Lamin A is a structural protein of the nuclear lamina. The nuclear lamina is a meshwork of intermediate filaments that underlies the inner face of the nuclear envelope. The precursor of lamin A, prelamin comprises 98 unique amino acids and also harbors the farnesyl group in C-terminus post-synthesis. The cleavage of the farnesyl group containing end 18 amino acids results in mature Lamin A. Lamin A is mapped to human chromosome 1q21.2.
Specificity
Anti-Lamin A-Atto 647N recognizes human Lamin A.
Application
Anti-Lamin A−Atto 647N antibody produced in rabbit may be used in direct immunofluorescence.
Biochem/physiol Actions
Lamin A is cleaved into a 47 kDa fragment during apoptosis. Lamin A cleavage seems to be essential for chromatin condensation and nuclear disassembly in apoptosis. Mutations in Lamin A and C have been linked to a variety of rare human diseases including muscular dystrophy, lipodystrophy, cardiomyopathy, neuropathy and progeroid syndromes (collectively termed laminopathies) and to premature aging (Hutchinson-Gilford progeria syndrome).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2–8 °C for up to one month. For extended storage, freeze in working aliquots. Protect from prolonged exposure to light. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 29(6), 2514-2525 (2015-03-04)
DNA double-strand breaks (DSBs) are the major lethal lesion induced by ionizing radiation (IR). RAD51-dependent homologous recombination (HR) is one of the most important pathways in DSB repair and genome integrity maintenance. However, the mechanism of HR regulation by RAD51
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