ABT1387
Anti-Phospho-Lamin A/C (Ser404)
from rabbit
Synonym(s):
Prelamin A/C, Renal carcinoma antigen NY-REN-32
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All Photos(3)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human
technique(s)
immunofluorescence: suitable
inhibition assay: suitable (peptide)
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
target post-translational modification
phosphorylation (pSer404)
Gene Information
human ... LMNA(4000)
General description
Prelamin-A/C (UniProt: P02545) is encoded by the LMNA (also known as LMN1) gene (Gene ID: 4000) in human. Prelamin-A/C is subsequently cleaved into Lamin A/C. Lamins are components of the nuclear lamina that provides a framework for the nuclear envelope and interact with chromatin. Prelamin-A/C
Is cleaved to generate Lamin A/C. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature Lamin-A/C that is inserted into the nuclear lamina. Lamin A and C are present in equal amounts in the lamina of mammals and they play an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Lamins are shown to be essential for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Lamins also prevent fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Phosphorylation of Lamins is reported to occur continuously throughout all interphase periods and takes place mainly on the assembled lamina. Phosphorylation of the major polypeptides of the lamina induces laminar disassembly during mitosis. Phosphorylated Lamin-A/C localizes to nucleoplasm. Lamin A/C undergoes phosphorylation at multiple sites and one of the best characterized phosphorylation sites is on Serine 22 and it is phosphorylated during interphase. Phosphorylation of Serine 22 stabilizes Lamin A/C. Overexpression of Lamin-A is shown to result in greater phosphorylation of Serine 22 and 390 and Lamin A/C knockdowns display reduced phosphorylation at both sites, which helps in maintaining the integrity of the diminished lamina. Lamin A/C can undergoes phosphorylation on Serine 404 by Akt1 and Ser4040 phosphorylated Lamin undergoes rapid lysosomal degradation. Mutations in LMNA gene can cause Emery-Dreifuss muscular dystrophy 2 and 3, which are characterized by weakness and atrophy of muscle without involvement of the nervous system and cardiac conduction defects. Some mutations have also been linked to familial Lipodystrophy that leads to the loss of subcutaneous adipose tissue in the lower parts of the body and accumulation of adipose tissue in the face and neck. (Ref.: Buxboim, A., et al. (2014). Curr. Biol. 24(16): 1909-1917; Toker, A., and Marmiroli, S. (2014). Adv. Biol. Regul. 55: 28-38).
Is cleaved to generate Lamin A/C. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature Lamin-A/C that is inserted into the nuclear lamina. Lamin A and C are present in equal amounts in the lamina of mammals and they play an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Lamins are shown to be essential for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Lamins also prevent fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Phosphorylation of Lamins is reported to occur continuously throughout all interphase periods and takes place mainly on the assembled lamina. Phosphorylation of the major polypeptides of the lamina induces laminar disassembly during mitosis. Phosphorylated Lamin-A/C localizes to nucleoplasm. Lamin A/C undergoes phosphorylation at multiple sites and one of the best characterized phosphorylation sites is on Serine 22 and it is phosphorylated during interphase. Phosphorylation of Serine 22 stabilizes Lamin A/C. Overexpression of Lamin-A is shown to result in greater phosphorylation of Serine 22 and 390 and Lamin A/C knockdowns display reduced phosphorylation at both sites, which helps in maintaining the integrity of the diminished lamina. Lamin A/C can undergoes phosphorylation on Serine 404 by Akt1 and Ser4040 phosphorylated Lamin undergoes rapid lysosomal degradation. Mutations in LMNA gene can cause Emery-Dreifuss muscular dystrophy 2 and 3, which are characterized by weakness and atrophy of muscle without involvement of the nervous system and cardiac conduction defects. Some mutations have also been linked to familial Lipodystrophy that leads to the loss of subcutaneous adipose tissue in the lower parts of the body and accumulation of adipose tissue in the face and neck. (Ref.: Buxboim, A., et al. (2014). Curr. Biol. 24(16): 1909-1917; Toker, A., and Marmiroli, S. (2014). Adv. Biol. Regul. 55: 28-38).
Specificity
This rabbit polyclonal antibody detects human Lamin A/C phosphorylated on Serine 404.
Immunogen
Epitope: unknown
KLH-conjugated linear peptide corresponding to 12 amino acids from human Lamin A/C surrounding phosphorylated Serine 404.
Application
Anti-Phospho-Lamin A/C (Ser404), Cat. No. ABT1387, is a rabbit polyclonal antibody that detects Lamin A/C phosphorylated on Serine 404 and has been tested for use in Immunofluorescence, Western Blotting, and Peptide Inhibition Assay.
Immunofluorescence Analysis: 0.2 µg/mL from a representative lot detected Phospho-Lamin A/C (Ser404) in A549 lung carcinoma cells. (Courtesy of Sangkyun Cho & Dr. D.E Discher at University of Pennsylvania).
Peptide Inhibition Analysis: A 1:500 dilution from a representative lot was used with A549 cells (specific for Lamin A/C phosphorylation) for peptide block analysis.
Peptide Inhibition Analysis: A 1:500 dilution from a representative lot was used with A549 cells (specific for Lamin A/C phosphorylation) for peptide block analysis.
Research Category
Cell Structure
Cell Structure
Quality
Evaluated by Western Blotting in A549 cells.
Western Blotting Analysis: A 1:500 dilution of this antibody detected Phospho-Lamin A/C (Ser404) in A549 cells (specific for Lamin A/C phosphorylation).
Western Blotting Analysis: A 1:500 dilution of this antibody detected Phospho-Lamin A/C (Ser404) in A549 cells (specific for Lamin A/C phosphorylation).
Target description
~75 kDa and 65 kDa observed; 74.14 and 65.14 kDa calculated for Lamin A and C, respectively. Uncharacterized bands may be observed in some lysate(s).
Physical form
Affinity Purified
Format: Purified
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Other Notes
Concentration: Please refer to lot specific datasheet.
Disclaimer
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.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Sangkyun Cho et al.
Nucleus (Austin, Tex.), 9(1), 230-245 (2018-04-06)
Interphase phosphorylation of lamin-A,C depends dynamically on a cell's microenvironment, including the stiffness of extracellular matrix. However, phosphorylation dynamics is poorly understood for diseased forms such as progerin, a permanently farnesylated mutant of LMNA that accelerates aging of stiff and
Jia-Rong Fan et al.
iScience, 26(6), 106992-106992 (2023-06-28)
Nuclear deformation has been observed in some cancer cells for decades, but its underlying mechanism and biological significance remain elusive. To address these questions, we employed human lung cancer A549 cell line as a model in context with transforming growth
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