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Updated: Apr 7, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Human coagulation factor VIII domain-specific recombinant polypeptide expression.

Su Jin Choi¹, Ki Jung Jang¹, Jeong-A Lim²

¹Department of Biological Science, College of Natural Sciences, Ajou University, Suwon, Korea.

|July 10, 2015

Summary

This summary is machine-generated.

Researchers created domain-specific recombinant polypeptides to study coagulation factor VIII (FVIII) functions. The A2 polypeptide specifically interacted with coagulation factor IX, advancing understanding of FVIII

Keywords:

Coagulation factor IX Coagulation factor VIII Domain-specific recombinant FVIII Hemophilia A Hep3B hepatocytes

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Last Updated: Apr 7, 2026

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Published on: February 2, 2018

Area of Science:

Biochemistry
Molecular Biology
Hematology

Background:

Hemophilia A arises from diverse mutations in the F8 gene.
Coagulation factor VIII (FVIII), encoded by F8, has distinct functional domains (A1-A2-B-A3-C1-C2).
While FVIII interacts with various proteins crucial for hemostasis, its domain-specific functions and binding partners remain largely uncharacterized.

Purpose of the Study:

To investigate the domain-specific functions of coagulation factor VIII (FVIII) during blood coagulation.
To develop tools for studying FVIII's molecular interactions and functions.

Main Methods:

Cloning of FVIII domains (A1, A2, A3, C) from Hep3B hepatocytes.
Expression and purification of domain-specific recombinant polypeptides using glutathione S-transferase (GST) or polyhistidine (His) tags in bacteria.
Affinity chromatography for polypeptide purification.

Main Results:

Successfully obtained recombinant polypeptides corresponding to predicted sizes.
The glutathione S-transferase (GST)-tagged A2 polypeptide demonstrated interaction with coagulation factor IX.
This interaction validates the binding site for coagulation factor IX on the FVIII A2 domain.

Conclusions:

Domain-specific recombinant polypeptides are valuable tools for elucidating FVIII's role in coagulation.
These recombinant tools can aid in the development of domain-specific antibodies for therapeutic or diagnostic purposes.