Mouse anti Lamin A, conjugated to FITC

Mouse anti Lamin A, conjugated to FITC

• 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.
• CAS Number: 9007-83-4
• UniProt: P02545
• Host: Mouse
• Species Reactivity: Bovine, Dog, Human, Mouse, Rat
• Isotype: IgG3
• Clone: 133A2
• Conjugation: FITC
• Type: Primary Antibodies
• 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.
• Applications: Flow Cytometry, ICC, IHC (frozen)
• Field of Research: Cytoskeleton, Neuroscience, Cell Biology
• Assay Principle: 133A2 is suitable for immunocytochemistry on permeabilized cells, immunohistochemistry on frozen sections and flow cytometry. Optimal antibody dilutions for the different applications should be determined by titration. The recommended dilution is 1:10.
• Form: Each vial contains 1 mL FITC-conjugated anti lamin A monoclonal antibody in PBS containing 0,1% BSA, 0,09% sodium azide Approximately 100 tests.
• Precautions: 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 datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
• References & Citations: Recent application paper:_x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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._x000D_ _x000D_ 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._x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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. _x000D_ _x000D_ 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.
• Storage Conditions: The antibody is shipped at ambient temperature and may be stored at +4°C; For prolonged storage prepare appropriate aliquots and store at or below -20°C; Prior to use, an aliquot is thawed slowly in the dark at ambient temperature, spun down again and used to prepare working dilutions by adding sterile phosphate buffered saline (PBS, pH 7.2); Repeated thawing and freezing should be avoided; Working dilutions should be stored at +4°C, not refrozen, and preferably used the same day; If a slight precipitation occurs upon storage, this should be removed by centrifugation; It will not affect the performance or the concentration of the product