Figure 1. Detection of c-Myc protein is examined across multiple cell lines using the PathScan® Total c-Myc Chemiluminescent Sandwich ELISA Kit. Immediate light generation with chemiluminescent substrate is shown in the top figure, while the corresponding western blot using c-Myc (D3N8F) Rabbit mAb #13987 shown in the bottom figure.Learn more about how we get our images
Figure 2. The relationship between protein concentration of cell lysate and immediate light generation with chemiluminescent substrate as detected by the PathScan® Total c-Myc Chemiluminescent Sandwich ELISA Kit is shown. HeLa cells (85% confluent) were harvested and then lysed with the Cell Lysis Buffer #9803.Learn more about how we get our images
The PathScan® Total c-Myc Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of c-Myc protein with a chemiluminescent readout. Chemiluminescent ELISAs often have a wider dynamic range and higher sensitivity than conventional chromogenic detection. This chemiluminescent ELISA, which is offered in low volume microplates, shows increased signal and sensitivity while using a smaller sample size. A c-Myc rabbit mAb has been coated on the microwells. After incubation with cell lysates, c-Myc proteins are captured by the coated antibody. Following extensive washing, a c-Myc mouse mAb is added to detect the captured c-Myc protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. Chemiluminescent reagent is added for signal development. The magnitude of light emission, measured in relative light units (RLU), is proportional to the quantity of c-Myc protein.
Antibodies in kit are custom formulations specific to kit.
PathScan® Total c-Myc Chemiluminescent Sandwich ELISA Kit detects endogenous levels of c-Myc in human or mouse cells. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc. PathScan is a trademark of Cell Signaling Technology, Inc.
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