Recombinant Human SRXN1 Protein, N-His-SUMO & C-Strep

Reference: YHK39601
Product nameRecombinant Human SRXN1 Protein, N-His-SUMO & C-Strep
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight24.23 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
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)
Host speciesEscherichia coli (E.coli)
Fragment TypeHis42-Gln137
Aliases /SynonymsSulfiredoxin-1, SRXN1, C20orf139, SRX, SRX1
NoteFor research use only.

Description of Recombinant Human SRXN1 Protein, N-His-SUMO & C-Strep

Title: Understanding Recombinant Human SRXN1 Protein: Structure and Function

Recombinant proteins have revolutionized the field of biotechnology and have become an essential tool in various scientific research and industrial applications. One such recombinant protein is the Human SRXN1 protein, also known as sulfiredoxin-1. In this article, we will delve into the structure, activity, and applications of this important protein.

Structure of Recombinant Human SRXN1 Protein:
The SRXN1 gene encodes for a 159 amino acid protein with a molecular weight of approximately 18 kDa. The recombinant human SRXN1 protein is produced through genetic engineering techniques, where the gene is inserted into a suitable expression system, such as bacteria, yeast, or mammalian cells. The resulting protein contains an N-terminal His-tag for purification and is highly pure and biologically active.

The tertiary structure of the SRXN1 protein consists of a thioredoxin-like fold, with a conserved CXXC motif, which is essential for its enzymatic activity. It also contains a highly conserved active site cysteine residue, which is responsible for its redox activity. The protein exists as a dimer in its active form, with each monomer containing a single active site.

Activity of Recombinant Human SRXN1 Protein:
The primary function of SRXN1 is to maintain the redox balance in cells by reducing oxidized cysteine residues in proteins. This is achieved through its thioredoxin-like activity, where it uses reducing equivalents from NADPH to reduce oxidized cysteine residues in target proteins. This process is crucial for maintaining the proper folding and activity of various proteins, including enzymes and transcription factors.

Apart from its redox activity, SRXN1 also plays a role in regulating cell proliferation, apoptosis, and immune response. It has been shown to interact with several proteins involved in these processes, such as p53 and NF-κB, and modulate their activity through redox regulation.

Applications of Recombinant Human SRXN1 Protein:
The recombinant human SRXN1 protein has a wide range of applications in various fields of research and industry. Its redox activity and role in cellular processes make it an important tool in studying the mechanisms of oxidative stress and its impact on various diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases.

The protein is also used in drug discovery and development, where it can serve as a target for potential therapeutic agents. Its interaction with various proteins involved in cell proliferation and apoptosis makes it a potential target for cancer therapy. In addition, the redox activity of SRXN1 can also be exploited to develop antioxidant therapies for diseases associated with oxidative stress.

Furthermore, the recombinant human SRXN1 protein has industrial applications in the production of biopharmaceuticals. It can be used as a fusion partner to improve the solubility and stability of target proteins, thus facilitating their purification and production.

In conclusion, recombinant human SRXN1 protein is a valuable tool in scientific research and has diverse applications in various fields. Its well-defined structure and enzymatic activity make it an ideal protein for studying redox processes and their impact on cellular functions. With ongoing research and advancements in protein engineering, the potential of SRXN1 in various applications is yet to be fully explored.


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