Our Anti-Lamin A/C primary antibody from PhosphoSolutions is mouse monoclonal. It detects human Lamin A/C and is Protein G purified. It is great for use in WB, IHC, ICC.
Immunostaining of HeLa cells showing strong nuclear lamina staining with anti-Lamin A/C (cat. 1027-LAM, red, 1:1000) and anti-Vimentin (cat. 2105-VIM, green, 1:500).
Lamins A and C are nuclear structural proteins that are part of the intermediate filament family and coded for by the same gene (LMNA). Lamins A and C are nearly identical except for their carboxy termini (McKeon et al., 1986). Mutations in the gene encoding lamins A/C have been shown to cause a variety of diseases including autosomal dominant Emery-Dreifuss muscular dystrophy (Bonne et al., 1995), autosomal dominant limbgirdle muscular dystrophy (Muchir et al., 2000) and Charcot-Marie-Tooth disorder type 2 (De Sandre-Giavonnoli et al., 2002).
Protein G Purified
Monoclonal
4C4
IgG1
ICC, IHC, WB
Mouse
LMNA
64, 74 kDa
Recombinant full length human lamin C expressed in and purified from E. Coli.
Human
AB_2492139
Recommended that the undiluted antibody be aliquoted into smaller working volumes (10-30 uL/vial depending on usage) upon arrival and stored long term at -20° C or -80° C, while keeping a working aliquot stored at 4° C for short term. Avoid freeze/thaw cycles. Stable for at least 1 year.
Liquid
Protein G purified culture supernatant
PBS + 10 mM NaN3.
WB: 1:5000
IHC: 1:1000
ICC: 1:1000
Unconjugated
Specific for endogenous levels of the ~64 kDa and ~74 kDa lamin A and C proteins.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Bonne, G., Di Barletta, M.R., Varnous, S., Bécane, H.M., Hammouda, E.H., Merlini, L., Muntoni, F., Greenberg, C.R., Gary, F., Urtizberea, J.A. and Duboc, D., 1999. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nature Genetics, 21(3), p.285-288. PMID: 10080180
De Sandre‐Giovannoli, A., Chaouch, M., Kozlov, S., Vallat, J.M., Tazir, M., Kassouri, N., Szepetowski, P., Hammadouche, T., Vandenberghe, A., Stewart, C.L. and Grid, D., 2002. Homozygous defects in LMNA, encoding lamin A/C nuclear‐envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot‐Marie‐Tooth disorder type 2) and mouse. Journal of the Peripheral Nervous System, 7(3), pp.205-205. PMID: 11799477
McKeon, F.D., Kirschner, M.W. and Caput, D., 1986. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature, 319(6053), pp.463-468. PMID: 3453101
Muchir, A., Bonne, G., van der Kooi, A.J., van Meegen, M., Baas, F., Bolhuis, P.A., de Visser, M. and Schwartz, K., 2000. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Human Molecular Genetics, 9(9), pp.1453-1459. PMID: 10814726
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