NOP16 Human

NOP16 Human Recombinant
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Description

Molecular Characterization of NOP16 Human

NOP16 (Nucleolar Protein 16 Homolog) is a 178-amino-acid protein encoded by the NOP16 gene (Gene ID: 51491) on chromosome 5q35.2. Recombinant variants, such as His-tagged NOP16 (e.g., Cat.No. NOP16-7099H), are produced in E. coli and purified via chromatography .

PropertySpecification
Molecular Mass23.6 kDa (201aa) / 40.0 kDa (366aa)
Amino Acid SequenceIncludes His-tag at N-terminus; residues 1-178 with conserved lysine motifs
Expression SystemEscherichia coli
Purity>85% (SDS-PAGE)
Storage-20°C or -70°C in glycerol-containing buffer

The protein contains methylated lysine residues (K29, K106, K107) critical for binding epigenetic regulators like PRC2 (Polycomb Repressive Complex 2) and JMJD3 (a histone demethylase) .

Biological Functions and Mechanisms

NOP16 regulates histone H3K27 methylation by acting as a histone mimetic:

  • Epigenetic Modulation:

    • Competes with histone H3 for binding to PRC2 (via EED subunit) and JMJD3, altering H3K27me3 levels .

    • Overexpression reduces global H3K27me3, promoting oncogenic gene expression .

  • Cell Cycle Regulation:

    • Depletion suppresses G1→S transition by upregulating H3K27me3 at E2F transcription factor targets (e.g., CCNE1, CDC6) .

    • Knockdown arrests cells in G2/M phase and inhibits DNA replication .

Breast Cancer

  • Upregulation: Driven by c-Myc transcription and estrogen signaling .

  • Prognostic Marker: Overexpression correlates with poor survival (HR = 1.76, p = 0.015) .

  • In Vivo Impact: NOP16 knockout in MDA-MB231 xenografts reduces tumor growth by 60% (p < 0.01) .

Hepatocellular Carcinoma (LIHC)

  • Pathogenic Role:

    • Activates Keap1-Nrf2 signaling, increasing antioxidant genes (e.g., NQO1, HO-1) and promoting EMT .

    • High expression linked to advanced tumor stage (T3/T4: HR = 2.95, p = 0.001) .

Cancer TypeKey Associations
Breastc-Myc dependency; H3K27me3 dysregulation; poor survival
Liver (LIHC)Keap1-Nrf2 pathway activation; T-lymphocyte infiltration imbalance

Key Studies

  1. bioRxiv (2023):

    • NOP16 knockout increases H3K27me3, repressing E2F targets (CCNE1, CDK2) and inhibiting proliferation in breast cancer cells .

    • In vitro knockdown reduces migration and invasiveness by 40-50% .

  2. Sage Journals (2024):

    • NOP16 silencing in HepG2 cells upregulates apoptosis markers (e.g., Caspase-3) and downregulates cyclins (e.g., Cyclin D1) .

Targeted Therapy Potential

  • EpCAM-AsiCs: NOP16-targeted siRNAs reduced tumor growth in triple-negative breast cancer models .

  • Combination Strategies: Inhibiting NOP16 with PRC2/JMJD3 modulators may amplify anti-tumor effects .

Product Specs

Introduction
NOP16, a protein regulated by c-Myc at the transcriptional level, shows increased expression in breast cancer and is associated with unfavorable prognosis in patients.
Description
Recombinantly produced in E. coli, the human NOP16 protein is a single polypeptide chain devoid of glycosylation. It comprises 201 amino acids, including a 23 amino acid His-tag attached to the N-terminus, and has a molecular weight of 23.6 kDa. The protein encompasses amino acids 1-178 of the NOP16 sequence. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The NOP16 protein is supplied in a solution with a concentration of 0.25 mg/ml. The solution is buffered at pH 8.0 with 20 mM Tris-HCl and contains additional components: 0.2 M NaCl, 50% glycerol, 2 mM EDTA, and 2 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the protein solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freezing and thawing of the protein solution should be avoided.
Purity
The purity of the NOP16 protein is determined by SDS-PAGE analysis and is found to be greater than 85%.
Synonyms
Nucleolar protein 16, HBV pre-S2 trans-regulated protein 3, NOP16, CGI-117, HSPC111, HSPC185.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKAKGK TRRQKFGYSV NRKRLNRNAR RKAAPRIECS HIRHAWDHAK SVRQNLAEMG LAVDPNRAVP LRKRKVKAME VDIEERPKEL VRKPYVLNDL EAEASLPEKK GNTLSRDLID YVRYMVENHG EDYKAMARDE KNYYQDTPKQ IRSKINVYKR FYPAEWQDFL DSLQKRKMEV E.

Product Science Overview

Gene and Protein Structure

The NOP16 gene is located on chromosome 5 in humans. It encodes a protein that is primarily localized in the nucleolus, a substructure within the nucleus responsible for ribosome production. The human recombinant NOP16 protein is typically expressed in E. coli and is a single, non-glycosylated polypeptide chain containing 201 amino acids, with a molecular weight of approximately 23.6 kDa . It is often fused to a His-tag at the N-terminus to facilitate purification.

Expression and Regulation

NOP16 expression is regulated by estrogens and the MYC protein . This regulation is significant because MYC is a well-known oncogene, and its overexpression is associated with various cancers, including breast cancer. High levels of NOP16 have been correlated with poor clinical outcomes in breast cancer patients, making it a potential biomarker for prognosis .

Functional Role

NOP16 plays a crucial role in ribosome biogenesis, which is essential for protein synthesis and cell growth. It is involved in the maturation of the 60S ribosomal subunit, a component of the ribosome. The protein’s expression is induced by estrogens and MYC, linking it to cell proliferation and cancer progression .

Clinical Significance

The clinical significance of NOP16 lies in its potential as a biomarker for cancer prognosis. Studies have shown that high expression levels of NOP16 are associated with aggressive tumor characteristics and poor survival rates in breast cancer patients . This makes NOP16 a valuable target for cancer research and potential therapeutic interventions.

Recombinant NOP16

Recombinant NOP16 is produced using recombinant DNA technology, which involves inserting the NOP16 gene into a suitable expression system, such as E. coli. The recombinant protein is then purified using various techniques, including affinity chromatography, which exploits the His-tag fused to the protein . This recombinant form is used in research to study the protein’s function, structure, and role in disease.

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