ERH Antibodies

Background

ERH is a conserved small molecule protein, mainly existing in the nucleus of eukaryotes, and is involved in gene expression regulation and the cell cycle process. This protein plays a key role in the process of pre-mRNA splicing and transcriptional extension by interacting with mRNA splicing factors and transcriptional extension complexes, thereby influencing a variety of biological functions. Studies have found that ERH is abnormally expressed in various cancers and may be related to tumorigenesis and development. The ERH protein was initially identified for its function in Drosophila embryonic development. Its highly conserved three-dimensional structure consists of four β -folds and one α -helix. This simple and stable structure makes it an ideal model for studying protein-nucleic acid interactions. In recent years, scientists have analyzed the structural features of ERH through techniques such as X-ray crystallography and nuclear magnetic resonance, providing important clues for understanding its molecular mechanism in the gene expression regulatory network.

Structure Function Application Advantage Our Products

Structure of ERH

ERH is a relatively small nucleoprotein with a molecular weight of approximately 12-14 kDa, and there are subtle differences among different species:

Species	Human	Mice	Fruit flies	Yeast
Molecular Weight (kDa)	12.4	12.3	13.1	14.0
Primary Structural Differences	Highly conservative, containing typical ERH domains	Highly homologous to human ERH	Participate in the regulation of RNA splicing	Play an important role in transcription extension

ERH proteins are typically composed of 104 to 120 amino acids, forming a compact β -folded -α helical structure. Its tertiary structure is mainly composed of four β -folded lamellae and one C-terminal α -helix, forming a stable nucleic acid binding interface. This protein maintains structural stability through a conserved hydrophobic core and interacts with RNA or proteins by means of positively charged residues on its surface, participating in the regulation of gene expression. ERH is highly conserved in evolution, and its structural features enable it to flexibly participate in the assembly of various molecular complexes.

Fig. 1:Changes in the structure of ERH. (OA Literature) Fig. 1 Three-dimensional structure of ERH and its protein partner binding sites. ¹

Fig. 2 Diagrammatic summary of the ERH functions, including the proposed genome integrity maintenance.¹

Key structural properties of ERH:

Conservative β -folded -α helical structure
Hydrophobic core to maintain stability
Surface of positively charged molecules
Conservative dimerization interface
Flexible connection area

Functions of ERH

The main function of ERH protein is to participate in the regulation of gene expression and play a key role in various cellular processes:

Function	Description
Regulation of pre-mRNA splicing	By interacting with splicing factors, it regulates the alternative splicing process of mRNA.
Regulation of transcriptional extension	As a component of the transcriptional extension complex, it affects the progression of RNA polymerase II.
Cell cycle regulation	By regulating the expression of key genes, it affects the activation of cell cycle checkpoints.
DNA damage response	Participate in DNA damage repair pathways and maintain genomic stability.
Cancer-related functions	Abnormal expression in various tumors may affect the transcriptional regulation of oncogenes.

ERH participates in the regulatory network in a dose-dependent manner through its conserved protein-protein interaction interface (unlike the synergistic effect of hemoglobin/myoglobin), a characteristic that makes it a key molecule for the precise regulation of gene expression.

Applications of ERH and ERH Antibody in Literature

1. Kozlowski, Piotr. "Thirty years with ERH: an mRNA splicing and mitosis factor only or rather a novel genome integrity protector?." Cells 12.20 (2023): 2449. https://doi.org/10.3390/cells12202449

The article indicates that ERH is a highly conserved nucleoprotein that forms a homodimer scaffold, participates in the metabolism of RNA Pol II transcripts (mRNA and ncRNA processing) and heterochromatin silencing, and maintains genomic stability through interaction with species-specific proteins (such as Schizoyeast Mmi1, human DGCR8, etc.).

2. Xie, Guodong, et al. "A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing." Nature communications 10.1 (2019): 251.https://doi.org/10.1038/s41467-018-08273-9

The article indicates that Erh1 (human ERH homolog) in Schizoyeast forms a 2:2 complex (EMC) with Mmi1, and its eutectic structure reveals a conserved binding interface. The Mmi1Trp112 mutation disrupts heterochromatin assembly and gene silencing, but does not affect transcriptional termination, revealing a key interface for the interaction between ERH and RNA-binding proteins.

3. Banko, Monika I., et al. "Identification of amino acid residues of ERH required for its recruitment to nuclear speckles and replication foci in HeLa cells." PLoS One 8.8 (2013): e74885.https://doi.org/10.1371/journal.pone.0074885

The article indicates that ERH, as a unique small nucleoprotein, forms homodimers through the β -sheet surface. It interacts with PDIP46/SKAR to locate nuclear plaques (monomer form is required), and interacts with Ciz1 to locate replication foci (either monomer or dimer is acceptable). The key mutants (H3A Q9A/E37A T51A) reveal the separation of their localization mechanisms, providing a tool for studying their nuclear functions.

4. Pang, Kun, et al. "The ERH gene regulates migration and invasion in 5637 and T24 bladder cancer cells." BMC cancer 19.1 (2019): 225. https://doi.org/10.1186/s12885-019-5423-9

Research has found that knocking down the ERH gene can significantly inhibit the migration and invasion ability of bladder cancer T24/5637 cells (in vitro experiments and nude mouse models). Mechanism studies have shown that ERH affects tumor metastasis by regulating MYC gene expression, suggesting that ERH may become a new therapeutic target for bladder urothelial carcinoma.

5. Krzyzanowski, Marek K., Ewa Kozlowska, and Piotr Kozlowski. "Identification and functional analysis of the erh1+ gene encoding enhancer of rudimentary homolog from the fission yeast Schizosaccharomyces pombe." PloS one 7.11 (2012): e49059. https://doi.org/10.1371/journal.pone.0049059

Research has found that all four species of the genus Schizomyces contain ERH homologous genes, and the nucleoprotein Erh1 encoded by them responds to nutritional stress and hypertonic stress. erh1 deficiency leads to abnormal cell morphology, G1 phase arrest and enhanced stress sensitivity, but human ERH can partially compensate for these functions, suggesting its role in environmental adaptation and cell cycle regulation.

Creative Biolabs: ERH Antibodies for Research

Creative Biolabs specializes in the production of high-quality ERH antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom ERH Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our ERH antibodies, custom preparations, or technical support, contact us at email.

Reference

Kozlowski, Piotr. "Thirty years with ERH: an mRNA splicing and mitosis factor only or rather a novel genome integrity protector?." Cells 12.20 (2023): 2449. https://doi.org/10.3390/cells12202449