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Merck

G8764

Sigma-Aldrich

Gc-globulin from human plasma

≥90% (SDS-PAGE), lyophilized powder (containing sodium chloride and sodium phosphate buffer salt)

Synonym(e):

DBP

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About This Item

CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352202
NACRES:
NA.61

Biologische Quelle

human plasma

Qualitätsniveau

Assay

≥90% (SDS-PAGE)

Form

lyophilized powder (containing sodium chloride and sodium phosphate buffer salt)

Mol-Gew.

~52 kDa

Methode(n)

LC/MS: suitable

Löslichkeit

H2O: soluble 2 mg/mL

UniProt-Hinterlegungsnummer

Lagertemp.

−20°C

Angaben zum Gen

human ... GC(2638)

Allgemeine Beschreibung

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.[1]
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.[2] It is a member of the albumin gene family and has the characteristic multiple disulfide-bonded, triple domain structure.[3]

Anwendung

Gc-globulin from human plasma has been used:
  • as a fluorescent probe for G-actin staining[4]
  • as a fluorescent probe to monitor steady-state rate of actin filament disassembly[5]
  • as a calibrator for liquid chromatography with mass spectrometry (LC-MS/MS)[6]

Gc-globulin is a multifunctional, albumin-like plasma protein that often requires cell surface binding to mediate some of its diverse functions.[7] It has been used to anlayze its glycosylation patterns.

Biochem./physiol. Wirkung

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].[1]

Angaben zur Herstellung

Native Gc-globulin from human plasma

Haftungsausschluss

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Die Dokumentenbibliothek aufrufen

Phosphoinositide-dependent enrichment of actin monomers in dendritic spines regulates synapse development and plasticity
Lei W, et al.
The Journal of Cell Biology, 216(8), 2551-2564 (2017)
The GC, CYP2R1 and DHCR7 genes are associated with vitamin D levels in northeastern Han Chinese children
Zhang Y, et al.
Swiss Medical Weekly, 142(2930) (2012)
Acute homeostatic changes following Vitamin D2 supplementation
Berg AH, et al.
Journal of the Endocrine Society, 1(9), 1135-1149 (2017)
Cofilin-2 controls actin filament length in muscle sarcomeres
Kremneva E, et al.
Developmental Cell, 31(2), 215-226 (2014)
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

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