HELZ Antibodies

Structure of HELZ

HELZ2 (also known as HELZ) is a large-molecular-weight multifunctional protein with a molecular weight of approximately 330 kDa. The human HELZ2 protein is composed of 2875 amino acids, and its primary structure contains multiple characteristic functional domains. These structural differences collectively determine its complex functions.

The secondary structure of this protein is composed of multiple α helices and β sheets, forming a complex spatial configuration. The core region contains a typical DExH-box RNA helicase domain, which can hydrolyze ATP to unwind the RNA double strand; meanwhile, the densely arranged CCCH-type zinc finger domains at the N-terminus are responsible for specifically recognizing and binding to the target RNA molecules. The coordinated action of these two key domains in space enables it to precisely regulate the metabolism and processing of RNA.

Fig. 1 Schematic representation of the predicted human HELZ protein architecture.¹

Key structural properties of HELZ:

• Containing the conservative DExH-box RNA helicase core domain
• Contains a tandemly repeated CCCH-type zinc finger motif for RNA binding
• Having the RING finger domain, it may be involved in protein interactions
• The overall structure of multiple domain of complex spatial configuration, control RNA metabolism and gene expression

Functions of HELZ

The protein encoded by the HELZ gene (HELZ2) is a multifunctional RNA helicase. Its core function is to participate in RNA metabolism and transcriptional regulation of gene expression, playing a crucial role especially in embryonic development and cell differentiation.

Unlike the simple myoglobin, the function of the HELZ protein is highly dependent on its complex multi-domain structure, which enables it to integrate instructions from multiple signaling pathways, functioning like a "molecular command center" to precisely coordinate the complex biological processes at the RNA level.

Applications of HELZ and HELZ Antibody in Literature

1. Hanet, Aoife, et al. "HELZ directly interacts with CCR4–NOT and causes decay of bound mRNAs." Life science alliance 2.5 (2019). https://doi.org/10.26508/lsa.201900405

The article indicates that the eukaryotic SF1 helicase HELZ has been discovered to directly bind to the C-terminal domain of the CCR4-NOT deadenylation complex. It relies on this complex to mediate translation inhibition and mRNA degradation, and plays a role in the regulation of gene expression related to nervous system development.

2. Hasgall, Philippe A., et al. "The putative RNA helicase HELZ promotes cell proliferation, translation initiation and ribosomal protein S6 phosphorylation." PloS one 6.7 (2011): e22107. https://doi.org/10.1371/journal.pone.0022107

The research has found that although the HELZ protein contains degradation motifs similar to HIFα, its degradation is not regulated by oxygen. Overexpression of HELZ can activate overall protein translation, while downregulation of HELZ will inhibit translation initiation, lead to the disassembly of polyribosomes, and slow down cell proliferation.

3. Lu, Wei, et al. "FOLFOX treatment response prediction in metastatic or recurrent colorectal cancer patients via machine learning algorithms." Cancer Medicine 9.4 (2020): 1419-1429. https://doi.org/10.1002/cam4.2786

The study found that the HELZ gene was expressed at a lower level in colorectal cancer patients who were sensitive to FOLFOX chemotherapy. The machine learning model constructed based on differentially expressed genes can effectively predict chemotherapy sensitivity, and among them, the MLKL and CCDC124 genes are independent prognostic factors.

4. Falcone, Noemi, et al. "Identification of a De novo deletion by using A-CGH involving PLNAX2: An interesting candidate gene in psychomotor developmental delay." Medicina 58.4 (2022): 524. https://doi.org/10.3390/medicina58040524

The research found that by analyzing the genome of a child with delayed motor development, it was discovered that the child carried copy number variations involving multiple genes such as PLXNA2 and HELZ. These gene variations jointly affected the development of the nervous system and might be related to the patient's clinical manifestations.

5. Chen, Chi-Hua, et al. "Leveraging genome characteristics to improve gene discovery for putamen subcortical brain structure." Scientific reports 7.1 (2017): 15736. https://doi.org/10.1038/s41598-017-15705-x

The research found that by using the newly enhanced functional annotation analysis method, the researchers discovered 11 genetic loci in the genome-wide association study of the volume of the brain nucleus, including HELZ. This has enhanced the effectiveness in identifying genetic variations related to brain structure.

Creative Biolabs: HELZ Antibodies for Research

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

• Custom HELZ 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 HELZ antibodies, custom preparations, or technical support, contact us at email.