Anti-Emerin/EMD Antibody Picoband®

Emerin is a serine-rich nuclear membrane protein that in humans is encoded by the EMD gene. And this gene is mapped to Xq28. Emerin is a member of the nuclear lamina-associated protein family. It mediates membrane anchorage to the cytoskeleton. Emery–Dreifuss muscular dystrophy is an X-linked inherited degenerative myopathy resulting from mutation in the EMD (also known clinically as STA) gene. Emerin appears to be involved in mechanotransduction, as emerin-deficient mouse fibroblasts failed to transduce normal mechanosensitive gene expression responses to strain stimuli. In cardiac muscle, emerin is also found complexed to beta-catenin at adherens junctions of intercalated discs, and cardiomyocytes from hearts lacking emerin showed beta-catenin redistribution as well as perturbed intercalated disc architecture and myocyte shape. This interaction appears to be regulated by glycogen synthase kinase 3 beta.

A synthetic peptide corresponding to a sequence at the N-terminus of human Emerin, different from the related mouse sequence by eight amino acids, and from the related rat sequence by nine amino acids.

Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta- catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD. Required for proper localization of non-farnesylated prelamin-A/C. .

1. Entrez Gene: EMD emerin (Emery–Dreifuss muscular dystrophy) . 2. Lammerding, J; Hsiao, J; Schulze, PC; Kozlov, S; Stewart, CL; Lee, RT (29 August 2005) . Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells.. The Journal of Cell Biology. 170 (5) : 781–91. 3. Nagano A, Koga R, Ogawa M, Kurano Y, Kawada J, Okada R, Hayashi YK, Tsukahara T, Arahata K (Mar 1996) . Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy. Nature Genetics. 12 (3) : 254–9.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Nucleus inner membrane ; Single-pass membrane protein; Nucleoplasmic side . Nucleus outer membrane. Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non- farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus.