Monoclonal Anti-LAP2 (TMPO) (mouse IgG1 isotype) is derived from the 6E10 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide (amino acids 29-50) common to the N-terminus of all TMPOs. Thymopoietin β (TMPOβ)/lamina associated polypeptide 2 (LAP2) is a type II integral protein of the inner nuclear envelope (NE). In mammalian cells, six alternatively spliced TMPO isoforms, designated α, β, β′, γ, δ, ε, and ζ have been isolated and characterized. LAP2/TMPO proteins is highly conserved in mammals and Xenopus. The expression of the various TMPO isoforms is ubiquitous, with higher levels in proliferative tissues. It has four domains: a hydrophilic C-terminus domain, a hydrophobic transmembrane domain, a NE targeting and lamina-binding domain, and a chromatin binding domain. TMPOβ/LAP2 contains two putative p34cdc2 kinase phosphorylation sites.
synthetic peptide corresponding to amino acids 29-50 common to the N-terminus of all human TMPOs (isoforms α, β, γ, δ, ε, and ζ).
Monoclonal Anti-LAP2 (TMPO) antibody produced in mouse may be used in immunoblotting and immunocytochemistry.
Thymopoietin β (TMPOβ)/lamina associated polypeptide 2 (LAP2) is putatively involved in functional nuclear architecture and cell cycle control. TMPOβ/LAP2 plays a key role in nuclear envelope (NE) disassembly and reassembly during mitosis and linking chromatin to the NE in interphase. TMPOβ/LAP2 binds lamin B1 and chromosomes in a phosphorylation dependent manner. TMPOβ/LAP2, either together with germ-cell-less (GCL) or alone, can repress the transcriptional activity of the elongation factor 2-dimerization partner (E2F-DP) heterodimer. TMPOα/LAP2 has a role in regulating the dynamics of the nuclear lamina and this interaction is required for nuclear growth after mitosis.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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