Human ZYX (Zyxin) ELISA Kit

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Product specifications
Category | ELISA Kits |
Reactivity | Human |
Assay Data | 4 hours |
Assay Type | Sandwich ELISA, Double Antibody |
Test Range | 31.25-2000pg/ml |
Sensitivity | 18.75pg/ml |
Size 1 | 96T |
Tested Applications | ELISA |
Sample Type | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
Availability | Shipped within 10-14 working days. |
Storage | 2-8 °C for 12 months |
UniProt ID | Q15942 |
Alias | ZYX, Zyxin, Zyxin-2 |
Background | Elisa kits for ZYX |
Status | RUO |
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Human ZYX (Zyxin) ELISA Kit
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ZYX antibody
Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin(ZYX) is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles.
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ZYX antibody
Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin(ZYX) is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles.
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