- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Clusterin (CLU), also known as Apolipoprotein J (APO-J), is a secreted glycoprotein that functions as both a molecular chaperone and a lipid-associated protein involved in extracellular homeostasis. APO-J antibody is widely used to study this proteinâs role in lipid transport, protein stabilization, and extracellular signaling, particularly in tissues where lipoprotein metabolism and protein turnover are tightly coordinated.
APO-J antibody, also referred to as Clusterin antibody, CLU antibody, or Apolipoprotein J antibody in the literature, enables detection of this multifunctional protein in pathways associated with lipid transport and extracellular chaperone activity. Clusterin associates with high-density lipoprotein-like particles and other lipid-protein complexes, where it contributes to maintaining solubility and preventing aggregation of extracellular proteins. This lipoprotein-associated chaperone function is a defining characteristic of APO-J biology and clearly differentiates it from intracellular stress-response proteins.
Functionally, APO-J binds hydrophobic regions of partially unfolded proteins, forming soluble complexes that facilitate extracellular clearance and prevent deposition in tissues. In parallel, its association with lipoproteins allows it to participate in lipid transport, membrane remodeling, and extracellular signaling processes. APO-J antibody is therefore particularly valuable for studying the interface between lipid metabolism and protein homeostasis, especially in systems involving secreted proteins and circulating factors.
APO-J is broadly expressed in epithelial tissues, liver, and secretory environments, where it is released into extracellular fluids including plasma and interstitial spaces. Its presence in circulation allows it to act in a paracrine and systemic manner, influencing neighboring cells and contributing to tissue-level homeostasis. This extracellular distribution and mobility reinforce its role as a mediator of protein stability and lipid-associated transport mechanisms.
Subcellularly, APO-J is synthesized in the endoplasmic reticulum, glycosylated, and secreted through the classical secretory pathway. Post-translational processing results in heterodimeric forms and heavily glycosylated variants that may be detected as multiple bands in western blot analysis. In immunohistochemistry, APO-J is typically observed in both cytoplasmic and extracellular compartments, consistent with its synthesis, secretion, and accumulation in the tissue microenvironment.
This APO-J antibody is supported by immunohistochemistry and western blot data demonstrating detection of Clusterin in relevant biological samples, along with protein microarray specificity validation confirming selective binding. Together, these features support its use in studies of lipid transport, extracellular chaperone function, and secreted protein biology.
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 APO-J Antibody / Lipid Transport and Chaperone Protein should be determined by the researcher.
A portion of amino acids 150-300 was used as the immunogen for the APO-J antibody.
Aliquot the APO-J antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Clusterin antibody, CLU antibody, Apolipoprotein J antibody, APO-J protein antibody, Lipoprotein-associated clusterin antibody
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