Analytical Data
-
Gene name
Vitamin D-binding protein/GC
- Application
-
Alternative Names
GC; VDBG; VDBP; Group-Specific Component; Gc-globulin
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P02774
-
Expression Region
Glu18~Leu211
-
Molecular Weight
26kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Vitamin D-binding protein (DBP), also known as group-specific component (GC), plays a critical role in the transport of vitamin D metabolites and other bioactive molecules in the bloodstream. It is a multifunctional protein that not only binds vitamin D and its metabolites but also acts in immune regulation, inflammation, and tissue repair. DBP has gained research interest due to its association with various health conditions, including osteoporosis, autoimmune diseases, and certain cancers. Understanding the structure and function of DBP is crucial, as alterations in its levels can impact vitamin D availability and lead to deficiencies or related diseases. Recombinant DBP studies have been undertaken to investigate its functional properties and therapeutic potential. These studies involve cloning the DBP gene, expressing it in suitable host systems, and characterizing the resultant recombinant protein to explore its binding affinities and biological effects. This research could establish the foundation for developing novel vitamin D-related therapies and improving our understanding of the protein's role in health and disease. Overall, the study of recombinant Vitamin D-binding protein/GC offers valuable insights into its biological importance and potential application in clinical settings.
