antibody

Mouse anti Lamin A

MBS570040

1 ml

265 USD

monoclonal

mouse

nonconjugated

133A2

western blot, immunohistochemistry, immunocytochemistry, flow cytometry, immunohistochemistry - paraffin section, immunohistochemistry - frozen section

Antibody

Mouse anti Lamin A

Lamin A

lamin-A; Lamin-A; lamin-A; lamin A/C<

lmna; lmna; lmna-A

LMNA_XENLA

Monoclonal

IgG3

133A2

Mouse

Bovine, Canine, Human, Mouse, Rat

133A2 recognizes an epitope loCated between residues 598-611 of lamin A and therefore 133A2 reacts exclusively with lamin A.

Each vial contains 1ml of culture supernatant of monoclonal antibody containing 0.09% sodium azide.

Store at 4 degree C, or in small aliquots at -20 degree C.

Flow Cytometry (FC), Immunocytochemistry (IHC), Immunohistochemistry (IHC) (frozen), Immunohistochemistry (IHC) (paraffin), Western Blot (WB)

133A2 is suitable for immunocytochemistry, immunohistochemistry on frozen and paraffin-embedded tissues, immunoblotting and flow cytometry. Optimal antibody dilution should be determined by titRation; recommended range is 1:5 - 1:20 for flow cytometry, and for immunohistochemistry with avidin-biotinylated Horseradish peroxidase complex (ABC) as detection reagent, and 1:5 - 1:100 for immunoblotting appliCations.

Source Note: 133A2 is a Mouse monoclonal IgG3/kappa antibody obtained from fusion of P3/X63.Ag8.653 Mouse myeloma cells with spleen cells from a BALB/c Mouse immunized with partially purified recombinant Human lamin A.

Nuclear proteins, Cytoskeleton

Nuclear lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane. Two main subtypes of nuclear lamins can be distinguished, i.e. A-type lamins and B-type lamins. The A-type lamins comprise a set of three proteins arising from the same gene by alternative splicing, i.e. lamin A, lamin C and lamin Adel 10, while the B-type lamins include two proteins arising from two distinct genes, i.e. lamin B1 and lamin B2. Recent evidence has revealed that mutations in A-type lamins give rise to a range of rare but dominant genetic disorders, including Emery-Dreifuss muscular dystrophy, dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy. In addition, the expression of A-type lamins coincides with cell differentiation and as A-type lamins specifically interact with chromatin, a role in the regulation of differential gene expression has been suggested for A-type lamins.

Hozak, P., Sasseville, A. M., Raymond, Y., and Cook, P. R. (1995). Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in Human cells, J Cell Sci 108, 635-44. Machiels, B. M., Broers, J. L., Raymond, Y., de Ley, L., Kuijpers, H. J., Caberg, N. E., and Ramaekers, F. C. (1995). Abnormal A-type lamin organization in a Human lung carcinoma cell line, Eur J Cell Biol 67, 328-35. Broers, J. L., Machiels, B. M., Kuijpers, H. J., Smedts, F., van den Kieboom, R., Raymond, Y., and Ramaekers, F. C. (1997). A- and B-type lamins are differentially expressed in normal Human tissues, Histochem Cell Biol 107, 505-17. Pugh, G. E., Coates, P. J., Lane, E. B., Raymond, Y., and Quinlan, R. A. (1997). Distinct nuclear assembly pathways for lamins A and C lead to their increase during quiescence in Swiss 3T3 cells, J Cell Sci 110, 2483-93. Machiels, B. M., Ramaekers, F. C., Kuijpers, H. J., Groenewoud, J. S., Oosterhuis, J. W., and Looijenga, L. H. (1997). Nuclear lamin expression in normal testis and testicular germ cell tumours of adolescents and adults, J Pathol 182, 197-204. Jansen, M. P., Machiels, B. M., Hopman, A. H., Broers, J. L., Bot, F. J., Arends, J. W., Ramaekers, F. C., and Schouten, H. C. (1997). Comparison of A and B-type lamin expression in reactive lymph nodes and nodular sclerosing Hodgkin's disease, Histopathology 31, 304-12. Neri, L. M., Raymond, Y., Giordano, A., Borgatti, P., Marchisio, M., Capitani, S., and Martelli, A. M. (1999). Spatial distribution of lamin A and B1 in the K562 cell nuclear matrix stabilized with metal ions, J Cell Biochem 75, 36-45. Neri, L. M., Raymond, Y., Giordano, A., Capitani, S., and Martelli, A. M. (1999). Lamin A is part of the internal nucleoskeleton of Human erythroleukemia cells, J Cell Physiol 178, 284-95. Broers, J. L., Machiels, B. M., van Eys, G. J., Kuijpers, H. J., Manders, E. M., van Driel, R., and Ramaekers, F. C. (1999). Dynamics of the nuclear lamina as monitored by GFP-tagged A-type lamins, J Cell Sci 112, 3463-75. Broers, J. L., Bronnenberg, N. M., Kuijpers, H. J., Schutte, B., Hutchison, C. J., and Ramaekers, F. C. (2002). Partial cleavage of A-type lamins concurs with their total disintegRation from the nuclear lamina during apoptosis. Eur J Cell Biol 81, 677-691. De Sandre-Giovannoli, A., Bernard, R., Cau, P., Navarro, C., Amiel, J., Boccaccio, I., Lyonnet, S., Stewart, C. L., Munnich, A., Le Merrer, M., and Levy, N. (2003). Lamin a trunCation in Hutchinson-Gilford progeria. Science 300, 2055. Eriksson, M., Brown, W. T., Gordon, L. B., Glynn, M. W., Singer, J., Scott, L., Erdos, M. R., Robbins, C. M., Moses, T. Y., Berglund, P., et al. (2003). Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 423, 293-298.

156119433

NP_001095210.1

NM_001101740.1

P11048

74,919 Da

Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Subcellular location: Nucleus. Miscellaneous: There are at least five different lamins in Xenopus: the somatic lamins L(I), L(II), and A; the oocyte germinal vesicle lamin L(III); and the male germ cells lamin l(IV). Sequence similarities: Belongs to the intermediate filament family.

1 ml

265 USD