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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Clusterin (CLU) is a secreted glycoprotein that undergoes extensive post-translational modification, including glycosylation and proteolytic cleavage, resulting in multiple detectable molecular forms in western blot analysis. Clusterin Antibody for WB is widely used to study this proteinâs expression, processing, and secretion, where it typically appears as a heterodimeric precursor at approximately 75-80 kDa along with lower molecular weight alpha and beta subunits generated through proteolytic cleavage.
Clusterin Antibody for WB / Secreted Glycoprotein Detection, also known as CLU antibody, APO-J antibody, or Apolipoprotein J antibody in the literature, enables detection of this protein in lysate-based assays where accurate identification of multiple processed forms is essential. Due to its secreted and heavily glycosylated nature, Clusterin often exhibits variable electrophoretic mobility depending on glycosylation state, sample preparation, and tissue origin. This complexity makes western blot-validated antibodies critical for reliable interpretation of banding patterns.
Functionally, Clusterin acts as an extracellular chaperone that binds misfolded proteins and prevents aggregation, contributing to protein homeostasis in both normal and stress conditions. These functions are closely linked to its maturation and secretion, which can be directly assessed by western blot through detection of precursor and cleaved forms. The presence of multiple bands provides insight into protein processing, secretion efficiency, and cellular stress status.
Clusterin is broadly expressed across tissues and is often enriched in secretory and stress-responsive environments. In western blot experiments, stronger signal intensity may be observed in tissues with high secretory activity or elevated stress response, reflecting increased synthesis and processing of the protein. This makes Clusterin Antibody for WB particularly useful for comparative analysis of expression levels and post-translational modification states.
Subcellularly, Clusterin is synthesized in the endoplasmic reticulum, glycosylated, and cleaved into alpha and beta chains prior to secretion. These biochemical features directly influence its electrophoretic behavior, resulting in characteristic banding patterns that include both full-length and processed forms. Proper interpretation of these bands is essential for understanding Clusterin biology in experimental systems.
This Clusterin antibody is supported by western blot data demonstrating clear detection of expected molecular weight forms, along with immunohistochemistry data confirming tissue expression patterns. Together, these features support its use in studies of protein processing, secretion dynamics, and extracellular chaperone function.
This antibody is part of a broader range of Clusterin antibody products supporting research into chaperone function, stress response, and disease biology.
The stated application concentrations are suggested starting points. Titration of the Clusterin Antibody for WB / Secreted Glycoprotein Detection may be required due to differences in protocols and secondary/substrate sensitivity.
A peptide corresponding to the C-terminus of Clusterin was used as the immunogen for the recombinant Clusterin antibody.
Store the Clusterin antibody at -20oC.
Clusterin antibody, CLU antibody, APO-J antibody, Apolipoprotein J antibody, Clusterin WB antibody
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