HEP-1

Product Details - HEP-1

HEP-1 is a synthetic peptide derived from a fragment of the ezrin protein (residues 324–337). It consists of 14 amino acids linked by peptide bonds and is utilized in controlled laboratory environments for peptide-based research applications.

In experimental settings, HEP-1 is examined for its interaction with cellular components and signaling systems. Its defined structure supports consistent investigation into peptide-receptor interactions and intracellular regulatory pathways.

This compound is supplied strictly for laboratory research purposes and is not intended for consumption, medical, or diagnostic use.

Mechanism of Action

At the molecular level, HEP-1 is studied for its interaction with cell surface receptors associated with immune-related signaling pathways. Upon binding, it is analyzed for its role in initiating intracellular signaling cascades involving regulatory proteins and transcriptional activity.

These signaling processes are evaluated in vitro to assess how peptide-receptor interactions influence cellular communication networks. Researchers examine pathways associated with cytokine signaling, receptor activation, and intracellular modulation.

Additionally, HEP-1 is investigated for its involvement in pathways related to inflammatory signaling, including the modulation of pro-inflammatory mediators and downstream transcriptional responses under controlled experimental conditions.

Chemical Properties of HEP-1

Attribute	Details
Compound Name	HEP-1 Peptide
Classification	Synthetic peptide (ezrin-derived fragment)
Molecular Formula	C74H132N26O27
Molecular Weight	1818 g/mol
CAS Number	174641-44-2
Synonyms	Human ezrin peptide (324–337); Ezrin peptide 1
Primary Target	Cell surface receptors and intracellular signaling pathways
Research Context	Peptide signaling and receptor interaction studies
Format	Research peptide (non-consumable)
Stability	Maintained under controlled laboratory storage conditions

Research Applications

Receptor Interaction Studies

HEP-1 is utilized in experimental systems to examine peptide binding to cell surface receptors. Researchers analyze ligand affinity, receptor activation, and signal initiation at the molecular level.

Intracellular Signaling Analysis

This compound is applied in studies investigating signaling pathways associated with cytokine activity and transcriptional regulation. These analyses focus on intracellular communication and pathway modulation.

Inflammatory Pathway Research

HEP-1 supports investigations into signaling networks associated with inflammatory mediators. Researchers evaluate how peptide interactions influence regulatory pathways under controlled laboratory conditions.

Why Choose BehemothLabz to Buy HEP-1 for Research

BehemothLabz supplies research-grade HEP-1 produced under controlled laboratory conditions with strict quality assurance protocols in place. Each batch undergoes detailed analytical verification to ensure consistency in molecular composition and purity.

In addition, comprehensive documentation, including laboratory testing reports and sourcing transparency, supports reproducibility across experimental applications. BehemothLabz maintains a compliance-focused approach, ensuring that all compounds are supplied exclusively for laboratory-based investigation and analytical research.

Disclaimer

HEP-1 is intended strictly for laboratory research and analytical purposes only. It is not designed for diagnostic procedures, therapeutic applications, or any form of in vivo study.

All references to biochemical pathways, receptor interactions, and enzymatic processes are provided solely within a research context. This compound must be handled only by qualified professionals within controlled laboratory environments, in accordance with applicable regulations and safety standards.

Any use outside of these defined research conditions is strictly prohibited.

References

• Lin, K. X., Wu, Z. Y., Qin, M. L., & Zeng, H. C. (2025). Bisphenol S Induces Lipid Metabolism Disorders in HepG2 and SK-Hep-1 Cells via Oxidative Stress. Toxics, 13(1), 44. https://doi.org/10.3390/toxics13010044
• Im, E., Yeo, C., Lee, H. J., & Lee, E. O. (2018). Dihydroartemisinin induced caspase-dependent apoptosis through inhibiting the specificity protein 1 pathway in hepatocellular carcinoma SK-Hep-1 cells. Life sciences, 192, 286–292. https://doi.org/10.1016/j.lfs.2017.11.008

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