Tag/Conjugate
Unconjugated
Purity
> 95 % by SDS-PAGE.
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.
Reconstitution
ZYX peptide is supplied as 1mg of dried peptide. When the peptide is reconstituted in 1 mL strile water, the concentration will be 1 mg/mL.
Introduction
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 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. Alternative splicing results in multiple transcript variants that encode the same isoform. [provided by RefSeq, Jul 2008]
Synonyms
ZYX; zyxin; ESP-2; HED-2; zyxin-2;
Citations
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Rottner, K; Krause, M; et al. Zyxin is not colocalized with vasodilator-stimulated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions. MOLECULAR BIOLOGY OF THE CELL 12:3103-3113(2001).
CRAWFORD, AW; PINO, JD; et al. BIOCHEMICAL AND MOLECULAR CHARACTERIZATION OF THE CHICKEN CYSTEINE-RICH PROTEIN, A DEVELOPMENTALLY-REGULATED LIM-DOMAIN PROTEIN THAT IS ASSOCIATED WITH THE ACTIN CYTOSKELETON. JOURNAL OF CELL BIOLOGY 124:117-127(1994).