PLEC Antibodies
Background
PLEC gene encoding a large cytoskeleton proteins, called plectin are mainly distributed in the tissue of the skin, muscles, and nerves. This protein, as a multifunctional linker molecule, can integrate the cytoskeletal network, maintain the integrity of the cell structure, and participate in key physiological processes such as cell movement and signal transduction. Research has found that plectin is particularly important for maintaining the mechanical stability of muscle fibers and epidermal cells. Its deficiency can lead to diseases such as epidermolysis bullosa and muscular dystrophy. The PLEC gene was initially identified by the team of German scientist Gerhard Wiche in the 1990s. Its complex molecular structure and diverse subtypes make it an important model for cytoskeletal research. In-depth research on this gene not only reveals the molecular mechanism of cytoskeletal organization but also provides new targets for the treatment of various genetic diseases.
Structure of PLEC
The plectin protein encoded by the PLEC gene is a large cytoskeletal junction protein with a molecular weight of approximately 500 kDa, and its molecular weight varies slightly among different species.
Species | Human | Mouse | Rat | Bovine |
Molecular Weight (kDa) | 500 | 498 | 499 | 501 |
Primary Structural Differences | Contains multiple functional domains (e.g., actin, microtubule, intermediate filament binding domains) | Highly conservative and highly homologous to human PLEK | Similar to the human PLEK structure | There is a small amount of amino acid variation |
Plectin protein is composed of over 4,600 amino acids and features a complex multi-domain architecture, including an actin binding domain at the N-terminal, a coiled-helix domain in the middle, and an intermediate fiber-binding domain at the C-terminal. Its core function relies on multiple repetitive units, which enable it to bridge different cytoskeletal networks (such as microfilaments, microtubules and intermediate filaments), maintaining the mechanical stability of the cell. This protein also contains multiple phosphorylation sites, which regulate its role in cell migration, signal transduction and damage repair. Mutations in Plectin can lead to a variety of genetic diseases, such as epidermolysis bullosa and muscular dystrophy, highlighting its crucial role in tissue integrity.
Fig. 1 Biological evolution and the conserved domains of the PLEC gene.1
Key structural properties of PLEC:
- Multi-domain architecture
- Conservative serial repeating units
- Phosphorylation regulatory site
- Dimerization ability
Functions of PLEC
The core function of the plectin protein encoded by the PLEC gene is to maintain the structural integrity of the cytoskeletal network and participate in a variety of key cellular physiological processes.
Function | Description |
Cytoskeletal junction | As a molecular bridge, it simultaneously combines microfilaments (F-actin), microtubules and intermediate fibers to maintain the mechanical stability of cells. |
Tissue tensile strength | Provides tensile strength in skin, muscle and nerve tissue, preventing cellular damage caused by mechanical stress. |
Regulation of cell migration | By integrating cytoskeletal dynamics, it influences the processes of wound healing, embryonic development and cancer cell metastasis. |
Signal transduction intermediary | As a scaffold protein, it participates in the regulation of signaling pathways such as MAPK and PI3K/AKT. |
Disease-related functions | Mutations can lead to epidermolysis bullosa (increased skin fragility) and muscular dystrophy (muscle degeneration). |
The plectin protein dynamically coordinates the interactions among different cytoskeletal systems through its multiple functional domains. The loss of its function can significantly affect the integrity of tissues with high mechanical stress, such as skin and muscle. Unlike single-function proteins (such as myoglobin), plectin exhibits typical "multitasking" properties, which are crucial for maintaining tissue homeostasis in multicellular organisms.
Applications of PLEC and PLEC Antibody in Literature
1. Koskeridis, Fotios, et al. "Multi-trait association analysis reveals shared genetic loci between Alzheimer's disease and cardiovascular traits." Nature Communications 15.1 (2024): 9827. https://doi.org/10.1038/s41467-024-53452-6
Research has found that the gene locus rs11786896 is expressed in the left ventricle and brain astrocytes through PLEC, simultaneously influencing Alzheimer's disease and atrial fibrillation. PLEC is upregulated in heart failure and Alzheimer's disease, suggesting it as a potential therapeutic target.
2. Tao, et al. "ΔNp63α promotes radioresistance in esophageal squamous cell carcinoma through the PLEC-KEAP1-NRF2 feedback loop." Cell Death & Disease 15.11 (2024): 793. https://doi.org/10.1038/s41419-024-07194-4
Research has found that ΔNP63α promotes antioxidant responses by up-regulating PLEC expression and competitively binding to KEAP1 to release NRF2, leading to radiotherapy resistance in esophageal squamous cell carcinoma. Targeting NRF2 can enhance radiosensitivity.
3. Ni, Kai-Di, et al. "Epoxy metabolites of linoleic acid promote the development of breast cancer via orchestrating PLEC/NFκB1/CXCL9-mediated tumor growth and metastasis." Cell Death & Disease 15.12 (2024): 901. https://doi.org/10.1038/s41419-024-07300-6
Research has found that EpOMEs activate the NFκB1/CXCL9 axis by upregulating PLEC, promoting the progression of triple-negative breast cancer. Targeting the PLEC or CYP2J2-EpOMEs pathway may become a potential therapeutic strategy.
4. Sorial, A. K., et al. "Multi-tissue epigenetic analysis of the osteoarthritis susceptibility locus map** to the plectin gene PLEC." Osteoarthritis and Cartilage 28.11 (2020): 1448-1458. https://doi.org/10.1016/j.joca.2020.06.001
Research has found that the OA risk site rs11780978 regulates its expression in cartilage and synovium through PLEC methylation (mQTL), influencing OA-related pathways such as Wnt signaling. The synovium and cartilage share this genetic mechanism, but there is no functional association of mQTL in the fat pad.
5. Wang, Ke, et al. "Effects of Copy Number Variations in the Plectin (PLEC) Gene on the Growth Traits and Meat Quality of Leizhou Black Goats." Animals 13.23 (2023): 3651. https://doi.org/10.3390/ani13233651
Research has found that the gain type of CNV-1 in the PLEC gene of Leizhou Black goats significantly enhances muscle development-related traits (such as body weight and eye muscle area) and the expression level of PLEC in the muscles, and can be used as a molecular marker to assist in breeding.
Creative Biolabs: PLEC Antibodies for Research
Creative Biolabs specializes in the production of high-quality PLEC antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.
- Custom PLEC Antibody Development: Tailor-made solutions to meet specific research requirements.
- Bulk Production: Large-scale antibody manufacturing for industry partners.
- Technical Support: Expert consultation for protocol optimization and troubleshooting.
- Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.
For more details on our PLEC antibodies, custom preparations, or technical support, contact us at email.
Reference
- Wang, Ke, et al. "Effects of Copy Number Variations in the Plectin (PLEC) Gene on the Growth Traits and Meat Quality of Leizhou Black Goats." Animals 13.23 (2023): 3651. https://doi.org/10.3390/ani13233651
Anti-PLEC antibodies

Hot products 
- AActivation
- AGAgonist
- APApoptosis
- BBlocking
- BABioassay
- BIBioimaging
- CImmunohistochemistry-Frozen Sections
- CIChromatin Immunoprecipitation
- CTCytotoxicity
- CSCostimulation
- DDepletion
- DBDot Blot
- EELISA
- ECELISA(Cap)
- EDELISA(Det)
- ESELISpot
- EMElectron Microscopy
- FFlow Cytometry
- FNFunction Assay
- GSGel Supershift
- IInhibition
- IAEnzyme Immunoassay
- ICImmunocytochemistry
- IDImmunodiffusion
- IEImmunoelectrophoresis
- IFImmunofluorescence
- IHImmunohistochemistry
- IMImmunomicroscopy
- IOImmunoassay
- IPImmunoprecipitation
- ISIntracellular Staining for Flow Cytometry
- LALuminex Assay
- LFLateral Flow Immunoassay
- MMicroarray
- MCMass Cytometry/CyTOF
- MDMeDIP
- MSElectrophoretic Mobility Shift Assay
- NNeutralization
- PImmunohistologyp-Paraffin Sections
- PAPeptide Array
- PEPeptide ELISA
- PLProximity Ligation Assay
- RRadioimmunoassay
- SStimulation
- SESandwich ELISA
- SHIn situ hybridization
- TCTissue Culture
- WBWestern Blot
