
These antibodies are validated on HuProt™ Human Protein Microarrays containing over 21,000 full-length human proteins, including the specific target of interest. LEARN MORE
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Formalin-fixed, paraffin-embedded human liver stained with GC Vitamin D Binding Protein Mouse Monoclonal Antibody (VDBP/9980). Inset: PBS instead of primary antibody; secondary only negative control.

Formalin-fixed, paraffin-embedded human pancreas stained with GC Vitamin D Binding Protein Mouse Monoclonal Antibody (VDBP/9980). Inset: PBS instead of primary antibody; secondary only negative control.
| Document Name | |
|---|---|
| Datasheet | Download Here |
| Material Safety Data Sheet | Download Here |
| Applications | Tested Dilutions | Protocol | Note |
|---|---|---|---|
| Immunohistochemistry (IHC) | 1-2ug/ml | IHC Protocol | 30 min at RT. Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95°C followed by cooling at RT for 20 minutes |
| Western Blot (WB) | 2-4ug/ml | Western Blot Protocol |
Vitamin D-binding protein (DBP) is a multi-functional serum protein that binds to the plasma membranes of numerous cell types and mediates a variety of cellular functions. The locus of the DBP protein (also known as group-specific component protein or GC) is located at human chromosome 4q13.3. DBP functions in organ-specific transportation of vitamin D and its metabolites to the various target organs of the vitamin D endocrine system. In addition, DBP has immunomodulatory properties and is able to bind to the surface of leukocytes. DBP binds to the plasma membrane through a chondroitin sulfate proteoglycan. DBP serves as a co-chemotactic factor for C5a to enhance the chemotactic activity of C5a. DBP can also bind to globular Actin with high affinity and is involved in the clearance of Actin from the blood. DBP plays an important role in osteoclast differentiation. The diverse cellular functions of DBP require its cell surface binding ability to mediate different biological processes.
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