JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB125679

Anti-Lamin C antibody - Nuclear Envelope Marker

5

(4 Reviews)

|

(8 Publications)

Rabbit Polyclonal Lamin-A/C antibody. Suitable for IHC-P and reacts with Human samples. Cited in 8 publications. Immunogen corresponding to Synthetic Peptide within Human LMNA aa 550 to C-terminus conjugated to Keyhole Limpet Haemocyanin.

View Alternative Names

LMN1, LMNA, Prelamin-A/C

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Lamin C antibody - Nuclear Envelope Marker (AB125679)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Lamin C antibody - Nuclear Envelope Marker (AB125679)

ab125679, staining Lamin C in paraffin embedded Human skin tissue by Immunohistochemistry.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Lamin C antibody - Nuclear Envelope Marker (AB125679)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Lamin C antibody - Nuclear Envelope Marker (AB125679)

Immunohistochemistry analysis of human skin and epithelium, staining Lamin C in the sweat glands with ab125679. Negative control with no primary antibody.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Synthetic Peptide within Human LMNA aa 550 to C-terminus conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.

P02545

Specificity

ab125679 reacts strongly in immunoblotting with fragments corresponding to peptide 319-572aa of Lamin C.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/100", "IHCP-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Preservative: 0.1% Sodium azide Constituents: PBS
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

Supplementary information

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

Lamin C also known as LMNA forms part of the nuclear lamina which provides structural support to the cell nucleus. It has a molecular weight of approximately 65 kDa. Lamin C is expressed in various cell types especially in differentiated cells within tissues such as muscle cardiac and certain epithelial cells. It helps to maintain nuclear stability and influences gene expression by interacting with chromatin.
Biological function summary

Lamin C contributes to the architecture of the nuclear envelope as part of the lamina complex. This structural role influences the mechanical properties of cells which affects how cells respond to mechanical stress. Lamin C associates with proteins from the inner nuclear membrane and chromatin playing an essential role in nuclear organization. Disruptions in Lamin C function can affect the physical properties of nuclei impacting gene regulation and cell function.

Pathways

Multiple processes integrate Lamin C including the mitogen-activated protein kinase (MAPK) signaling pathway and the PI3K/AKT pathway. In these pathways Lamin C can interact with proteins like MAPK and Akt which are important for transmitting signals that regulate cell growth survival and differentiation. In these processes Lamin C ensures proper cell cycle progression and nuclear structural integrity highlighting its significant involvement in cellular dynamics.

Mutations and malfunctions in Lamin C are connected to muscular dystrophies and cardiomyopathies. These diseases highlight the importance of Lamin C in maintaining muscle tissue integrity and proper cardiac function. Lamin C mutations often co-occur with dysfunctions in Lamin A as both arise from the same precursor protein leading to overlapping symptoms in conditions like Emery-Dreifuss muscular dystrophy and dilated cardiomyopathy.

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 involved 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 (8)

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

microPublication biology 2024: PubMed38440331

2024

Nuclear shape is affected differentially by loss of lamin A, lamin C, or both lamin A and C.

Applications

Unspecified application

Species

Unspecified reactive species

Mai Pho,Yasmin Berrada,Aachal Gunda,Andrew D Stephens

Oncology letters 26:533 PubMed38020294

2023

LAMC2 is a potential prognostic biomarker for cholangiocarcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Khaa Hoo Ong,Yao-Yu Hsieh,Hong-Yue Lai,Ding-Ping Sun,Tzu-Ju Chen,Steven Kuan-Hua Huang,Yu-Feng Tian,Chia-Lin Chou,Yow-Ling Shiue,Hung-Chang Wu,Ti-Chun Chan,Hsin-Hwa Tsai,Chien-Feng Li,Yu-Hsuan Kuo

The Journal of cell biology 221: PubMed36301259

2022

Nucleoplasmic lamin C rapidly accumulates at sites of nuclear envelope rupture with BAF and cGAS.

Applications

IHC-P

Species

Human

Yohei Kono,Stephen A Adam,Yuko Sato,Karen L Reddy,Yixian Zheng,Ohad Medalia,Robert D Goldman,Hiroshi Kimura,Takeshi Shimi

Genome biology 22:305 PubMed34775987

2021

Lamin C is required to establish genome organization after mitosis.

Applications

Unspecified application

Species

Unspecified reactive species

Xianrong Wong,Victoria E Hoskins,Ashley J Melendez-Perez,Jennifer C Harr,Molly Gordon,Karen L Reddy

International journal of molecular sciences 21: PubMed32155994

2020

Perinuclear Lamin A and Nucleoplasmic Lamin B2 Characterize Two Types of Hippocampal Neurons through Alzheimer's Disease Progression.

Applications

Unspecified application

Species

Unspecified reactive species

Laura Gil,Sandra A Niño,Erika Chi-Ahumada,Ildelfonso Rodríguez-Leyva,Carmen Guerrero,Ana Belén Rebolledo,José A Arias,María E Jiménez-Capdeville

Oxidative medicine and cellular longevity 2019:8239642 PubMed31885818

2019

FA-97, a New Synthetic Caffeic Acid Phenethyl Ester Derivative, Protects against Oxidative Stress-Mediated Neuronal Cell Apoptosis and Scopolamine-Induced Cognitive Impairment by Activating Nrf2/HO-1 Signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Ting Wan,Zihao Wang,Yi Luo,Yifan Zhang,Wei He,Yu Mei,Jincheng Xue,Min Li,Huafeng Pan,Weirong Li,Qi Wang,Yujie Huang

Cells 7: PubMed29690642

2018

Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

Applications

Unspecified application

Species

Unspecified reactive species

Xiang Lu,Karima Djabali

Oncotarget 7:24700-18 PubMed27015553

2016

Progerin impairs chromosome maintenance by depleting CENP-F from metaphase kinetochores in Hutchinson-Gilford progeria fibroblasts.

Applications

ICC/IF

Species

Human

Veronika Eisch,Xiang Lu,Diana Gabriel,Karima Djabali
View all publications

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

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com