Recombinant Human DIRAS1 Protein, N-His

Reference: YHB52101
Product nameRecombinant Human DIRAS1 Protein, N-His
Origin speciesHuman
Expression systemProkaryotic expression
Molecular weight21.44 kDa
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 TypeMet1-Arg171
Aliases /SynonymsDistinct subgroup of the Ras family member 1, RIG, GBTS1, Rig, DIRAS1, GTP-binding protein Di-Ras1, Small GTP-binding tumor suppressor 1, Ras-related inhibitor of cell growth
ReferenceYHB52101
NoteFor research use only.

Description of Recombinant Human DIRAS1 Protein, N-His

Introduction

The Recombinant Human DIRAS1 Protein is a highly purified and biologically active protein that has been produced through recombinant DNA technology. This protein is a member of the Ras family of small GTPases and plays an important role in various cellular processes such as cell growth, differentiation, and apoptosis. In this article, we will discuss the structure, activity, and applications of this protein in detail.

Structure of Recombinant Human DIRAS1 Protein

The Recombinant Human DIRAS1 Protein is a 26 kDa protein consisting of 233 amino acids. It has a conserved GTP-binding domain and a C-terminal CAAX motif, which is important for membrane association. The protein also contains a polybasic region that is involved in protein-protein interactions. The crystal structure of DIRAS1 has been determined, revealing the presence of a unique loop structure in the GTP-binding domain that distinguishes it from other members of the Ras family.

Activity of Recombinant Human DIRAS1 Protein

The main activity of Recombinant Human DIRAS1 Protein is its role as a small GTPase. Like other members of the Ras family, DIRAS1 can switch between an inactive GDP-bound state and an active GTP-bound state. In its active state, DIRAS1 interacts with various effector molecules to regulate downstream signaling pathways. It has been shown to activate the PI3K/Akt pathway, which is involved in cell survival and proliferation. DIRAS1 also regulates the activity of the MAPK pathway, which is important for cell growth and differentiation.

In addition to its role as a signaling molecule, Recombinant Human DIRAS1 Protein has been shown to have a role in membrane trafficking. It has been found to interact with proteins involved in endocytosis and exocytosis, suggesting its involvement in the transport of cellular components.

Applications of Recombinant Human DIRAS1 Protein

The unique structure and activity of Recombinant Human DIRAS1 Protein make it a valuable tool for various research applications. One of its main applications is in the study of Ras signaling pathways. As a member of the Ras family, DIRAS1 can provide insights into the mechanisms of Ras-mediated signaling and its role in cellular processes.

Recombinant Human DIRAS1 Protein has also been used in cancer research. Its involvement in the PI3K/Akt and MAPK pathways makes it a potential target for cancer therapy. In addition, DIRAS1 has been found to be overexpressed in certain types of cancers, making it a potential biomarker for disease diagnosis and prognosis.

Furthermore, Recombinant Human DIRAS1 Protein has been used in drug discovery and development. Its role in membrane trafficking and cellular transport makes it a potential target for the development of drugs that can modulate these processes. In addition, DIRAS1 has been found to interact with proteins involved in viral infection, making it a potential target for antiviral drugs.

Conclusion

The Recombinant Human DIRAS1 Protein is a biologically active protein that plays important roles in cellular processes such as signaling and membrane trafficking. Its unique structure and activity make it a valuable tool for research in various fields, including cancer, drug discovery, and viral infection. Further studies on this protein may provide insights into its potential as a therapeutic target for various diseases.

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