- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Vitamin D binding protein (VDBP), also known as Group-specific component (GC), is a circulating endocrine transport protein involved in systemic distribution of vitamin D metabolites, extracellular actin scavenging, and metabolic homeostasis. The VDBP Antibody / Endocrine Vitamin D Transport Protein Antibody clone VDBP/4481 is positioned for highly selective detection of VDBP expression in studies involving endocrine transport biology, hepatic secretory proteins, vitamin D metabolism, and circulating carrier-associated signaling pathways.
VDBP is encoded by the GC gene on chromosome 4q13 and is synthesized predominantly by hepatocytes before secretion into plasma and extracellular fluids. The protein functions as the principal carrier of vitamin D and its metabolites within the circulation, regulating systemic transport, tissue delivery, and bioavailability of vitamin D-associated endocrine signaling molecules. Because VDBP circulates at high concentrations in serum, the protein serves as a major component of systemic metabolic transport and endocrine homeostasis pathways.
In addition to vitamin D transport, VDBP participates in extracellular actin scavenging mechanisms that help maintain tissue and vascular integrity during cellular injury and inflammatory stress. The protein may also contribute to macrophage-associated immune regulation and cytokine-responsive inflammatory signaling pathways. Altered VDBP levels have been associated with liver dysfunction, inflammatory disease states, kidney-associated disorders, metabolic abnormalities, and disruptions involving calcium and phosphate balance.
VDBP has attracted substantial interest across endocrinology, hepatology, nephrology, and metabolic disease research due to its central role in vitamin D physiology and circulating metabolite transport. Changes in VDBP abundance or binding dynamics may influence vitamin D bioavailability and endocrine signaling responses within multiple tissue systems. The protein is therefore frequently studied alongside markers of metabolic regulation, hepatic secretory function, and systemic inflammatory signaling.
The clone VDBP/4481 monoclonal antibody is further differentiated by protein microarray specificity validation performed against a HuProt(TM) array containing more than 19,000 full-length human proteins. This large-scale specificity screening approach helps evaluate potential cross-reactivity across the human proteome and is particularly valuable for abundant circulating proteins and serum-associated transport factors that may share conserved structural features with related carrier proteins. The resulting specificity profile supports selective detection of VDBP in studies where target specificity and reduced off-target recognition are important experimental considerations.
Immunohistochemical analysis using VDBP antibodies commonly demonstrates cytoplasmic staining patterns within hepatocyte-associated and epithelial tissue compartments consistent with the secretory biology of this circulating transport protein. VDBP continues to serve as an important target in studies involving endocrine metabolism, systemic transport physiology, vitamin D homeostasis, liver-associated biology, and circulating carrier protein regulation.
Additional antibodies involved in endocrine metabolism, hepatic secretory biology, vitamin D homeostasis, and circulating transport-associated signaling pathways can be explored within our Metabolism Antibodies collection.
Optimal dilution of the VDBP antibody should be determined by the researcher.
A portion of amino acids 35-175 was used as the immunogen for the VDBP antibody.
Aliquot the VDBP antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
VDBP antibody, Vitamin D binding protein antibody, GC antibody, Group-specific component antibody, Endocrine vitamin D transport protein antibody
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