ERH Human

Enhancer of Rudimentary Human Recombinant
Cat. No.
BT7150
Source
Escherichia Coli.
Synonyms
Enhancer of rudimentary homolog, ERH, DROER, FLJ27340.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

ERH 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 127 amino acids (1-104 a.a.) and having a molecular mass of 14.6kDa. The ERH is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Enhancer of rudimentary homolog (ERH) is a ubiquitously expressed transcriptional coregulator that plays a critical role in various cellular processes, including cell cycle regulation and pyrimidine biosynthesis. This highly conserved protein is found in numerous eukaryotic organisms. ERH possesses two casein kinase II phosphorylation sites, which are believed to influence its ability to form dimers.
Description
Recombinant human ERH protein, expressed in E. coli, is engineered with a 23 amino acid His tag at the N-terminus. This non-glycosylated polypeptide chain comprises 127 amino acids (residues 1-104 of the ERH sequence) and has a molecular weight of 14.6 kDa. Purification of ERH is achieved through proprietary chromatographic techniques, ensuring high purity.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
The ERH protein is supplied in a solution containing 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.1M NaCl, and 1mM DTT, at a concentration of 1 mg/ml.
Stability
For short-term storage (2-4 weeks), keep the ERH solution at 4°C. For extended storage, freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage to maintain protein stability. Avoid repeated freeze-thaw cycles.
Purity
The purity of ERH protein is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms
Enhancer of rudimentary homolog, ERH, DROER, FLJ27340.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMSHTILL VQPTKRPEGR TYADYESVNE CMEGVCKMYE EHLKRMNPNS PSITYDISQL FDFIDDLADL SCLVYRADTQ TYQPYNKDWI KEKIYVLLRR QAQQAGK.

Product Science Overview

Historical Background and Discovery

The ERH protein was initially discovered in the fruit fly, Drosophila melanogaster, where it was identified as an enhancer of the rudimentary gene involved in pyrimidine biosynthesis . The human homolog of this protein shares significant structural and functional similarities with its Drosophila counterpart, highlighting its evolutionary conservation .

Structure and Function

ERH is a small protein consisting of 104 amino acids . Despite its modest size, it plays a crucial role in various cellular processes. The protein has been implicated in:

  • Cell Cycle Regulation: ERH is involved in the progression of mitosis by promoting mitotic chromosome alignment .
  • RNA Splicing: It binds to the Sm complex and is required for the mRNA splicing of the mitotic motor protein CENP-E .
  • Transcriptional Regulation: ERH acts as a transcriptional coregulator, influencing the expression of various genes .
Role in Disease and Therapeutic Potential

Recent studies have highlighted the importance of ERH in cancer biology. Cancer cells driven by mutations in the KRAS oncogene are particularly sensitive to RNAi-mediated suppression of ERH function . Additionally, ERH expression is inversely correlated with survival in colorectal cancer patients whose tumors harbor KRAS mutations . These findings suggest that ERH could be a potential therapeutic target for certain types of cancer.

Recombinant ERH Protein

Recombinant ERH protein is produced using recombinant DNA technology, which involves inserting the human ERH gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and role in disease .

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