G8764
Gc-globulin from human plasma
≥90% (SDS-PAGE), lyophilized powder (containing sodium chloride and sodium phosphate buffer salt)
Synonym(s):
DBP, Group-Specific Component, Vitamin D Binding Protein
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General description
Gc-Globulin, a member of the albumin superfamily, is the major plasma carrier of vitamin D and its metabolites. It is also, along with gelsolin, part of the extracellular actin scavenger system. Gc-globulin also binds monomeric actin (G-actin) with high affinity to scavenge actin released by necrotic cells, preventing its polymerization into filaments. Gc-globulin enhances the chemoattractant activity of C5a for inflammatory cells.
Gc-globulin from human plasma is encoded by the gene GC, which is mapped to human chromosome 4q13.3.
Gc-globulin or the vitamin D binding protein (DBP) is a 51-58 kDa multifunctional serum glycoprotein synthesized in large quantities by primarily in the liver. It is a member of the albumin gene family and has the characteristic multiple disulfide-bonded, triple domain structure.
Application
Gc-globulin from human plasma has been used:
- as a fluorescent probe for G-actin staining
- as a fluorescent probe to monitor steady-state rate of actin filament disassembly
- as a calibrator for liquid chromatography with mass spectrometry (LC-MS/MS)
Gc-globulin is a multifunctional, albumin-like plasma protein that often requires cell surface binding to mediate some of its diverse functions. It has been used to anlayze its glycosylation patterns.
Biochem/physiol Actions
Gc-Globulin, a member of the albumin superfamily, is the major plasma carrier of vitamin D and its metabolites. It is also, along with gelsolin, a part of the extracellular actin scavenger system. Gc-globulin also binds monomeric actin (G-actin) with high affinity to scavenge actin released by necrotic cells, preventing its polymerization into filaments. Gc-globulin enhances the chemoattractant activity of C5a for inflammatory cells.
Single nucleotide polymorphism in the gene GC is associated with deficiency of 25-hydroxyvitamin D [25(OH)D].
Preparation Note
Native Gc-globulin from human plasma
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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K Jie et al.
Journal of hypertension. Supplement : official journal of the International Society of Hypertension, 3(3), S145-S147 (1985-12-01)
Effects of exogenous and endogenous noradrenaline, released by tyramine and lower body negative pressure (LBNP), on vascular post-synaptic alpha 1- and alpha 2-adrenoceptors have been compared in healthy volunteers. Intra-arterial (i.a.) infusions of noradrenaline and tyramine into the forearm were
Cofilin-2 controls actin filament length in muscle sarcomeres
Kremneva E, et al.
Developmental Cell, 31(2), 215-226 (2014)
Acute homeostatic changes following Vitamin D2 supplementation
Berg AH, et al.
Journal of the Endocrine Society, 1(9), 1135-1149 (2017)
David Palmer et al.
Internal medicine journal, 52(1), 89-94 (2020-10-12)
Free concentrations of highly protein bound hormones, such as cortisol and thyroxine, are unchanged in critical illness despite substantial decreases in total concentration. Total 25-hydroxyvitamin D (25(OH)D) concentration is decreased in critical illness, but the free concentration of 25(OH)D has
V F Rusiaev
Meditsinskaia tekhnika, (3)(3), 36-40 (1987-05-01)
A conductometric method for studying flowing blood coagulation is proposed. Phases of conductograms characterizing the kinetics and intensity of blood cells aggregation, release of biologically active compounds, fibrin formation, its mechanical properties, retraction process and fibrinolysis of clot are analysed
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