SELENON Antibody, FITC conjugated
Description
Technical Overview of SELENON Antibody, FITC Conjugated
SELENON (selenoprotein N) is a glycoprotein localized to the endoplasmic reticulum, critical for protein folding and degradation of misfolded proteins. Mutations in the SELENON gene are linked to congenital muscular dystrophies, such as rigid spine muscular dystrophy (RSMD1) .
The FITC-conjugated SELENON antibody leverages:
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FITC: A fluorophore with excitation/emission wavelengths of ~498 nm and ~519 nm, respectively, optimized for green fluorescence detection .
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Epitope specificity: Targets the SELENON protein’s unique sequence, such as the immunogen sequence WSLVKELEELQNKQENSSHQKLAGLHLEKYSFPVEMMICLPNGTVVHHINANYFLDITSVKPEEIESNLFSFSSTFEDPST .
Key Properties:
Immunofluorescence and Localization Studies
FITC-conjugated SELENON antibodies are employed to visualize endoplasmic reticulum (ER) localization in cells. For example:
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Muscle tissue analysis: Detects SELENON in skeletal muscle fibers, aiding studies on muscular dystrophy pathogenesis .
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Cell culture models: Used to monitor ER stress responses in conditions like hypoxia or drug-induced toxicity .
Immunohistochemistry (IHC)
In tissue sections, these antibodies enable spatial mapping of SELENON expression:
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Reactivity: Demonstrated in human, mouse, and rat tissues, with optimal dilutions of 1:500–1:1000 .
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Limitations: Background fluorescence may require optimization with blocking agents .
Flow Cytometry
FITC-conjugated SELENON antibodies can quantify protein expression in live or fixed cells:
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Advantage: Rapid analysis of SELENON levels in cell populations, critical for studying protein turnover .
Comparative Analysis of Conjugates
| Conjugate | Excitation/Emission (nm) | Applications | Photostability | Multiplexing Capability |
|---|---|---|---|---|
| FITC | 498/519 | IF, IHC, Flow Cytometry | Moderate | Compatible with TRITC, Cy3 |
| HRP | N/A | ELISA, WB | N/A | N/A |
| Biotin | N/A | ELISA, Pull-down assays | High | Limited |
FITC’s broad emission spectrum may necessitate filter optimization in multiplex experiments .
Challenges and Future Directions
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Limited Experimental Data: Publicly available studies focus on unconjugated SELENON antibodies; FITC-conjugated variants require validation in peer-reviewed research.
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Stability Concerns: FITC’s susceptibility to photobleaching may limit long-term imaging applications .
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Therapeutic Potential: While not directly explored for SELENON, FITC-conjugated antibodies could enable targeted imaging in preclinical models .
Product Specs
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
- Case Report: rigid spine muscular dystrophy 1 in a compound heterozygote with two novel mutations in the SEPN1 gene; a novel missense mutation (c.1384T>C; p.Sec462Arg) and a novel nonsense mutation (c.1525C>T; p.Gln509Ter), inherited from the father and mother respectively. PMID: 27863379
- This study reports two previously undescribed mutations in SEPN1, adding two novel homozygous mutations to the existing repertoire of reported pathogenic SEPN1 variants. PMID: 26780752
- This review article explores the physiological function of SelN in muscle tissue and the pathogenesis of SEPN1-related myopathies. PMID: 22527882
- This study provides evidence that the spectrum of severity of SEPN1-related myopathies is broader than previously reported. PMID: 21670436
- This study demonstrates that Argonaute 2 expression is crucial for stem cells to escape senescence by downregulating miR10b and miR23b. It also highlights the involvement of selenoprotein N1 in the survival and self-renewal of ATSCs through ROS-mediated p38 MAPK inactivation. PMID: 21241449
- This study presents a series of patients illustrating the clinical, histopathological, and MRI findings of SEPN1-related myopathy. It also adds new mutations to the limited number of fully described pathogenic SEPN1 variants. PMID: 20937510
- This study reveals that mutations in the selenoprotein N gene, previously implicated in rigid spine muscular dystrophy, can cause the classical phenotype of multiminicore disease. PMID: 12192640
- A new SEPN1 point mutation, 943g->A causing G315S, was identified in a rigid spine muscular dystrophy patient with cor pulmonale. PMID: 15668457
- SEPN1 mutation analysis revealed that the patient was a compound heterozygote carrying a previously described insertion (713-714 insA) and a novel nonsense mutation (R439stop). PMID: 15792869
- This study reports two patients presenting with 'Dropped head syndrome' due to mutations in SEPN1 genes. PMID: 15961312
- This study identifies SEPN1 as the second genetic cause of CFTD and the first cause of autosomal recessive CFTD. CFTD is now recognized as the fourth clinicopathological presentation associated with mutations in SEPN1. PMID: 16365872
- This study identifies a mutation affecting a conserved base in the selenocysteine insertion sequence functional motif, revealing a novel pathological mechanism leading to SEPN1-related myopathy. PMID: 16498447
- This study explores the possible molecular mechanism behind mutations in SEPN1, clarifying the molecular mechanisms of this muscular disorder. PMID: 16779558
- SEPN1 and RYR1 are essential for the same cellular differentiation events and are required for normal calcium fluxes. PMID: 18713863
- This study highlights the importance of the SRE element during SelN expression and illustrates a novel molecular mechanism by which point mutations may lead to SEPN1-related myopathy. PMID: 19067361
- This study emphasizes that SelN plays a key role in redox homeostasis and human cell protection against oxidative stress. PMID: 19557870
- The Alu-derived exon 3 of human SEPN1 acquired its muscle-specific splicing activity after the divergence of humans and chimpanzees, suggesting its potential role in human evolution. PMID: 18841251
