Product Pathways - Apoptosis
LAP2α (3A3) Mouse mAb #5369
|5369S||100 µl (10 western blots)||---||In Stock||---|
|5369||carrier free and custom formulation / quantity||email request|
Already purchased this product? Write a Review.
|W||1:1000||Human, Monkey||Endogenous||76||Mouse IgG1|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry)
* 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).
- Gruenbaum, Y. et al. (2000) J Struct Biol 129, 313-23.
- Goldberg, M. et al. (1999) Crit Rev Eukaryot Gene Expr 9, 285-93.
- Holmer, L. and Worman, H.J. (2001) Cell Mol Life Sci 58, 1741-7.
- Lazebnik, Y.A. et al. (1995) Proc Natl Acad Sci USA 92, 9042-6.
- Oberhammer, F.A. et al. (1994) J Cell Biol 126, 827-37.
- Rao, L. et al. (1996) J Cell Biol 135, 1441-55.
- Furukawa, K. et al. (1995) EMBO J 14, 1626-36.
- Foisner, R. and Gerace, L. (1993) Cell 73, 1267-79.
- Harris, C.A. et al. (1994) Proc Natl Acad Sci USA 91, 6283-7.
- Dechat, T. et al. (2000) J Cell Sci 113 Pt 19, 3473-84.
- Markiewicz, E. et al. (2002) Mol Biol Cell 13, 4401-13.
- Gotzmann, J. et al. (2000) J Cell Sci 113 Pt 21, 3769-80.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.