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AB58528

Anti-Lamin A + Lamin C (phospho S392) antibody

4

(1 Review)

|

(12 Publications)

Rabbit Polyclonal Lamin-A/C phospho S392 antibody. Suitable for ICC, WB, IHC-P and reacts with Human samples. Cited in 12 publications. Immunogen corresponding to Synthetic Peptide within Human LMNA phospho S392.

View Alternative Names

LMN1, LMNA, Prelamin-A/C

4 Images
Western blot - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)
  • WB

Supplier Data

Western blot - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)

Western blot analysis of HeLa cells labeling Lamin A + C (phospho S392) with ab58528. The lane on the right is blocked with the phospho peptide. Western blot analysis of HeLa cells labelling Lamin A + C (phosphor S392) with ab58528 at 1 : 1000 dilution.

All lanes:

Western blot - Anti-Lamin A + Lamin C (phospho S392) antibody (ab58528)

Predicted band size: 74 kDa

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Immunocytochemistry - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)
  • ICC

Supplier Data

Immunocytochemistry - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)

Immunocytochemistry/ Immunofluorescence analysis of HeLa cells labeling Lamin A + C (phospho S392) with ab58528. The image on the right is blocked with the phospho peptide. Immunocytochemistry/ Immunofluorescence analysis of HeLa cells labelling Lamin A + C (phosphor S392) with ab58528 at 1 : 200 dilution

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human breast carcinoma tissue labeling Lamin A + C (phospho S392) with ab58528. The image on the right is blocked with the phospho peptide. Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human breast carcinoma tissue labelling Lamin A + C (phosphor S392) with ab58528 at 1 : 100 dilution.

Western blot - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)
  • WB

Unknown

Western blot - Anti-Lamin A + Lamin C (phospho S392) antibody (AB58528)

All lanes:

Western blot - Anti-Lamin A + Lamin C (phospho S392) antibody (ab58528) at 1/500 dilution

Lane 1:

Extracts from Hela cells

Lane 2:

Extracts from Hela cells with immunizing peptide

Predicted band size: 74 kDa

Observed band size: 75 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, ICC, WB

applications

Immunogen

Synthetic Peptide within Human LMNA phospho S392. The exact immunogen used to generate this antibody is proprietary information.

P02545

Specificity

This antibody detects endogenous levels of Lamin A + C only when phosphorylated at serine 392.

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Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
The antibody was affinity-purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non phosphopeptide corresponding to the phosphorylation site.
Storage buffer
pH: 7 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Lamin A and Lamin C also known as lamin A/C are proteins encoded by the LMNA gene. These proteins are key components of the nuclear envelope where they provide structural support and maintain the shape of the nucleus. The lamin A/C molecule has a molecular weight of approximately 60-70 kDa. Expression of lamin A and lamin C occurs predominantly in differentiated cells where these proteins integrate into the nuclear lamina alongside other lamin molecules like lamin B. Lamin A alone sometimes referred to by designations like 4C11 plays a significant role in mechanical support at a molecular level.
Biological function summary

Lamin A/C proteins play a role in maintaining nuclear stability chromosome organization and gene regulation. They are part of a complex network within the nuclear lamina that includes interactions with proteins and DNA. Lamin A with a molecular weight distinct from other lamins participates in assembling this supportive matrix and contributes to DNA maintenance and repair processes. Their interaction with chromatin and gene expression regulation emphasizes their influence on important cellular functions.

Pathways

Lamin A/C proteins engage in the mechanosensory signaling and DNA damage response pathways. They interact with pathways involving the nuclear envelope structure and have connections to proteins like emerin and nuclear actin. Lamin A's role in these pathways supports its involvement in responding to mechanical stress and preserving genomic integrity highlighting its integration with these cellular processes.

Mutations in lamin A/C are linked to disorders such as Hutchinson-Gilford Progeria Syndrome and Emery-Dreifuss Muscular Dystrophy. These conditions highlight the importance of lamin A/C in cellular stability and nuclear integrity. Proteins such as emerin often relate to lamin A/C in these diseases as disruptions to their interactions can lead to compromised nuclear function and disease phenotypes.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Lamin-A/C. Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed : 10080180, PubMed : 10580070, PubMed : 10587585, PubMed : 10814726, PubMed : 11799477, PubMed : 12075506, PubMed : 12927431, PubMed : 15317753, PubMed : 18551513, PubMed : 18611980, PubMed : 2188730, PubMed : 22431096, PubMed : 2344612, PubMed : 23666920, PubMed : 24741066, PubMed : 31434876, PubMed : 31548606, PubMed : 37788673, PubMed : 37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed : 10080180, PubMed : 10580070, PubMed : 10587585, PubMed : 10814726, PubMed : 11799477, PubMed : 12075506, PubMed : 12927431, PubMed : 15317753, PubMed : 18551513, PubMed : 18611980, PubMed : 22431096, PubMed : 23666920, PubMed : 24741066, PubMed : 31548606, PubMed : 37788673, PubMed : 37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed : 23990565, PubMed : 25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed : 2188730, PubMed : 2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed : 10080180, PubMed : 10580070, PubMed : 10587585, PubMed : 10814726, PubMed : 11799477, PubMed : 12075506, PubMed : 12927431, PubMed : 15317753, PubMed : 18551513, PubMed : 18611980, PubMed : 22431096, PubMed : 23666920, PubMed : 31548606). Also invoved in DNA repair : recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed : 31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed : 10080180, PubMed : 10814726, PubMed : 11799477, PubMed : 18551513, PubMed : 22431096). Required for osteoblastogenesis and bone formation (PubMed : 12075506, PubMed : 15317753, PubMed : 18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed : 10587585). Required for cardiac homeostasis (PubMed : 10580070, PubMed : 12927431, PubMed : 18611980, PubMed : 23666920).. Prelamin-A/C. Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed : 20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed : 20458013).
See full target information LMNA phospho S392
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Publications (12)

Recent publications for all applications. Explore the full list and refine your search

iScience 26:106992 PubMed37378334

2023

AKT2-mediated nuclear deformation leads to genome instability during epithelial-mesenchymal transition.

Applications

Unspecified application

Species

Unspecified reactive species

Jia-Rong Fan,Sung-Nian Chang,Ching-Tung Chu,Hong-Chen Chen

Journal of cell science 136: PubMed36695453

2023

Lamin A/C phosphorylation at serine 22 is a conserved heat shock response to regulate nuclear adaptation during stress.

Applications

Unspecified application

Species

Unspecified reactive species

Laura Virtanen,Emilia Holm,Mona Halme,Gun West,Fanny Lindholm,Josef Gullmets,Juho Irjala,Tiina Heliö,Artur Padzik,Annika Meinander,John E Eriksson,Pekka Taimen

Cells 11: PubMed36552752

2022

Loss of Mature Lamin A/C Triggers a Shift in Intracellular Metabolic Homeostasis via AMPKα Activation.

Applications

Unspecified application

Species

Unspecified reactive species

Ying Zhou,Jia-Jie Yang,Yuan Cheng,Ge-Xuan Feng,Rong-Hui Yang,Yuan Yuan,Li-Yong Wang,Miao Wang,Lu Kong

eLife 10: PubMed33605210

2021

LAP2alpha maintains a mobile and low assembly state of A-type lamins in the nuclear interior.

Applications

Unspecified application

Species

Unspecified reactive species

Nana Naetar,Konstantina Georgiou,Christian Knapp,Irena Bronshtein,Elisabeth Zier,Petra Fichtinger,Thomas Dechat,Yuval Garini,Roland Foisner

Aging cell 19:e13257 PubMed33146912

2020

Autophagic receptor p62 protects against glycation-derived toxicity and enhances viability.

Applications

Unspecified application

Species

Unspecified reactive species

Gemma Aragonès,Kalavathi Dasuri,Opeoluwa Olukorede,Sarah G Francisco,Carol Renneburg,Caroline Kumsta,Malene Hansen,Shun Kageyama,Masaaki Komatsu,Sheldon Rowan,Jonathan Volkin,Michael Workman,Wenxin Yang,Paula Daza,Diego Ruano,Helena Dominguez-Martín,José Antonio Rodríguez-Navarro,Xue-Liang Du,Michael A Brownlee,Eloy Bejarano,Allen Taylor

Scientific reports 10:15659 PubMed32973212

2020

Novel targets identified by integrated proteomic and phosphoproteomic analysis in spermatogenesis of swamp buffalo (Bubalus bubalis).

Applications

Unspecified application

Species

Unspecified reactive species

Yu-Lin Huang,Peng-Fei Zhang,Qiang Fu,Weng-Tan He,Kai Xiao,Ming Zhang

PLoS genetics 14:e1007278 PubMed29565969

2018

The RNA-binding protein Celf1 post-transcriptionally regulates p27Kip1 and Dnase2b to control fiber cell nuclear degradation in lens development.

Applications

Unspecified application

Species

Unspecified reactive species

Archana D Siddam,Carole Gautier-Courteille,Linette Perez-Campos,Deepti Anand,Atul Kakrana,Christine A Dang,Vincent Legagneux,Agnès Méreau,Justine Viet,Jeffrey M Gross,Luc Paillard,Salil A Lachke

Science (New York, N.Y.) 358:803-806 PubMed28982797

2017

Calibrated mitotic oscillator drives motile ciliogenesis.

Applications

Unspecified application

Species

Mouse

Adel Al Jord,Asm Shihavuddin,Raphaël Servignat d'Aout,Marion Faucourt,Auguste Genovesio,Anthi Karaiskou,Joëlle Sobczak-Thépot,Nathalie Spassky,Alice Meunier

PLoS pathogens 12:e1005825 PubMed27556400

2016

The Prolyl Isomerase Pin1 Promotes the Herpesvirus-Induced Phosphorylation-Dependent Disassembly of the Nuclear Lamina Required for Nucleocytoplasmic Egress.

Applications

Unspecified application

Species

Unspecified reactive species

Jens Milbradt,Corina Hutterer,Hanife Bahsi,Sabrina Wagner,Eric Sonntag,Anselm H C Horn,Benedikt B Kaufer,Yasuko Mori,Heinrich Sticht,Torgils Fossen,Manfred Marschall

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 30:1087-95 PubMed26590164

2015

Unfolded-protein response-associated stabilization of p27(Cdkn1b) interferes with lens fiber cell denucleation, leading to cataract.

Applications

Unspecified application

Species

Unspecified reactive species

Lei Lyu,Elizabeth A Whitcomb,Shuhong Jiang,Min-Lee Chang,Yumei Gu,Melinda K Duncan,Ales Cvekl,Wei-Lin Wang,Saima Limi,Lixing W Reneker,Fu Shang,Linfang Du,Allen Taylor
View all publications
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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions
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