Analytical Data
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Gene name
Vitamin D-binding protein/GC
- Application
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Alternative Names
/
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Species
Human herpesvirus 1
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P10228
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Expression Region
250-480aa
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Molecular Weight
33.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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), is a multifunctional protein primarily synthesized in the liver, playing a critical role in the transport of vitamin D metabolites in the circulatory system. Its significance extends beyond vitamin D transport, as DBP is involved in several physiological processes, including macrophage activation, immune regulation, and bone metabolism. Given its diverse biological functions, variations in DBP levels have been associated with various health conditions, such as osteoporosis, cardiovascular diseases, and certain cancers. The study of recombinant DBP (rDBP) has gained traction in recent years as researchers seek to understand its structure-function relationship and therapeutic potential. Recombinant techniques allow for the production of DBP in a controlled manner, facilitating investigations into its role in disease pathways and potential applications in clinical settings. Moreover, rDBP can be utilized in diagnostic assays to measure DBP levels in clinical samples, further highlighting the protein's relevance in health monitoring. As ongoing research unveils more about the mechanisms through which DBP influences health, there is growing interest in its potential as a biomarker for disease progression and treatment response, making rDBP a significant focus for both clinical and laboratory research.
