Recombinant Human DGKE, N-His

Reference: YHE91901
Product nameRecombinant Human DGKE, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight31.09 kDa
Protein delivered with Tag?N-Terminal His Tag
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°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)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeLeu243-Gly502
Aliases /SynonymsDGKE, Diglyceride kinase epsilon, DAG kinase epsilon, DGK-epsilon, Diacylglycerol kinase epsilon, DAGK5
ReferenceYHE91901
NoteFor research use only.

Description of Recombinant Human DGKE, N-His

Title: Introduction to Recombinant Human DGKE
Recombinant Human DGKE: Structure and Function
Applications of Recombinant Human DGKE in Biomedical Research

Introduction:
Recombinant Human DGKE (Diacylglycerol Kinase E) is a protein that plays a crucial role in lipid metabolism and signaling pathways. It is a member of the diacylglycerol kinase family and is known to regulate the levels of diacylglycerol (DAG) and phosphatidic acid (PA) in the cell. In this article, we will explore the structure, function, and applications of Recombinant Human DGKE in biomedical research.

Recombinant Protein:
Recombinant Human DGKE is a protein that is produced using recombinant DNA technology. It is derived from the human DGKE gene and is expressed in a host cell, such as bacteria or yeast. The resulting protein is identical to the native human DGKE, making it a valuable tool for studying its structure and function.

Structure:
The structure of Recombinant Human DGKE consists of a conserved catalytic domain and a variable regulatory domain. The catalytic domain contains a highly conserved ATP-binding site and a DAG-binding site, which are essential for its enzymatic activity. The regulatory domain, on the other hand, contains several protein-protein interaction sites that control the activity of DGKE.

Function:
Recombinant Human DGKE is a key player in the regulation of lipid signaling pathways. It catalyzes the conversion of DAG to PA, which is involved in various cellular processes, including cell growth, differentiation, and apoptosis. By regulating the levels of DAG and PA, DGKE plays a critical role in maintaining cellular homeostasis.

Applications:
Recombinant Human DGKE has a wide range of applications in biomedical research. Some of the key applications include:

1. Study of Lipid Metabolism:
Recombinant Human DGKE is a valuable tool for studying the role of DAG and PA in lipid metabolism. It can be used to investigate the effects of DGKE on lipid signaling pathways and its potential role in diseases such as obesity and diabetes.

2. Drug Discovery:
The dysregulation of lipid signaling pathways has been linked to various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Recombinant Human DGKE can be used to screen for potential drugs that target these pathways and may have therapeutic potential.

3. Biomarker Discovery:
Recombinant Human DGKE has been found to be dysregulated in several diseases, including cancer and neurodegenerative disorders. Its expression levels can serve as a potential biomarker for disease diagnosis and prognosis.

4. Vaccine Development:
Recombinant Human DGKE has been identified as an antigen in several infectious diseases, including malaria and tuberculosis. Its use as a vaccine candidate has shown promising results in preclinical studies.

Conclusion:
Recombinant Human DGKE is a versatile protein with a crucial role in lipid metabolism and signaling pathways. Its recombinant form has enabled researchers to study its structure and function in detail, leading to a better understanding of its role in health and disease. With its wide range of applications, Recombinant Human DGKE continues to be a valuable tool in biomedical research.

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