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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human DBP Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 17.90 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Pro193-Leu325 |
Aliases /Synonyms | Albumin D box-binding protein, TaxREB302, Tax-responsive enhancer element-binding protein 302, D site-binding protein, DBP, Albumin D-element-binding protein |
Reference | ARO-P10756 |
Note | For research use only. |
Recombinant Human DBP Protein, also known as Vitamin D Binding Protein, is a glycoprotein that plays a crucial role in the transport of vitamin D and its metabolites in the blood. It is encoded by the GC gene and is primarily synthesized in the liver. This protein has been extensively studied and has shown to have various structural and functional properties that make it a valuable tool in the field of biotechnology and medicine. In this article, we will explore the structure, activity, and applications of Recombinant Human DBP Protein.
Recombinant Human DBP Protein is a single-chain polypeptide with a molecular weight of approximately 52 kDa. It consists of 458 amino acids and has a three-dimensional structure that is composed of multiple domains. The protein has a globular shape and is composed of three distinct domains – the N-terminal domain, the central domain, and the C-terminal domain.
The N-terminal domain is responsible for the binding of vitamin D and its metabolites, while the central domain is involved in the binding of fatty acids. The C-terminal domain, on the other hand, plays a crucial role in the binding of actin and other proteins. The structure of Recombinant Human DBP Protein is highly conserved among different species, indicating its importance in biological processes.
Recombinant Human DBP Protein is primarily known for its role in the transport of vitamin D and its metabolites in the blood. It binds to these molecules with high affinity and protects them from degradation, thereby increasing their half-life in the circulation. This protein also has a role in regulating the levels of free vitamin D in the blood, which is essential for maintaining calcium homeostasis and bone health.
In addition to its role in vitamin D transport, Recombinant Human DBP Protein has been shown to have immunomodulatory properties. It has been found to interact with various immune cells and modulate their functions, such as T cell proliferation and cytokine production. This suggests that this protein may have a role in regulating immune responses and could be a potential target for immunotherapeutic interventions.
Recombinant Human DBP Protein has a wide range of applications in both research and medicine. Its ability to bind to vitamin D and its metabolites with high affinity makes it a valuable tool for studying the metabolism and transport of this essential vitamin. It is also used in diagnostic assays to measure vitamin D levels in the blood.
Furthermore, Recombinant Human DBP Protein has been investigated as a potential therapeutic agent for various diseases. Its immunomodulatory properties make it a promising candidate for the treatment of autoimmune disorders, such as multiple sclerosis and rheumatoid arthritis. It has also been studied for its potential role in cancer therapy, as it has been found to inhibit tumor growth and induce cell death in cancer cells.
In conclusion, Recombinant Human DBP Protein is a versatile protein with a well-defined structure and diverse biological activities. Its role in vitamin D transport and immunomodulation make it a valuable tool for research and potential therapeutic applications. With ongoing studies and advancements in biotechnology, the potential of this protein is yet to be fully explored, and it holds great promise for the future of medicine.
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