NUP210 Antibody
Description
NUP210 Antibody: Definition and Core Applications
NUP210 antibodies are immunoreagents designed to bind specifically to the NUP210 protein, a transmembrane nucleoporin critical for nuclear pore complex (NPC) structure and function. These antibodies are widely used in:
Muscle Differentiation and ER Stress Regulation
NUP210 antibodies revealed that NUP210’s luminal domain (amino acids 1–1,783) is essential for muscle cell differentiation. Key insights include:
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Rescue of differentiation defects in NUP210-depleted C2C12 myoblasts using truncated NUP210 constructs .
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Activation of ER stress-specific caspase-12 in NUP210 knockdown cells, linking NUP210 to ER homeostasis .
Table 1: NUP210 in Muscle Differentiation
| Parameter | Finding | Method Used | Source |
|---|---|---|---|
| Differentiation rescue | Luminal domain sufficient for myogenesis | shRNA + rescue assay | |
| Apoptosis mechanism | Caspase-12 activation via ER stress | Western blot |
Metastasis Suppression in Breast Cancer
In ER+ breast cancer models, NUP210 antibodies identified its role as a mechanosensor and chromatin organizer:
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NUP210 depletion reduced lung metastasis by 60–80% in 4T1 mouse models .
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Interaction partners: SUN2 (LINC complex), BRD4, and histone H3.1/H3.2 via Co-IP .
Table 2: NUP210 in Cancer Metastasis
| Interaction Partner | Functional Role | Experimental Model | Source |
|---|---|---|---|
| SUN2 | Nuclear-cytoskeletal linkage | CRISPR/Cas9 KO | |
| H3.1/H3.2 | Chromatin anchoring at nuclear periphery | Co-IP + ChIP-seq |
Immune System Regulation
NUP210 knockout mice studies using flow cytometry and antibody-based profiling showed:
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Altered CD4+/CD8+ T cell ratios (1.8:1 in WT vs. 2.5:1 in KO) .
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Increased IFNγ-producing CD4+ and CD8+ T cells, suggesting enhanced Th1 responses .
Technical Considerations for NUP210 Antibody Usage
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Epitope specificity: Most antibodies target the conserved luminal domain (e.g., residues 1–300) .
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Cross-reactivity: Validated in human, mouse, and rat models .
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Functional assays: Optimal for formaldehyde-fixed samples in immunofluorescence .
Research Gaps and Future Directions
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Structural details of NUP210’s luminal domain remain unresolved.
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Clinical potential in ER+ breast cancer requires validation in patient-derived xenografts.
Product Specs
Target Background
- Solution structure of the C-terminal domain of NUP210 PMID: 12653556
- GP210 (NUP210) plays critical roles at the nuclear membrane PMID: 14517331
- WT1 is likely not regulating GP210 (NUP210) expression, despite the presence of binding sites for WT1 PMID: 15613247
- Quantitation of serum anti-gp210-C-terminal peptide antibodies is valuable for monitoring the effectiveness of ursodeoxycholic acid therapy and for early identification of patients at high risk of end-stage hepatic failure. PMID: 15710222
- The increased expression of gp210 (NUP210) in small bile ducts may contribute to the autoimmune response to gp210, leading to the progression to end-stage hepatic failure in primary biliary cirrhosis. PMID: 16337775
- Double knockdowns of gp210 (NUP210) in HeLa cells suggest that nuclear pore complexes can assemble or persist in a gp210-free form. PMID: 16702234
