Assays & Kits

Sandwich TR-FRET immunoassay for the quantitative measurement of human CCL17 (C-C motif chemokine 17; CC chemokine TARC) in cell culture supernatants. The kit does not include a recombinant human CCL17/TARC standard, which must be purchased separately from R&D Systems® (catalog number 364-DN).

Sandwich TR-FRET immunoassay for the quantitative measurement of human CCL17 (C-C motif chemokine 17; CC chemokine TARC) in cell culture supernatants. The kit does not include a recombinant human CCL17/TARC standard, which must be purchased separately from R&D Systems® (catalog number 364-DN).

Sandwich TR-FRET immunoassay for the quantitative measurement of human CCL17 (C-C motif chemokine 17; CC chemokine TARC) in cell culture supernatants. The kit does not include a recombinant human CCL17/TARC standard, which must be purchased separately from R&D Systems® (catalog number 364-DN).

DR3 (death receptor 3), also known as tumor necrosis factor receptor superfamily member 25 or TNFRSF25, is a membrane receptor of the tumor necrosis factor receptor superfamily of proteins (TNFRSF), which associates with TL1A (TNF-like protein 1A) in T and NK cells. DR3 has been recognized as a significant anti-apoptotic and differentiation factor and it is a co-stimulatory receptor. TL1A, also called TNFSF15, is a member of the tumor necrosis factor family. It is expressed in different immune cells, such as monocyte, macrophage, dendritic cell, T cell and non-immune cells. TL1A competitively binds to DR3, having a higher affinity for DcR3 (decoy receptor 3), providing stimulatory signal for downstream signaling pathways. It then regulates proliferation, activation, apoptosis, and chemokine production in effector cells. The role of DR3 in T cell activation, and consequently in cytokine secretion and cell proliferation, makes it an attractive target in cancer therapy. Inhibition of DR3-

DR3 (death receptor 3), also known as tumor necrosis factor receptor superfamily member 25 or TNFRSF25, is a membrane receptor of the tumor necrosis factor receptor superfamily of proteins (TNFRSF), which associates with TL1A (TNF-like protein 1A) in T and NK cells. DR3 has been recognized as a significant anti-apoptotic and differentiation factor and it is a co-stimulatory receptor. TL1A, also called TNFSF15, is a member of the tumor necrosis factor family. It is expressed in different immune cells, such as monocyte, macrophage, dendritic cell, T cell and non-immune cells. TL1A competitively binds to DR3, having a higher affinity for DcR3 (decoy receptor 3), providing stimulatory signal for downstream signaling pathways. It then regulates proliferation, activation, apoptosis, and chemokine production in effector cells. The role of DR3 in T cell activation, and consequently in cytokine secretion and cell proliferation, makes it an attractive target in cancer therapy. Inhibition of DR3-

ACHE (acetylcholinesterase), also known as AChase or acetylhydrolase, is known to hydrolyze acetylcholine (ACh), a naturally occurring neurotransmitter, into acetic acid and choline. It is a highly effective hydrolase, with an activity near the limit of substrate diffusion. It can be found in motor and sensory neurons, and it is involved in the termination of impulse transmission, by being located on the post-synaptic membrane and hydrolyzing Ach. Ach can be taken up by and used to synthesize acetyl-Coa again in a reaction catalyzed by choline acetyltransferase. ACHE can exist in different molecular forms, which have different expression patterns. It has been known for many years that AD (Alzheimer€™s disease) patients have an abnormal distribution of these molecular forms, with an increase in the light forms versus G4 molecules. P-tau can lead to higher expression of T-ACHE, and ACHE may play a role in formation of beta-amyloid plaques. Inhibitors of ACHE result in high concentrations

ERK1 (extracellular signal-regulated kinase 1) is also known as mitogen-activated protein kinase 3 (MAPK3),  is a dual serine/threonine and tyrosine kinase. ERK (extracellular signal-regulated kinases), also known as classical MAPK (mitogen-activated protein kinases), are protein kinases involved in crucial intracellular signaling pathways, and regulate processes like mitoses, meiosis, and other functions. In the MAPK/ERK pathway Ras proteins are activated by several external molecules, including cytokines and viruses. These are followed by an activation cascade of c-Raf, MEK (mitogen-activated protein kinase kinase) and finally ERK. ERK1/2 in turn activates transcription factors. Disruption of the MAPK/ERK pathway at any point results in cancer. Inhibitors for Ras, Raf and MEK have been developed and result in rapid tumor reductions. However, resistance to treatment and relapse are quite frequent. This has led the field to focus on the development of ERK inhibitors, although these are

The Notch (neurogenic locus notch homolog protein) signaling is evolutionally highly conserved and implicated in various aspects of cancer development and progression. Aberrant activation of Notch1 signaling, often through mutations or overexpression, is associated with several types of cancer, including leukemia, breast cancer, lung cancer, and others. DLL4 (delta like canonical notch ligand 4), as a ligand of Notch receptors, can also influence tumor angiogenesis, promoting the growth of blood vessels within tumors and facilitating tumor progression. As Notch1 and DLL4 signaling pathway plays significant roles in cancer development, several Notch1 and DLL4 neutralizing antibodies have been evaluated in preclinical studies and clinical trials across various cancer types.

CD200 (Cluster of Differentiation 200) and its receptor, CD200R, are cell surface proteins that play a crucial role in immune regulation and tolerance. The CD200-CD200R pathway is primarily involved in inhibiting immune responses, helping to maintain immune homeostasis and prevent excessive inflammation. In many cancers, tumor cells overexpress CD200, which interacts with CD200R on immune cells, particularly myeloid cells like macrophages and dendritic cells. This interaction leads to the suppression of immune responses against the tumor, effectively promoting immune evasion. Neutralizing antibodies against CD200 or CD200R can block this interaction, preventing the inhibitory signal from being delivered to immune cells. As a result, the anti-tumor immune response is enhanced, leading to improved recognition and elimination of tumor cells by the immune system. The development of strategies targeting this complex holds great potential in cancer therapy.