RPL22 Human

Ribosomal Protein L22 Human Recombinant
Cat. No.
BT16005
Source
Escherichia Coli.
Synonyms

Ribosomal Protein L22, Epstein-Barr-Encoded RNA-Associated Protein, Epstein-Barr Virus Small RNA-Associated Protein, 60S Ribosomal Protein L22, EBER-Associated Protein, EAP, HBP15/L22.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 85% 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

RPL22 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (1-128) and having a molecular mass of 17.0kDa.
RPL22 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
RPL22, a cytoplasmic ribosomal protein belonging to the L22E family, is found within the 60S ribosomal subunit. This protein exhibits specific binding affinity for Epstein-Barr virus-encoded RNAs (EBERs) 1 and 2.
Description
Recombinant human RPL22, expressed in E.coli, is a single, non-glycosylated polypeptide chain consisting of 151 amino acids (residues 1-128). It has a molecular weight of 17.0 kDa. The protein is engineered with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The provided RPL22 solution (0.25 mg/ml) is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 1 mM DTT, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
Purity exceeds 85% as determined by SDS-PAGE analysis.
Synonyms

Ribosomal Protein L22, Epstein-Barr-Encoded RNA-Associated Protein, Epstein-Barr Virus Small RNA-Associated Protein, 60S Ribosomal Protein L22, EBER-Associated Protein, EAP, HBP15/L22.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPVKKL VVKGGKKKKQ VLKFTLDCTH PVEDGIMDAA NFEQFLQERI KVNGKAGNLG GGVVTIERSK SKITVTSEVP FSKRYLKYLT KKYLKKNNLR DWLRVVANSK ESYELRYFQI NQDEEEEEDE D.

Product Science Overview

Introduction

Ribosomal Protein L22 (RPL22) is a component of the large 60S subunit of the ribosome, which plays a crucial role in protein synthesis. Ribosomes are essential macromolecular machines within the cell, responsible for translating mRNA into functional proteins. RPL22 is one of the many ribosomal proteins that contribute to the structure and function of the ribosome.

Structure and Function

RPL22 is an external protein on the 60S ribosomal subunit that is incorporated into the ribosome at later stages of ribosome maturation . It has a highly conserved structure across different species, indicating its essential role in ribosome function. The protein is involved in the assembly and stability of the ribosome, ensuring accurate translation of genetic information.

Regulatory Role

Recent studies have suggested that ribosomal proteins, including RPL22, may have regulatory functions beyond their structural roles. For instance, RPL22 has been shown to control the composition of the ribosome by directly repressing the expression of its own paralog, RPL22-like1 (RPL22L1) . This regulation is achieved through binding to an internal hairpin structure in the mRNA of RPL22L1, thereby influencing its expression and incorporation into ribosomes.

Human Recombinant RPL22

Human recombinant RPL22 is produced using recombinant DNA technology, which involves inserting the gene encoding RPL22 into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the protein for research and therapeutic purposes. Recombinant RPL22 retains the same structure and function as the naturally occurring protein, making it a valuable tool for studying ribosome biology and potential therapeutic applications.

Clinical Significance

Mutations in ribosomal proteins, including RPL22, have been linked to various human diseases. These include developmental malformations, inherited bone marrow failure syndromes, and cancer . Understanding the role of RPL22 in ribosome function and its regulatory mechanisms can provide insights into the molecular basis of these diseases and potential therapeutic targets.

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