Product Pathways - Apoptosis
LAP2α (3A3) Mouse mAb #5369
|W IF-IC||H Mk||Endogenous||76||Mouse IgG1|
Reactivity Key: H=Human Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
* Product-specific protocol.
Specificity / Sensitivity
LAP2α (3A3) Mouse mAb detects endogenous levels of total LAP2α protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human LAP2α protein.
Western blot analysis of extracts from various cell lines using LAP2α (3A3) Mouse mAb.
Lamins and lamin associated proteins are the major components of nuclear lamina found between the inner nuclear membrane and the peripheral chromatin. These proteins play important roles in maintaining nuclear structure, chromatin organization, DNA replication, cell cycle regulation, and apoptosis (1-3). Lamins are type V intermediate filaments that are further classified into type A and type B lamin proteins. Type A lamins (including lamin A and the smaller lamin C splice variant) are predominately expressed in terminally differentiated cells, whereas type B lamins (lamin B1, lamin B2) are encoded by distinct genes and are expressed constitutively. Cleavage of lamins by caspases occurs during apoptosis as part of the disassembly of the cell (4-6). A number of lamina-associated proteins contribute to the nuclear lamina and include the lamin B receptor, LAP1, LAP2, emerin, MAN1, otefin, and YA. Several isoforms of lamina-associated polypeptide 2 (LAP2, also known as thymopoietin or TMPO) have been described, with the α, β, and γ isoforms most abundant in humans (7-10). Structurally similar LAP2β and LAP2γ are type II integral membrane proteins. LAP2α has a unique carboxy-terminus that lacks a transmembrane region and results in localization of LAP2α throughout the nucleus where it can associate with lamin A/C (10). LAP2α is also thought to contribute to the nuclear anchorage of retinoblastoma protein (Rb) and control cell cycle progression (11). LAP2α is also targeted for cleavage by caspases, which may contribute to changes in chromatin structure during apoptosis (12).
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For Research Use Only. Not For Use In Diagnostic Procedures.