RPS14 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-151 a.a.) and having a molecular mass of 18.7kDa. The RPS14 is purified by proprietary chromatographic techniques.
MGSSHHHHHH SSGLVPRGSH MGSMAPRKGK EKKEEQVISL GPQVAEGENV FGVCHIFASF NDTFVHVTDL SGKETICRVT GGMKVKADRD ESSPYAAMLA AQDVAQRCKE LGITALHIKL RATGGNRTKT PGPGAQSALR ALARSGMKIG RIEDVTPIPS DSTRRKGGRR GRRL.
Ribosomal Protein S14 (RPS14) is a crucial component of the small 40S subunit of the ribosome, which plays a vital role in the synthesis of proteins within cells. The human recombinant form of RPS14 is produced using recombinant DNA technology, typically in Escherichia coli (E. coli) expression systems. This article delves into the background, structure, function, and significance of RPS14.
RPS14 is a single, non-glycosylated polypeptide chain consisting of 174 amino acids, with a molecular mass of approximately 18.7 kDa . The recombinant form of RPS14 is often fused with a 23 amino acid His tag at the N-terminus to facilitate purification. The production process involves expressing the RPS14 gene in E. coli, followed by purification using proprietary chromatographic techniques .
RPS14 is a structural constituent of the ribosome and is involved in the assembly and function of the small ribosomal subunit. It plays a critical role in the translation of mRNA into proteins by facilitating the binding of tRNA and the formation of peptide bonds. RPS14 is also part of the small subunit (SSU) processome, which is essential for the biogenesis of the small ribosomal subunit .
The proper functioning of RPS14 is essential for cellular protein synthesis. Mutations or deficiencies in RPS14 can lead to various diseases, including Chromosome 5q Deletion Syndrome and Deficiency Anemia . Additionally, RPS14 has been implicated in resistance to emetine, a protein synthesis inhibitor, in Chinese hamster ovary cells .
Human recombinant RPS14 is widely used in laboratory research to study ribosome function, protein synthesis, and related cellular processes. It is also utilized in the development of therapeutic interventions for diseases associated with ribosomal protein dysfunction.