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Brand: ProteoGenix

Recombinant Human DBP Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
17.90 kDa

329.00

100ug + 329 loyalty points
Pro193–Leu325
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Recombinant Human DBP Protein, N-His

Recombinant Human DBP Protein, N-His

Product name Recombinant Human DBP Protein, N-His
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.
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 ProteoGenix
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.
Molecular Constructor
Pro193–Leu325

Introduction

Recombinant Human DBP Protein, also known as Vitamin D binding protein, is a multifunctional protein that plays a crucial role in the transport and metabolism of vitamin D in the body. This protein is encoded by the GC gene and is found in the blood and extracellular fluids.

Structure of Recombinant Human DBP Protein

The recombinant form of human DBP protein is a glycoprotein with a molecular weight of approximately 58 kDa. It is composed of 458 amino acids and has a three-dimensional structure similar to that of other members of the albumin superfamily. The protein contains three domains: a N-terminal domain, a central domain, and a C-terminal domain.

The N-terminal domain is responsible for binding to vitamin D and its metabolites, while the central domain is involved in binding to fatty acids and other ligands. The C-terminal domain is responsible for the transport of DBP across the cell membrane.

Activity of Recombinant Human DBP Protein

The main function of recombinant human DBP protein is to bind to and transport vitamin D and its metabolites in the blood. It has a high affinity for 25-hydroxyvitamin D, the major circulating form of vitamin D, and also binds to other forms such as 1,25-dihydroxyvitamin D and 24,25-dihydroxyvitamin D.

In addition to its role in vitamin D transport, DBP has been shown to have other activities such as antioxidant and anti-inflammatory properties. It also plays a role in regulating the immune system and has been implicated in various diseases such as cancer, diabetes, and autoimmune disorders.

Application of Recombinant Human DBP Protein

The production of recombinant human DBP protein has numerous applications in the field of medicine and research. One of the main applications is in the diagnosis and monitoring of vitamin D deficiency. Measurement of DBP levels in the blood can provide valuable information about an individual’s vitamin D status.

Another important application is in the development of therapeutic drugs. Recombinant DBP protein has been used in studies to evaluate its potential as a treatment for various diseases such as diabetes, multiple sclerosis, and inflammatory bowel disease. It has also been investigated as a potential biomarker for predicting the risk of developing certain diseases.

Furthermore, recombinant human DBP protein has been used in research to study the role of vitamin D in various physiological processes and diseases. Its ability to bind to different forms of vitamin D makes it a valuable tool for investigating the mechanisms of action of this important vitamin.

Conclusion

In summary, recombinant human DBP protein is a multifunctional protein with a crucial role in the transport and metabolism of vitamin D. Its structure, activity, and various applications make it a valuable tool in the fields of medicine and research. Further studies on this protein may provide insights into its potential therapeutic uses and shed light on the role of vitamin D in various diseases.

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