What is RCHY1 Protein

      What is RCHY1 Protein?

      The RCHY1 (the RING finger and CHY zinc finger domain-containing protein 1), also known as Pirh-2, is a multifaceted protein encoded by the RCHY1 gene. This gene is situated on human chromosome 4q24, and the RCHY1 protein it encodes plays pivotal roles in various cellular processes. Structurally characterized by a Ring Finger domain and a CHY Zinc Finger domain, RCHY1 orchestrates intricate cellular processes. This protein's intricate structure lays the foundation for its multifaceted functions.

      Secondary sequence organization of the CHY-zinc-finger/RING-finger domain. (Jung, Y.S., et al. 2012)

      Figure 1. Secondary sequence organization of the CHY-zinc-finger/RING-finger domain. (Jung, Y.S., et al. 2012)

      The Function of RCHY1 Protein

      1. Ubiquitin Ligase Activity

      At the molecular level, RCHY1 operates as an E3 ubiquitin ligase, facilitating the transfer of ubiquitin molecules to specific target proteins. This ubiquitination marks proteins for degradation by the proteasome, a process vital for cellular homeostasis. An exemplary instance of this function is its interaction with the tumor suppressor protein p53.

      1. p53 Regulation

      RCHY1 engages in a complex interplay with p53, a key guardian of genomic integrity. By promoting ubiquitination and subsequent degradation of p53, RCHY1 regulates cellular responses to stress, DNA damage, and other signaling cues. This interaction underscores the protein's role in preventing the accumulation of excessive p53, finely tuning cellular stress responses.

      1. Cell Cycle Control

      The regulatory influence of RCHY1 extends to the cell cycle, where it modulates the stability of proteins governing cell division and proliferation. Through precise orchestration of these events, RCHY1 ensures normal cell growth and prevents uncontrolled proliferation, contributing to the maintenance of cellular integrity.

      RCHY1-Related Diseases

      1. Cancer

      The intricate involvement of RCHY1 in the regulation of p53 positions it at the forefront of cancer research. Dysregulation or mutations in the RCHY1 gene have been associated with various cancers, emphasizing its potential as a therapeutic target. By modulating RCHY1 activity, researchers aim to restore p53 function, triggering apoptosis and inhibiting tumor progression.

      1. Neurological Disorders

      Emerging research suggests a connection between RCHY1 and neurological disorders. As a participant in cellular processes crucial for neuronal function, RCHY1's implications in neurodegenerative diseases prompt further investigation. Unraveling its role in neurological contexts may unveil novel therapeutic strategies.

      RCHY1 Related Signaling Pathways

      1. p53 Signaling Pathway

      The nexus between RCHY1 and the p53 signaling pathway is paramount. By influencing p53 levels, RCHY1 plays a pivotal role in modulating cellular responses to stressors and maintaining genomic stability. This intricate signaling cascade highlights RCHY1 as a key orchestrator in the cellular stress response.

      1. NF-κB Signaling Pathway

      Beyond p53, RCHY1 intersects with the NF-κB signaling pathway, known for its involvement in inflammation, immunity, and cell survival. While the precise mechanisms remain under scrutiny, RCHY1's interaction with NF-κB components offers insights into immune responses and inflammatory processes.

      Applications of RCHY1 in Biomedical Research

      1. Cancer Therapeutics

      Exploiting RCHY1 as a potential target opens avenues for cancer therapeutics. The protein's regulation of p53 presents an innovative approach to cancer treatment. Modulating RCHY1 activity may offer a means to restore p53 function in cancer cells, inducing apoptosis and inhibiting tumorigenesis.

      1. Neurological Disorder Research

      Understanding RCHY1's implications in neurological disorders provides a springboard for research and therapeutic development. As RCHY1 influences processes crucial for neuronal function, exploring its role in neurodegenerative diseases may pave the way for novel interventions.

      1. Drug Development

      RCHY1's involvement in diverse cellular processes positions it as an attractive target for drug development. Small molecules or compounds that modulate RCHY1 activity hold promise for influencing cellular regulation beyond cancer and neurological disorders. The potential applications of such compounds in various disease contexts make RCHY1 a focal point in drug discovery efforts.

      From its ubiquitin ligase activity to its role in regulating pivotal signaling pathways, RCHY1's impact spans cellular regulation, disease etiology, and biomedical applications. As researchers unravel the complexities of RCHY1, the prospect of therapeutic interventions and drug development in cancer, neurological disorders, and beyond beckons on the horizon of scientific exploration.

      Recommended Products for RCHY1 Protein

      Cat.# Species Product name Source (Host) Tag
      RCHY1-233H Human Recombinant Human ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase, His-tagged E.coli His
      RCHY1-4559H Human Recombinant Human RCHY1 Protein, Myc/DDK-tagged, C13 and N15-labeled HEK293T Myc/DDK
      RCHY1-4646H Human Recombinant Human RCHY1 protein, GST-tagged E.coli GST
      RCHY1-234H Human Recombinant Human RCHY1 Protein, Myc/DDK-tagged HEK293T Myc/DDK
      RCHY1-14034M Mouse Recombinant Mouse RCHY1 Protein Mammalian Cell His
      Rchy1-5437M Mouse Recombinant Mouse Rchy1 Protein, Myc/DDK-tagged HEK293T Myc/DDK
      RCHY1-3833R Rhesus Macaque Recombinant Rhesus monkey RCHY1 Protein, His-tagged Mammalian Cell His
      RCHY1-3650R Rhesus Macaque Recombinant Rhesus Macaque RCHY1 Protein, His (Fc)-Avi-tagged HEK293 His (Fc)-Avi
      RCHY1-11879Z Zebrafish Recombinant Zebrafish RCHY1 Mammalian Cell His
      RCHY1-3643C Chicken Recombinant Chicken RCHY1 Mammalian Cell His

      Reference

      • Jung, Y.S., et al. Pirh2 RING-finger E3 ubiquitin ligase: its role in tumorigenesis and cancer therapy. FEBS Lett. 2012, 586(10): 1397-402.