SARS Human
Description
SARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Seryl-tRNA synthetase (SerRS) is an essential enzyme in the aminoacyl-tRNA synthetase (aaRS) family, responsible for catalyzing the attachment of serine to its corresponding tRNA (tRNA^Ser). This process is crucial for the accurate translation of the genetic code into proteins. The human recombinant form of SerRS has been extensively studied for its role in various cellular processes and its potential therapeutic applications.
SerRS is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit contains an active site where the aminoacylation reaction occurs. The enzyme recognizes the anticodon loop of tRNA^Ser and catalyzes the esterification of serine to the 3’-end of the tRNA. This charged tRNA^Ser is then used by the ribosome during protein synthesis.
In addition to its canonical role in translation, human SerRS has been found to interact with various proteins and participate in non-translational functions. For example, SerRS can bind to the VEGFA promoter and act as a negative regulator of VEGFA gene expression, which is important for vascular development and angiogenesis .
The recombinant production of human SerRS involves cloning the gene encoding SerRS into an expression vector, which is then introduced into a suitable host organism, such as Escherichia coli. The host cells are cultured, and the recombinant protein is expressed and purified using techniques such as affinity chromatography. This recombinant form of SerRS is used in various biochemical and structural studies to understand its function and interactions.
Human SerRS plays a critical role in maintaining the fidelity of protein synthesis. By ensuring the correct attachment of serine to tRNA^Ser, SerRS helps prevent errors in translation that could lead to the production of dysfunctional proteins. Additionally, the enzyme’s involvement in non-translational processes, such as the regulation of VEGFA expression, highlights its importance in cellular homeostasis and disease.
Recent studies have explored the therapeutic potential of targeting SerRS for the treatment of diseases caused by nonsense mutations. Nonsense mutations introduce premature stop codons in mRNA, leading to truncated and non-functional proteins. SerRS has been shown to promote translational readthrough of these premature stop codons, allowing the synthesis of full-length, functional proteins . This property of SerRS could be harnessed to develop therapies for genetic disorders caused by nonsense mutations.
