Catalogue

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 Adel10, while the B-type lamins include two proteins arising from two distinct genes, i.e. lamin B1 and lamin B2. Lamins play a crucial role in the maintenence of nuclear structure, gene regulation and signalling from cytoplasm to nucleus. Mutations in lamins have been associated with a number of pathologies; the so-called laminopathies.

Source
119D5-F1 is a Mouse monoclonal IgG1/k antibody derived by fusion of P3/X63.Ag8.653 Mouse myeloma cells with spleen cells from a BALB/c Mouse immunized with purified Rat liver lamins.

Product
Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.

Formulation: Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.

Specificity
119D5-F1 reacts with an epitope located C-terminal of residue 231 in lamin B1.

Applications
119D5-F1 is suitable for immunocytochemistry on permeabilised cells, immunohistochemistry on frozen tissues, immunoblotting, ELISA and flow cytometry. Optimal antibody dilution should be determined by titration; recommended range is 1:100 – 1:200 for flow cytometry, immunocytochemistry and for immunohistochemistry with avidin-biotinylated Horseradish peroxidase complex (ABC) as detection reagent, and 1:100 – 1:1000 for immunoblotting applications.

Storage
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.

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. It may contain hazardous ingredients. Please refer to the Safety Data Sheets (SDS) for additional information and proper handling procedures. Dispose product remainders according to local regulations.This datasheet is as accurate as reasonably achievable, but our company accepts no liability for any inaccuracies or omissions in this information.

References
1. Broers, J.L., Ramaekers, F.C.S., Bonne, G., Hutchison, C.J. (2006). Nuclear Lamins: laminopathies and their role in premature aging. Physiol Rev 86, 967-1008. 2. Weaver, V. M., Carson, C. E., Walker, P. R., Chaly, N., Lach, B., Raymond, Y., Brown, D. L., and Sikorska, M. (1996). Degradation of nuclear matrix and DNA cleavage in apoptotic thymocytes, J Cell Sci 109, 45-56. 3. 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. 4. 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. 5. 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. 6. 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. 7. 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. 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., 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.

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