Cart (0 Items)
Your cart is currently empty.
View ProductsSize | 100ug |
---|---|
Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human SMS Protein, N-His |
---|---|
Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 43.43 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 | Met1-Pro366 |
Aliases /Synonyms | Spermine synthase, SPMSY, SMS, Spermidine aminopropyltransferase |
Reference | ARO-P11909 |
Note | For research use only. |
Recombinant Human SMS Protein is a protein that is produced through genetic engineering techniques, specifically through the process of recombinant DNA technology. This protein is a recombinant version of the human SMS (spermine synthase) protein, which is responsible for the production of the polyamine spermine in the body.
The recombinant version of this protein is produced in a laboratory setting using host cells, such as bacteria or yeast, that have been genetically modified to contain the gene for human SMS protein. This allows for the production of a large amount of pure and standardized recombinant protein for use in various applications.
The structure of recombinant Human SMS Protein is similar to that of the natural human protein, with a similar amino acid sequence and three-dimensional structure. This allows it to function similarly to the natural protein in the body.
The main activity of recombinant Human SMS Protein is the conversion of spermidine to spermine. Spermidine and spermine are polyamines that play important roles in various cellular processes, such as cell growth, proliferation, and differentiation. The production of spermine from spermidine is essential for maintaining proper cellular function and is regulated by the activity of SMS protein.
Recombinant Human SMS Protein is highly specific and efficient in its activity, as it is produced in a controlled environment and is free from any impurities or contaminants. This allows for precise and reliable results in various applications.
In addition to its main activity, recombinant Human SMS Protein also has secondary activities, such as binding to other proteins and regulating gene expression. These activities may have potential implications in various biological processes and can be further studied for potential therapeutic applications.
The recombinant version of Human SMS Protein has various applications in both research and clinical settings. One of its main applications is in the study of polyamine metabolism and its role in various diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases. By understanding the activity and regulation of SMS protein, researchers can gain insight into the underlying mechanisms of these diseases and potentially develop new treatments.
Recombinant Human SMS Protein is also used in drug discovery and development, as it can serve as a target for drug screening and as a tool for studying the effects of potential therapeutic compounds on polyamine metabolism. Furthermore, this protein can be used in the production of antibodies for diagnostic and therapeutic purposes, as it is an antigen that can elicit an immune response in the body.
In clinical practice, recombinant Human SMS Protein has potential applications in the treatment of diseases related to abnormal polyamine metabolism. For example, it can be used as a therapeutic agent to regulate the levels of spermine in the body, which may be beneficial in certain diseases where abnormal polyamine levels have been observed.
In summary, recombinant Human SMS Protein is a genetically engineered version of the human SMS protein with a similar structure and activity. It has various applications in research and clinical settings, particularly in the study of polyamine metabolism and its role in diseases. With its high specificity and efficiency, this protein is a valuable tool for further understanding the complex processes of the human body and for developing potential treatments for various diseases.
Send us a message from the form below
Reviews
There are no reviews yet.