RPL31 Human

Ribosomal Protein L31 Human Recombinant
Cat. No.
BT16312
Source
Escherichia Coli.
Synonyms
Ribosomal Protein L31, 60S Ribosomal Protein L31, L31, MMRPS32, MRPL42.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's 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.
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Description

RPL31 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 148 amino acids (1-125 a.a) and having a molecular mass of 16.9kDa.RPL31 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Ribosomes play a crucial role in protein synthesis, acting as catalysts for the process. They consist of two subunits, one small and one large, each composed of over 80 distinct ribosomal proteins. RPL31, belonging to the L31E ribosomal protein family, is a vital component of the larger 60S subunit and resides within the cytoplasm. Notably, elevated levels of RPL31 expression have been observed in individuals with familial adenomatous polyps. As is characteristic of genes encoding ribosomal proteins, multiple processed pseudogenes of RPL31 are dispersed throughout the genome.
Description
Recombinant human RPL31, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein encompasses 148 amino acids (specifically, residues 1 to 125) and exhibits a molecular weight of 16.9 kDa. For purification purposes, a 23-amino acid His-tag is fused to the N-terminus, and the protein is subsequently purified using proprietary chromatographic methods.
Physical Appearance
A clear solution that has undergone sterile filtration.
Formulation
The RPL31 protein solution is provided at a concentration of 0.25 mg/ml. It is formulated in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, 1 mM DTT, and 50% glycerol.
Stability
For optimal storage, the protein solution should be kept at 4°C if the entire vial will be used within 2-4 weeks. If longer storage is required, it should be stored frozen at -20°C. To ensure long-term stability during storage, the addition of a carrier protein, such as HSA or BSA, at a concentration of 0.1% is recommended. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the protein is determined by SDS-PAGE analysis and is consistently greater than 85.0%.
Synonyms
Ribosomal Protein L31, 60S Ribosomal Protein L31, L31, MMRPS32, MRPL42.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPAKKG GEKKKGRSAI NEVVTREYTI NIHKRIHGVG FKKRAPRALK EIRKFAMKEM GTPDVRIDTR LNKAVWAKGI RNVPYRIRVR LSRKRNEDED SPNKLYTLVT YVPVTTFKNL QTVNVDEN

Product Science Overview

Introduction

Ribosomal Protein L31 (RPL31) is a crucial component of the ribosome, the cellular machinery responsible for protein synthesis. Specifically, RPL31 is part of the large 60S subunit of the ribosome. The ribosome itself is composed of two subunits: the small 40S subunit and the large 60S subunit. Together, these subunits are made up of four RNA species and approximately 80 structurally distinct proteins .

Structure and Function

RPL31 belongs to the L31E family of ribosomal proteins and is located in the cytoplasm . The protein plays a vital role in the assembly and function of the ribosome, contributing to the translation of mRNA into proteins. This process is fundamental to cellular function and growth.

Expression and Clinical Relevance

Higher levels of RPL31 expression have been observed in familial adenomatous polyps compared to matched normal tissues . This suggests a potential role in the development or progression of certain types of cancer. As with many ribosomal proteins, there are multiple processed pseudogenes of RPL31 dispersed throughout the genome .

Recombinant Production

Recombinant Human RPL31 is typically produced using bacterial expression systems, such as Escherichia coli (E. coli). The recombinant protein is often fused with a His-tag at the N-terminus to facilitate purification. The protein is then purified using conventional chromatography techniques .

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