EPLIN Antibody recognizes endogenous levels of total EPLIN protein, including EPLIN-α and EPLIN-β isoforms.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly450 of full-length human EPLIN-β protein, which corresponds to Gly290 of EPLIN-α protein. Antibodies are purified by protein A and peptide affinity chromatography.
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Specificity / Sensitivity
EPLIN Antibody recognizes endogenous levels of total EPLIN protein, including EPLIN-α and EPLIN-β isoforms.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly450 of full-length human EPLIN-β protein, which corresponds to Gly290 of EPLIN-α protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Epithelial Protein Lost in Neoplasm (EPLIN) is an actin-binding protein that regulates actin filament dynamics and cross-linking (1). Alpha and beta isoforms are generated from alternate promoters, with the EPLIN-β isoform representing the full-length protein and the EPLIN-α isoform lacking the amino-terminal 160 amino acids (2). Increased expression of EPLIN protein results in more abundant and larger actin stress fibers due to stabilizing of cross-links and inhibition of actin depolymerization. EPLIN protein inhibits Rac1-promoted membrane ruffling and Arp2/3-associated actin filament branching (1).
Research studies demonstrate reduced EPLIN-α expression in tumor tissues, and correlate this reduction with increased invasiveness and poor clinical outcomes (3). The EPLIN protein is an important negative regulator of the epithelial-mesenchymal transition (EMT)(4). While EMT is a critical process during normal embryonic development, dysregulation in transformed cells is a key step in the transition to metastasis (5).