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由来生物
rabbit
抗体製品の状態
affinity isolated antibody
抗体製品タイプ
primary antibodies
クローン
polyclonal
化学種の反応性
human
テクニック
immunofluorescence: suitable
inhibition assay: suitable (peptide)
western blot: suitable
アイソタイプ
IgG
NCBIアクセッション番号
UniProtアクセッション番号
ターゲットの翻訳後修飾
phosphorylation (pSer404)
遺伝子情報
human ... LMNA(4000)
詳細
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).
特異性
This rabbit polyclonal antibody detects human Lamin A/C phosphorylated on Serine 404.
免疫原
Epitope: unknown
KLH-conjugated linear peptide corresponding to 12 amino acids from human Lamin A/C surrounding phosphorylated Serine 404.
アプリケーション
Research Category
細胞骨格
細胞骨格
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.
品質
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).
ターゲットの説明
~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).
物理的形状
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.
保管および安定性
Stable for 1 year at 2-8°C from date of receipt.
その他情報
Concentration: Please refer to lot specific datasheet.
免責事項
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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保管分類コード
12 - Non Combustible Liquids
WGK
WGK 1
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
ABT1387-50UL:
ABT1387-200UL:
試験成績書(COA)
製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
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
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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