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Brand: ProteoGenix

Recombinant Human RABGEF1 Protein, N-His

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

329.00

100ug + 329 loyalty points
Thr131–Lys368
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Recombinant Human RABGEF1 Protein, N-His

Recombinant Human RABGEF1 Protein, N-His

Product name Recombinant Human RABGEF1 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 30.14 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 Thr131-Lys368
Aliases /Synonyms RAP1, Rabex-5, RABEX5, Rab5 GDP/GTP exchange factor, RABGEF1, Rabaptin-5-associated exchange factor for Rab5
Reference ARO-P12042
Note For research use only.
Molecular Constructor
Thr131–Lys368

Introduction

Recombinant human RABGEF1 protein is a genetically engineered form of the human protein RABGEF1. It is produced in a laboratory using recombinant DNA technology, which involves inserting the gene for RABGEF1 into a host cell and allowing it to produce the protein. This process results in a highly pure and specific form of the protein, making it a valuable tool for scientific research and medical applications.

Structure

RABGEF1 is a protein that plays a crucial role in intracellular membrane trafficking. It is a member of the RAB guanine nucleotide exchange factor (GEF) family, which are proteins that regulate the activity of RAB GTPases. RABGEF1 is composed of 1,005 amino acids and has a molecular weight of approximately 114 kDa. It contains several functional domains, including a catalytic Sec7 domain, a pleckstrin homology (PH) domain, and a RAB-binding domain (RBD). These domains work together to facilitate the exchange of GDP for GTP on specific RAB proteins, thereby regulating their activity.

Activity

The primary function of RABGEF1 is to act as a guanine nucleotide exchange factor for RAB1, a protein involved in the transport of proteins and vesicles between the endoplasmic reticulum and the Golgi apparatus. RABGEF1 activates RAB1 by promoting the exchange of GDP for GTP, which causes a conformational change in RAB1 and allows it to bind to its effector proteins. This ultimately leads to the formation of transport vesicles that carry cargo from the endoplasmic reticulum to the Golgi apparatus.

In addition to its role in RAB1-mediated membrane trafficking, RABGEF1 has also been shown to interact with other RAB proteins, including RAB2, RAB3, and RAB6. These interactions suggest that RABGEF1 may play a broader role in regulating intracellular membrane trafficking and organization.

Application

Recombinant human RABGEF1 protein has a wide range of applications in both basic research and medical fields. In basic research, it is commonly used as a tool to study the molecular mechanisms of intracellular membrane trafficking. Its ability to activate specific RAB proteins allows researchers to manipulate and study the transport of proteins and vesicles within cells. This has led to a better understanding of various cellular processes, including protein secretion, endocytosis, and autophagy.

In the medical field, RABGEF1 has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. As such, recombinant RABGEF1 protein has the potential to be used as a therapeutic target or diagnostic marker for these conditions. Additionally, the ability to produce large quantities of pure RABGEF1 protein through recombinant technology has made it a valuable tool for drug discovery and development.

Conclusion

Recombinant human RABGEF1 protein is a crucial tool for studying intracellular membrane trafficking and its role in various diseases. Its highly specific and well-defined structure, as well as its ability to activate specific RAB proteins, make it a valuable tool for both basic research and medical applications. With ongoing advancements in recombinant technology, the potential for RABGEF1 to further our understanding of cellular processes and contribute to the development of new treatments for diseases is immense.

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