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AB196636

HRP Anti-Lamin A + Lamin C antibody [JOL2]

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(11 Publications)

Mouse Monoclonal Lamin-A/C antibody - conjugated to HRP. Suitable for WB, IHC-P and reacts with Human, African green monkey samples. Cited in 11 publications. Immunogen corresponding to Recombinant Fragment Protein within Human LMNA.

View Alternative Names

LMN1, LMNA, Prelamin-A/C

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - HRP Anti-Lamin A + Lamin C antibody [JOL2] (AB196636)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - HRP Anti-Lamin A + Lamin C antibody [JOL2] (AB196636)

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of human colon tissue sections labelling Lamin A + C with ab196636.

Western blot - HRP Anti-Lamin A + Lamin C antibody [JOL2] (AB196636)
  • WB

Lab

Western blot - HRP Anti-Lamin A + Lamin C antibody [JOL2] (AB196636)

ab196636 was shown to react with Anti-Lamin A + C antibody [JOL2] (HRP) in wild-type HAP1 cells in Western blot. Loss of signal was observed when LMNA knockout sample was used. Membranes were blocked in 3% milk in TBS-T (0.1% Tween®) before incubation with ab196636 overnight at 4°C at a 1 in 200 dilution and ab184095 (Mouse Anti-GAPDH antibody [mAbcam 9484] - Alexa Fluor® 680) at a 1 in 1000 dilution. Blots were developed with Optiblot ECL reagent (ab133456) and imaged.

All lanes:

Western blot - HRP Anti-Lamin A + Lamin C antibody [JOL2] (ab196636) at 1/200 dilution

Lane 1:

Wild-type HAP1 cell lysate at 40 µg

Lane 2:

LMNA knockout HAP1 cell lysate at 40 µg

Lane 3:

HeLa cell lysate at 20 µg

Lane 4:

HepG2 cell lysate at 20 µg

Predicted band size: 74 kDa

Observed band size: 70-75 kDa

false

Exposure time: 150s

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

JOL2

Isotype

IgG1

Conjugation

HRP

Excitation/Emission
Carrier free

No

Reacts with

Human, African green monkey

Applications

WB, IHC-P

applications

Immunogen

Recombinant Fragment Protein within Human LMNA. The exact immunogen used to generate this antibody is proprietary information.

P02545

Epitope

This product has been shown to bind to an epitope between amino acids 464-572.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Storage buffer
pH: 7.4 Preservative: 0.01% Thimerosal (merthiolate) Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot

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.

Product protocols

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

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

Publications (11)

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

The Journal of biological chemistry 289:18752-69 PubMed24838313

2014

Caspase-activated DNase is necessary and sufficient for oligonucleosomal DNA breakdown, but not for chromatin disassembly during caspase-dependent apoptosis of LN-18 glioblastoma cells.

Applications

Unspecified application

Species

Human

María Sánchez-Osuna,Mercè Garcia-Belinchón,Victoria Iglesias-Guimarais,Estel Gil-Guiñón,Elisenda Casanelles,Victor J Yuste

Human molecular genetics 23:4125-33 PubMed24659496

2014

Nuclear protein spreading: implication for pathophysiology of neuromuscular diseases.

Applications

Unspecified application

Species

Unspecified reactive species

Maxime Ferreboeuf,Virginie Mariot,Denis Furling,Gillian Butler-Browne,Vincent Mouly,Julie Dumonceaux

Human molecular genetics 23:3180-8 PubMed24452336

2014

Human skeletal muscle xenograft as a new preclinical model for muscle disorders.

Applications

Unspecified application

Species

Human

Yuanfan Zhang,Oliver D King,Fedik Rahimov,Takako I Jones,Christopher W Ward,Jaclyn P Kerr,Naili Liu,Charles P Emerson,Louis M Kunkel,Terence A Partridge,Kathryn R Wagner

The Journal of biological chemistry 287:7766-79 PubMed22253444

2012

Apoptotic DNA degradation into oligonucleosomal fragments, but not apoptotic nuclear morphology, relies on a cytosolic pool of DFF40/CAD endonuclease.

Applications

WB

Species

Human

Victoria Iglesias-Guimarais,Estel Gil-Guiñon,Gisela Gabernet,Mercè García-Belinchón,María Sánchez-Osuna,Elisenda Casanelles,Joan X Comella,Victor J Yuste

Skeletal muscle 1:34 PubMed22040608

2011

Immortalized pathological human myoblasts: towards a universal tool for the study of neuromuscular disorders.

Applications

ICC/IF

Species

Human

Kamel Mamchaoui,Capucine Trollet,Anne Bigot,Elisa Negroni,Soraya Chaouch,Annie Wolff,Prashanth K Kandalla,Solenne Marie,James Di Santo,Jean Lacau St Guily,Francesco Muntoni,Jihee Kim,Susanne Philippi,Simone Spuler,Nicolas Levy,Sergiu C Blumen,Thomas Voit,Woodring E Wright,Ahmed Aamiri,Gillian Butler-Browne,Vincent Mouly

The journals of gerontology. Series A, Biological 66:1201-7 PubMed21852285

2011

Age-dependent loss of MMP-3 in Hutchinson-Gilford progeria syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Ingrid A Harten,Rima S Zahr,Joan M Lemire,Jason T Machan,Marsha A Moses,Robert J Doiron,Adam S Curatolo,Frank G Rothman,Thomas N Wight,Bryan P Toole,Leslie B Gordon

Journal of cell science 124:2077-85 PubMed21610090

2011

Samp1 is functionally associated with the LINC complex and A-type lamina networks.

Applications

Unspecified application

Species

Unspecified reactive species

Santhosh Gudise,Ricardo A Figueroa,Robert Lindberg,Veronica Larsson,Einar Hallberg

The Journal of cell biology 193:97-108 PubMed21444690

2011

Replication stress induces 53BP1-containing OPT domains in G1 cells.

Applications

ICC/IF

Species

Human

Jeanine A Harrigan,Rimma Belotserkovskaya,Julia Coates,Daniela S Dimitrova,Sophie E Polo,Charles R Bradshaw,Peter Fraser,Stephen P Jackson

Breast cancer research : BCR 13:R28 PubMed21392397

2011

Impact of oncogenic K-RAS on YB-1 phosphorylation induced by ionizing radiation.

Applications

WB

Species

Human

Mahmoud Toulany,Tim-Andre Schickfluss,Wolfgang Eicheler,Rainer Kehlbach,Birgit Schittek,H Peter Rodemann

Molecular therapy : the journal of the American So 17:1771-8 PubMed19623164

2009

In vivo myogenic potential of human CD133+ muscle-derived stem cells: a quantitative study.

Applications

ICC/IF

Species

Human

Elisa Negroni,Ingo Riederer,Soraya Chaouch,Marzia Belicchi,Paola Razini,James Di Santo,Yvan Torrente,Gillian S Butler-Browne,Vincent Mouly
View all publications

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