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PathScan® RP TACSTD2/TROP2 Sandwich ELISA Kit #95446

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  • ELISA

Important Ordering Details

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    Supporting Data

    REACTIVITY H
    Application Key:
    • ELISA-ELISA 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    The rapid protocol (RP) PathScan® RP TACSTD2/TROP2 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of TACSTD2/TROP2 protein in a reduced assay time of 1.5 hours. Incubation of cell lysates and detection antibody on the coated microwell plate forms a sandwich with TACSTD2/TROP2 in a single step. The plate is then extensively washed and TMB reagent is added for signal development. The magnitude of absorbance for the developed color is proportional to the quantity of TACSTD2/TROP2 protein. Learn more about your ELISA kit options here.

    *Antibodies in this kit are custom formulations specific to kit.

    Protocol

    Specificity / Sensitivity

    The PathScan® RP TACSTD2/TROP2 Sandwich ELISA Kit detects endogenous levels of TACSTD2/TROP2 protein. The kit sensitivity is shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.

    Species Reactivity:

    Human

    Background

    TROP2 is a transmembrane glycoprotein encoded by gene TACSTD2 (tumor-associated calcium signal transducer 2). TROP2 was first discovered as a biomarker of invasive trophoblast cells and later reported in many types of cancer cells, in various organs during development, and adult stem cells during homeostasis (1,2). TROP2 has an extracellular domain with EGF thyroglobulin type-1 repeats, a transmembrane domain, and a short cytoplasmic tail with a HIKE domain containing a PIP2 binding site and PKC phosphorylation site (Ser303) (1-4). TROP2 functions by regulating multiple signaling pathways, including the interaction of its extracellular domain with integrin beta1 to regulate FAK signaling, the association of its transmembrane domain with claudin-1 and claudin-7 for tight junction formation, and the regulation of intracellular calcium release by its PIP2 binding and activation of the ERK/MAPK pathway (1,2,5-8). All these functions are important for its role in tumor proliferation, metastasis, and invasion (1,2). PKC can phosphorylate TROP2 at Ser303; the phosphorylation changes the cytoplasmic tail conformation and further promotes its signaling (9). TROP2 can be activated through intramembrane proteolysis first by TACE, followed by further cleavage by Presenilin 1 and Presenilin 2. The proteolysis process is required for its role in tumor cell proliferation (10,11).
    For Research Use Only. Not for Use in Diagnostic Procedures.
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