tissue array, 80 cases/ 160 cores, replaced by LV1601a

Description: True Blue

Description: True Blue

Description: True Blue

Description: True Blue

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: How a therapeutic antibody is metabolized in the body is pertinently relevant to its efficacy. Therefore, pharmacokinetics study is an important part of the drug development. HER-2 is probably the most targeted molecule in today’s pharmaceutical industry, thanking to the clinical success of Herceptin®. Many investigational anti-HER-2 mAbs are being developed. There is a growing need for a standard assay that can be used to facilitate the study of their pharmacokinetics.

Description: CTLA-4 (Cytotoxic T-Lymphocyte Antigen 4) is also known as CD152 (Cluster of differentiation 152), is a protein receptor that downregulates the immune system. CTLA4 is a member of the immunoglobulin superfamily, which is expressed on the surface of Helper T cells and transmits an inhibitory signal to T cells. The protein contains an extracellular V domain, a transmembrane domain, and a cytoplasmic tail. Alternate splice variants, encoding different isoforms. CTLA4 is similar to the T-cell co-stimulatory protein, CD28, and both molecules bind to CD80 and CD86, also called B7-1 and B7-2 respectively, on antigen-presenting cells. CTLA4 transmits an inhibitory signal to T cells, whereas CD28 transmits a stimulatory signal. Intracellular CTLA4 is also found in regulatory T cells and may be important to their function. Fusion proteins of CTLA4 and antibodies (CTLA4-Ig) have been used in clinical trials for rheumatoid arthritis.

Description: CTLA-4 (Cytotoxic T-Lymphocyte Antigen 4) is also known as CD152 (Cluster of differentiation 152), is a protein receptor that downregulates the immune system. CTLA4 is a member of the immunoglobulin superfamily, which is expressed on the surface of Helper T cells and transmits an inhibitory signal to T cells. The protein contains an extracellular V domain, a transmembrane domain, and a cytoplasmic tail. Alternate splice variants, encoding different isoforms. CTLA4 is similar to the T-cell co-stimulatory protein, CD28, and both molecules bind to CD80 and CD86, also called B7-1 and B7-2 respectively, on antigen-presenting cells. CTLA4 transmits an inhibitory signal to T cells, whereas CD28 transmits a stimulatory signal. Intracellular CTLA4 is also found in regulatory T cells and may be important to their function. Fusion proteins of CTLA4 and antibodies (CTLA4-Ig) have been used in clinical trials for rheumatoid arthritis.

Description: How a therapeutic antibody is metabolized in the body is pertinently relevant to its efficacy. Therefore, pharmacokinetics study is an important part of the drug development. CTLA-4 is probably the most targeted molecule in today’s pharmaceutical industry, thanking to the clinical success of Yervoy®. Many investigational anti-CTLA-4 mAbs are being developed. There is a growing need for a standard assay that can be used to facilitate the study of their pharmacokinetics.

Description: The PARPtrap™ Assay Kit for PARP2 is designed to measure PARP2/DNA complex formation in a high throughput screening assay using fluorescence polarization (FP). Similarly, to PARP1, PARP2 recognizes and binds damaged DNA via its DNA-binding domain. Binding to DNA activates PARP2 and in the presence of NAD+ PARP2 ribosylates itself (auto-ribosylation), which leads to PARP2 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 is the fluorescent-labeled oligonucleotide duplex. In the absence of ribosylation, PARP2 binds to the fluorescent probe, forming a large complex and resulting in the emission of highly polarized light. However, after auto-ribosylation PARP2 dissociates from the oligonucleotide duplex, which then rotates freely, emitting less polarized light (Fig. 1). Addition of a PARP2 inhibitor results in trapping of PARP2 to the fluorescent oligonucleotide duplex, and increases the FP signal in a dose dependent manner.The PARPtrap™ Assay Kit is a fluorescence polarization homogeneous assay. The FP signal is measured using a fluorescent microplate reader capable of measuring fluorescence polarization.

Description: The PARPtrap™ Assay Kit for PARP2 is designed to measure PARP2/DNA complex formation in a high throughput screening assay using fluorescence polarization (FP). Similarly, to PARP1, PARP2 recognizes and binds damaged DNA via its DNA-binding domain. Binding to DNA activates PARP2 and in the presence of NAD+ PARP2 ribosylates itself (auto-ribosylation), which leads to PARP2 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 is the fluorescent-labeled oligonucleotide duplex. In the absence of ribosylation, PARP2 binds to the fluorescent probe, forming a large complex and resulting in the emission of highly polarized light. However, after auto-ribosylation PARP2 dissociates from the oligonucleotide duplex, which then rotates freely, emitting less polarized light (Fig. 1). Addition of a PARP2 inhibitor results in trapping of PARP2 to the fluorescent oligonucleotide duplex, and increases the FP signal in a dose dependent manner.The PARPtrap™ Assay Kit is a fluorescence polarization homogeneous assay. The FP signal is measured using a fluorescent microplate reader capable of measuring fluorescence polarization.

Description: 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.