- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
Clusterin Antibody / Secreted Chaperone Protein Marker [clone CLU/8865R] (V5240)
Email: info@nsjbio.com
| Catalog No | Formulation | Size | Price (USD) | ||
|---|---|---|---|---|---|
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V5240-100UG | 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide | 100 ug | 559 | |
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V5240-20UG | 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide | 20 ug | 259 | |
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V5240SAF-100UG | 1 mg/ml in 1X PBS; BSA free, sodium azide free | 100 ug | 559 |
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| Availability | 1-3 business days |
| Species Reactivity | Human |
| Format | Purified |
| Host | Rabbit |
| Clonality | Recombinant Rabbit Monoclonal |
| Isotype | Rabbit IgG, kappa |
| Clone Name | CLU/8865R |
| Purity | Protein A/G affinity |
| UniProt | P10909 |
| Localization | Nucleus, Cytoplasm |
| Applications | Immunohistochemistry (FFPE) : 1-2ug/ml for 30 min at RT |
| Limitations | This Clusterin Antibody / Secreted Chaperone Protein Marker is available for research use only. |
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Clusterin (CLU) is a secreted glycoprotein that functions as a molecular chaperone involved in protein folding, stabilization, and extracellular proteostasis. Clusterin antibody is widely used to study this protein’s role in maintaining protein homeostasis across diverse tissues, where it protects cells from stress-induced damage by binding misfolded or aggregated proteins. This function is particularly important in environments characterized by oxidative stress, inflammation, or high protein turnover.
Clusterin Antibody / Secreted Chaperone Protein Marker, also known as CLU antibody, APO-J antibody, or Apolipoprotein J antibody in the literature, enables detection of this multifunctional protein in pathways associated with extracellular chaperone activity, lipid transport, and immune modulation. Additional Clusterin antibody variants are available for stress response, lipid transport, and neurodegeneration-focused research applications. Unlike intracellular chaperones, Clusterin is secreted into the extracellular space where it stabilizes proteins and prevents aggregation, acting as a first-line defense against proteotoxic stress in the tissue microenvironment. This extracellular chaperone role is a defining feature of Clusterin biology and a key reason it is widely studied in disease contexts.
Functionally, Clusterin binds partially unfolded or damaged proteins, forming soluble complexes that facilitate clearance and prevent toxic aggregation. This activity is essential in maintaining proteostasis under both normal and stress conditions. Clusterin Antibody is therefore valuable for investigating protein quality control mechanisms, particularly in tissues undergoing remodeling or injury. In addition, Clusterin participates in lipid transport through association with lipoprotein particles, linking its chaperone function to broader roles in extracellular homeostasis.
Clusterin also contributes to immune regulation by interacting with complement system components and modulating inflammatory signaling. These interactions allow it to influence tissue repair and cellular protection in response to damage. Its widespread expression and secretion into biological fluids further support its role as a systemic regulator of protein stability and immune balance.
Subcellularly, Clusterin is synthesized in the endoplasmic reticulum, glycosylated, and secreted through the classical secretory pathway. Post-translational processing results in multiple protein forms, including cleaved and heavily glycosylated variants that may be detected as distinct bands in western blot analysis. In immunohistochemistry, Clusterin is typically observed in both cytoplasmic and extracellular compartments, reflecting its synthesis and secretion dynamics.
This Clusterin antibody is supported by immunohistochemistry data demonstrating detection in tissue samples consistent with known expression patterns, as well as protein microarray specificity validation confirming selective binding. Together, these features support its use in studies of extracellular chaperone function, protein homeostasis, and tissue-level stress adaptation.
This antibody is part of a broader range of Clusterin antibody products supporting research into chaperone function, stress response, and disease biology.
Optimal dilution of the Clusterin Antibody / Secreted Chaperone Protein Marker should be determined by the researcher.
A recombinant partial protein sequence (within amino acids 249-449) from the human protein was used as the immunogen for the Clusterin antibody.
Aliquot the Clusterin antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
CLU antibody, APO-J antibody, Apolipoprotein J antibody, Clusterin protein antibody, Secreted clusterin antibody
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