GPN1 Human
Description
Introduction to GPN1 Human
GPN1 is a 44.3 kDa protein encoded by the GPN1 gene (chromosome 2) and belongs to the GPN-loop GTPase family. It contains a conserved Gly-Pro-Asn (GPN) motif essential for nucleotide binding and hydrolysis . Key features include:
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Structure: Recombinant human GPN1 produced in E. coli includes a 24-amino-acid His-tag for purification .
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Function: Facilitates RNAPII nuclear transport, links transcriptional regulators, and participates in DNA repair via interactions with XPA .
Core Activities
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RNAPII Nuclear Import:
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DNA Repair:
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Transcriptional Regulation:
Clinical Relevance in Cancer
GPN1 is upregulated in multiple cancers and linked to poor prognosis.
Cancer-Specific Expression and Prognosis
Key Findings:
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Immune Infiltration: High GPN1 correlates with increased cytotoxic T-cell markers and PD-1/PD-L1 expression .
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Drug Sensitivity: Responsiveness to 16 drugs, including refametinib and selumetinib, inversely linked to GPN1 levels .
Functional Pathways and Mechanisms
GPN1-enriched pathways highlight its role in RNA and DNA metabolism:
| Pathway/Process | Biological Role | Source |
|---|---|---|
| RNA Localization | Regulates mRNA export and splicing | |
| Spliceosome | Modulates pre-mRNA processing | |
| DNA Replication | Supports transcriptional elongation |
Experimental Validation:
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Knockdown in HCC cells reduces migration via wound healing and transwell assays .
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Nomogram models predict 1/3/5-year survival in HCC patients using GPN1 expression .
Diagnostic and Therapeutic Potential
Product Specs
Product Science Overview
GPN-loop GTPase 1 (GPN1) is a member of the GPN-loop GTPase family. This family of proteins is characterized by the presence of a conserved GPN-loop motif, which is essential for their function as guanosine triphosphatases (GTPases). GTPases are enzymes that hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP), playing crucial roles in various cellular processes.
GPN1 is a guanosine triphosphatase enzyme that consists of 398 amino acids and has a molecular mass of approximately 44.3 kDa . The recombinant form of GPN1 is typically produced in Escherichia coli (E. coli) and is purified using proprietary chromatographic techniques. The protein is often fused to a 24 amino acid His-tag at the N-terminus to facilitate purification .
GPN1 plays a significant role in DNA repair and transcription activation. It is involved in the nucleocytoplasmic transport of both proteins and RNA, acting as a molecular switch that regulates these processes . One of the key functions of GPN1 is to establish an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, which is essential for the proper assembly and nuclear import of RNA polymerase II . Additionally, GPN1 may be involved in the nuclear localization of the XPA protein, which is crucial for nucleotide excision repair .
Mutations or dysregulation of GPN1 have been associated with various diseases. For instance, GPN1 has been linked to Plasmodium malariae malaria and multiple types of cataracts . Understanding the function and regulation of GPN1 can provide insights into the molecular mechanisms underlying these conditions and potentially lead to the development of targeted therapies.
The recombinant form of GPN1 is produced in E. coli and is available for laboratory research purposes. It is used in various biochemical and molecular biology studies to investigate the protein’s function, interactions, and role in cellular processes . The recombinant protein is typically stored at 4°C for short-term use or frozen at -20°C for long-term storage, with the addition of carrier proteins to prevent degradation .
