Recombinant Human MSRB3 Protein, N-His

Reference: YHN28501
Product nameRecombinant Human MSRB3 Protein, N-His
Origin speciesHuman
Expression systemEukaryotic expression
Molecular weight16.14 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 TypeGln47-Asp170
Aliases /SynonymsMSRB3, Methionine-R-sulfoxide reductase B3, MsrB3
ReferenceYHN28501
NoteFor research use only.

Description of Recombinant Human MSRB3 Protein, N-His

Introduction to Recombinant Human MSRB3 Protein

Recombinant Human MSRB3 Protein, also known as Methionine Sulfoxide Reductase B3, is a protein that plays a crucial role in protecting cells against oxidative stress and maintaining cellular homeostasis. It is a member of the methionine sulfoxide reductase (MSR) family, which are enzymes involved in the repair of oxidative damage to proteins.

Structure of Recombinant Human MSRB3 Protein

The human MSRB3 gene is located on chromosome 12 and encodes for a protein of 248 amino acids. The recombinant protein is produced through genetic engineering techniques, where the gene is inserted into a host cell, such as E. coli, and expressed to produce large quantities of the protein.

The crystal structure of Recombinant Human MSRB3 Protein has been determined, revealing a homodimeric structure with each monomer consisting of an N-terminal thioredoxin-like domain and a C-terminal helical domain. The active site, where the reduction of methionine sulfoxide occurs, is located at the interface of the two domains.

Activity of Recombinant Human MSRB3 Protein

Recombinant Human MSRB3 Protein has been shown to possess strong antioxidant activity, specifically in reducing methionine sulfoxide to methionine. This activity is essential in protecting proteins from oxidative damage, which can lead to structural changes and loss of function.

Studies have also demonstrated that Recombinant Human MSRB3 Protein is highly selective for the reduction of methionine sulfoxide in the R-form, which is the most abundant form of oxidized methionine in proteins. This selective activity is crucial in maintaining the proper function of proteins, as the D-form of methionine sulfoxide is not reversible and can lead to protein dysfunction.

Applications of Recombinant Human MSRB3 Protein

Due to its antioxidant activity, Recombinant Human MSRB3 Protein has potential applications in various fields, including medicine, food preservation, and cosmetics.

In medicine, the protein has been shown to protect against oxidative stress-induced cell death in various cell types, including neurons and cardiomyocytes. This is particularly relevant in neurodegenerative diseases and cardiovascular diseases, where oxidative stress plays a significant role in disease progression. Recombinant Human MSRB3 Protein could potentially be used as a therapeutic agent to prevent or treat these diseases.

In food preservation, the protein could be used as a natural antioxidant to prevent the oxidation of lipids and proteins in food products, extending their shelf life. This could be particularly useful in the preservation of meat and dairy products, which are prone to oxidative spoilage.

In the cosmetics industry, Recombinant Human MSRB3 Protein could be incorporated into skincare products to protect against oxidative damage to skin cells, helping to maintain the youthful appearance of the skin.

Conclusion

In summary, Recombinant Human MSRB3 Protein is a critical enzyme involved in protecting cells against oxidative stress. Its antioxidant activity and selectivity for reducing methionine sulfoxide make it a promising candidate for various applications in medicine, food preservation, and cosmetics. With further research and development, this protein has the potential to make a significant impact in these fields and improve human health and well-being.

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