RPLP2 Human
Description
RPLP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Ribosomal Phosphoprotein P2 (RPLP2) is a crucial component of the ribosome, specifically part of the large 60S subunit. This protein plays a significant role in the elongation step of protein synthesis, which is essential for cellular function and growth. The human recombinant form of RPLP2 is produced using recombinant DNA technology, typically in an E. coli expression system .
RPLP2 is a single, non-glycosylated polypeptide chain consisting of 139 amino acids, with a molecular mass of approximately 14.2 kDa . It belongs to the L12P family of ribosomal proteins and is functionally equivalent to the E. coli L7/L12 ribosomal protein . Unlike most ribosomal proteins, which are basic, RPLP2 is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P1 .
RPLP2 can interact with P0 and P1 to form a pentameric complex consisting of P1 and P2 dimers and a P0 monomer . This complex is vital for the ribosome’s function in protein synthesis.
The human recombinant RPLP2 is typically produced in E. coli. The process involves cloning the gene encoding RPLP2 into an expression vector, which is then introduced into E. coli cells. These cells are cultured under conditions that induce the expression of the recombinant protein. The protein is then purified using chromatographic techniques to achieve a high level of purity .
The recombinant RPLP2 produced in E. coli is fused to a 24 amino acid His-tag at the N-terminus, which facilitates its purification . The final product is a sterile, filtered, colorless solution containing the RPLP2 protein in a buffer solution .
RPLP2 is involved in the elongation step of protein synthesis, where it plays a role in the interaction between the ribosome and elongation factors. This interaction is crucial for the accurate and efficient synthesis of proteins. The acidic nature of RPLP2 and its ability to form complexes with other ribosomal proteins are essential for its function .
The analysis of RPLP2 typically involves techniques such as SDS-PAGE to determine its purity and molecular weight . Additionally, its interaction with other ribosomal proteins can be studied using various biochemical and biophysical methods.
