Anti-Emerin/EMD Antibody Picoband®

Overview

This antibody is intended for detection of EMD (Emerin) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.

Vendor notes: Boster Bio Anti-Emerin/EMD Antibody Picoband® catalog # A00714. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Key elements and design rationale

• Antibody format: Rabbit Polyclonal Rabbit IgG
• Immunogen / epitope context: 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.
• Molecular weight context: reported MW: 34 kDa; calculated MW: 28994 MW
• Reactivity: Human,Mouse,Rat
• Applications: Flow Cytometry, IF, IHC, ICC, WB

As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.

Biological background

Emerin; Emerin. 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. Functional note: 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. . Reported localization: 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. Expression/tissue context: Skeletal muscle, heart, colon, testis, ovary and pancreas.

Research relevance and current trends

• Biochemicals: Researchers commonly examine how EMD (Emerin) relates to this theme using model systems and orthogonal readouts.
• Chemical Type: Researchers commonly examine how EMD (Emerin) relates to this theme using model systems and orthogonal readouts.
• Neuroscience: Researchers commonly examine how EMD (Emerin) relates to this theme using model systems and orthogonal readouts.

Common research applications

• Western blotting: compare relative EMD (Emerin) levels across conditions; band patterns may reflect isoforms and processing.
• IHC/IHC-F: assess spatial distribution of EMD (Emerin) across tissue regions and cell types using matched controls.
• IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
• Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.

Notes for experimental interpretation

• Specificity notes: No cross reactivity with other proteins.
• Cross-reactivity: No cross-reactivity with other proteins
• Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
• Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.

Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.