Recombinant Human Vitamin D Binding protein (His tag) is a Human Fragment protein, in the 19 to 474 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
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| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation.
Vitamin D-binding protein, DBP, VDB, Gc protein-derived macrophage activating factor, Gc-globulin, Group-specific component, Vitamin D-binding protein-macrophage activating factor, Gc-MAF, GcMAF, Gc, DBP-maf, GC
Recombinant Human Vitamin D Binding protein (His tag) is a Human Fragment protein, in the 19 to 474 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation.
Belongs to the ALB/AFP/VDB family.
Allele GC*1S is O-glycosylated at Thr-436 (PubMed:20079467). The trisaccharide sugar moiety can be modified by the successive removal of neuraminic acid and galactose leaving an O-mceeN-acetyl-galactosamine. This conversion is thought to produce a macrophage-activating factor (Gc-MAF). Only a minor proportion of plasma GC is O-glycosylated (PubMed:17360250). The potential N-glycosylation site predicted at Asn-288 is thought to be nonglycosylated.
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