Technical Data

L1220-06-ML490
Clone Type
Monoclonal
Host
Mouse
Source
Human
Conjugate
MaxLight™490
Isotype
IgG3
Clone Number
133A2
Grade
Purified
Applications
IC IHC WB
Crossreactivity
Bo Ca Hu Mo Rt
Shipping Temp
Blue Ice
Storage Temp
4°C Do Not Freeze
Notes
Preservative Free
BSA Free
Mouse Anti-Lamin A (MaxLight 490)

MaxLight™490 is a new Blue-Green photostable dye conjugate comparable to DyLight™488, Alexa Fluor™488 and offers better labeling efficiency, brighter imaging and increased immunodetection. Absorbance (491nm); Emission (515nm); Extinction Coefficient 73,000.

Nuclear lamins form a network of filaments at the nucleoplasmic site of the nuclear membrane. Two main subtypes of nuclear lamins can be distinguished: 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. Type A lamins comprise a set of three proteins arising from the same gene by alternative splicing: lamins A, C, and Adel 10. B-type lamins include two proteins arising from two distinct genes, i.e. lamin B1 and lamin B2. Mutations in A-lamins give rise to a range of genetic disorders, including autosomal dominant Emery-Dreifuss muscular dystrophy (AD-EDMD), dilated cardiomyopathy and Dunnigan-type familial partial lipodystrophy. Aberrant expression patterns of nuclear lamins have been described in various types of cancer depending on the subtype of cancer, its aggressiveness, proliferative capacity and degree of differentiation. In general, the expression of A-type lamins (lamins A and C) has been correlated with a non-proliferating, differentiated state of cells and tissues. Lamins A and C, the products of the LMNA gene, are nuclear intermediate filament proteins and are the major structural components of the lamina network that underlies and supports the nuclear envelope. Expression of A-lamin coincides with cell differentiation and may be related protein’s abnormal expression and organization in neoplastic tissues and cells.
Applications
Suitable for use in Western Blot, Immunohistochemistry and Immunocytochemistry. Other applications not tested.
Recommended Dilutions
Immunohistochemistry: Frozen sections Immunocytochemistry: Fixed cells using methanol/acetone fixation Optimal dilutions to be determined by the researcher.
Storage and Stability
Store product at 4°C in the dark. DO NOT FREEZE! Stable at 4°C for 12 months after receipt as an undiluted liquid. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Caution: MaxLight™490 conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial prior to removing the cap.
Note: Applications are based on unconjugated antibody.
Immunogen
Synthetic peptide corresponding to the C-terminus, aa598-611, of human lamin A. This sequence is not present in the the lamin C isoform.
Form
Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with MaxLight™490.
Purity
Purified culture supernatant.
Specificity
Recognizes human lamin A but not lamin C. The epitope lies with the 98aa of the C terminus that is unique to lamin A. Specifically deletion analysis has shown that aa598-611 were essential for reactivity. Species Crossreactivity: bovine, canine, mouse and rat

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. 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. 2. 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. 3. 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. 4. 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. 5. 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. 6. 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. 7. 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. 8. 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. 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.
USBio References
No references available
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