Clone: 133A2
Background: 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.
Source: 133A2 is a mouse monoclonal IgG3/κ 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.
Specificity: 133A2 recognizes an epitope located between residues 598-611 of lamin A and therefore 133A2 reacts exclusively with lamin A.
Formulation: Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide. Since this IgG3 antibody has to be purified from the culture medium by ion-exchange chromatography it will contain remnants of bovine serum albumin.
References: Recent application paper:van Tienen FHJ, Lindsey PJ, Kamps MAF, Krapels IP, Ramaekers FCS, Brunner HG, van den Wijngaard A, Broers JLV. Assessment of fibroblast nuclear morphology aids interpretation of LMNA variants. Eur J Hum Genet. 2019 Mar;27(3):389-399. doi: 10.1038/s41431-018-0294-0. 1. 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. 2. 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. 3. 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. 4. 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. 5. 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. 6. 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. 7. 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. 8. 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. 9. 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. 10. 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. 11. 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. 12. 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.
UniProt: P02545
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
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