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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human SRXN1 Protein, N-His-SUMO & C-Strep |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 24.23 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 | His42-Gln137 |
Aliases /Synonyms | Sulfiredoxin-1, SRXN1, C20orf139, SRX, SRX1 |
Reference | ARO-P12497 |
Note | For research use only. |
Title: Introduction to Recombinant Human SRXN1 Protein
Recombinant Human SRXN1 protein, also known as sulfiredoxin-1, is a highly conserved protein that plays a crucial role in regulating cellular redox balance. This protein is encoded by the SRXN1 gene and is found in a wide range of organisms, from bacteria to humans. In this article, we will discuss the structure, activity, and application of recombinant Human SRXN1 protein.
Title: Structure of Recombinant Human SRXN1 Protein
The recombinant Human SRXN1 protein is a small, 12 kDa protein that consists of 105 amino acids. It contains a conserved Cys-X-X-Cys motif, which is essential for its activity. The protein has a globular structure with a central beta-sheet surrounded by alpha-helices. This structure is highly similar to other members of the thioredoxin superfamily, indicating its functional similarity.
Title: Activity of Recombinant Human SRXN1 Protein
The main function of recombinant Human SRXN1 protein is to reduce oxidized cysteine residues in proteins, thereby maintaining their proper function. This is achieved through its thioredoxin-like activity, where it uses a conserved cysteine residue to reduce disulfide bonds in target proteins. This process is crucial for maintaining cellular redox balance and protecting cells from oxidative stress.
Title: Role of Recombinant Human SRXN1 Protein in Cellular Redox Regulation
Recombinant Human SRXN1 protein is involved in regulating the redox state of various cellular components, including proteins, lipids, and DNA. It plays a critical role in maintaining the redox balance of the cell by reducing oxidized proteins and preventing the accumulation of reactive oxygen species (ROS). This function is particularly important in cells that are exposed to high levels of oxidative stress, such as neurons and immune cells.
Title: Applications of Recombinant Human SRXN1 Protein
The unique properties of recombinant Human SRXN1 protein make it a valuable tool in various scientific and medical applications. One of its main applications is in studying the mechanisms of redox regulation in cells. By studying the activity and function of this protein, researchers can gain a better understanding of how cells maintain their redox balance and respond to oxidative stress.
Another important application of recombinant Human SRXN1 protein is in the development of therapeutics for diseases related to oxidative stress. Studies have shown that this protein is involved in protecting cells from damage caused by ROS, making it a potential target for the treatment of diseases such as cancer, neurodegenerative disorders, and cardiovascular diseases.
Title: Production of Recombinant Human SRXN1 Protein
Recombinant Human SRXN1 protein can be produced using various expression systems, including bacteria, yeast, and mammalian cells. The most commonly used system is Escherichia coli, which allows for the production of large quantities of the protein at a relatively low cost. The recombinant protein can then be purified using various techniques, such as affinity chromatography, to obtain a highly pure and active form of the protein.
Title: Conclusion
In conclusion, recombinant Human SRXN1 protein is a crucial player in maintaining cellular redox balance and protecting cells from oxidative stress. Its unique structure and activity make it a valuable tool for studying redox regulation and developing therapeutics for diseases related to oxidative stress. With the advancements in protein production and purification techniques, this protein holds great potential for future research and applications in the field of redox biology.
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