RPS16 Human

Ribosomal Protein S16 Human Recombinant
Cat. No.
BT17388
Source
Escherichia Coli.
Synonyms
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

RPS16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146) and having a molecular mass of 18.8kDa.
RPS16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ribosomes are essential cellular machinery responsible for protein synthesis. They consist of two subunits: a small 40S subunit and a large 60S subunit. These subunits are composed of four types of RNA and approximately 80 distinct proteins. RPS16, a ribosomal protein belonging to the S9P family, is a crucial component of the 40S subunit. It is located in the cytoplasm. Similar to other genes encoding ribosomal proteins, multiple processed pseudogenes of RPS16 are dispersed throughout the genome.
Description
This product consists of the human RPS16 protein recombinantly produced in E. coli. It is a single, non-glycosylated polypeptide chain with 169 amino acids (residues 1-146) and a molecular weight of 18.8 kDa. For purification and detection purposes, a 23 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
The product appears as a clear, sterile-filtered solution.
Formulation
The RPS16 protein is supplied in a solution at a concentration of 0.5 mg/ml. The solution is buffered with 20 mM Tris-HCl at pH 8.0 and contains 0.4 M urea and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance long-term stability, the addition of a carrier protein such as HSA or BSA (0.1%) is advisable. Repeated freezing and thawing of the product should be minimized.
Purity
Analysis by SDS-PAGE indicates that the purity of the RPS16 protein is greater than 90%.
Synonyms
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPSKGPL QSVQVFGRKK TATAVAHCKR GNGLIKVNGR PLEMIEPRTL QYKLLEPVLL LGKERFAGVD IRVRVKGGGH VAQIYAIRQS ISKALVAYYQ KYVDEASKKE IKDILIQYDR TLLVADPRRC ESKKFGGPGA RARYQKSYR

Product Science Overview

Introduction

Ribosomal Protein S16 (RPS16) is a crucial component of the 40S subunit of the eukaryotic ribosome. It belongs to the S9P family of ribosomal proteins and is encoded by the RPS16 gene. This protein plays a vital role in the process of translation, where it contributes to the assembly and function of the ribosome, facilitating the synthesis of proteins from mRNA templates .

Gene and Protein Structure

The RPS16 gene is located on chromosome 19 in humans and is characterized by multiple processed pseudogenes dispersed throughout the genome . The human recombinant RPS16 protein is typically produced in Escherichia coli (E. coli) and consists of a single, non-glycosylated polypeptide chain containing 169 amino acids, with a molecular mass of approximately 18.8 kDa . The recombinant protein often includes a His-tag at the N-terminus to facilitate purification .

Expression and Purification

The cDNA of human RPS16 is cloned into an expression vector, such as pET-15b, and expressed in E. coli cells . Large-scale production of the recombinant protein involves isolating highly purified protein from inclusion bodies. The refolding of the protein from these inclusion bodies is optimized to ensure proper structural stability . Techniques such as circular dichroism (CD) spectroscopy are used to analyze the secondary structure content of the refolded protein, revealing that approximately 21% of the amino acid sequence forms α-helices and 24% forms β-strands .

Functional and Structural Stability

RPS16 is essential for the proper functioning of the ribosome. Its stability is influenced by various factors, including pH and urea concentration. The protein is quickly denatured at pH values above 8.0, while increasing urea concentration causes a slow unfolding of the protein . These properties are crucial for understanding the conditions under which RPS16 can maintain its functional integrity.

Biological Significance

RPS16 is involved in several critical biological processes, including cell proliferation, immune response, and protein ubiquitination . It is expressed in various tissues, such as lymphoid tissue, bone marrow, testis, and skeletal muscle . The protein’s role in the ribosome makes it indispensable for the translation process, impacting overall cellular function and protein synthesis.

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