Versican G1 Domain (human, recombinant)

Versican is a secreted proteoglycan and member of the hyalectan family of proteoglycans.^1,2 It is composed of an N-terminal G1 domain containing a secretory signal peptide, an immunoglobulin-like motif, and two proteoglycan tandem repeats followed by two glycosaminoglycan (GAG) binding regions, α-GAG and β-GAG, and a C-terminal G3 domain containing two EGF-like repeats, a carbohydrate recognition domain, and a complement-binding protein-like motif.^2,3 Alternative splicing of versican produces four isoforms (V0-V3) that are expressed in a tissue- and development-specific manner and differ based on the GAG-binding region, containing either α- and β-GAG (V0), β-GAG only (V1), α-GAG only (V2), or no GAG-binding regions (V3).² Versican is expressed in a variety of tissues, including connective tissue, cartilage, neural tissues, and vessels.^4,5 It interacts with a variety of ligands, including hyaluronan at the G1 domain and fibulin-1 and -2 at the G3 domain.³ It is involved in tissue and organ development, including cardiac development, and is a structural macromolecule of the extracellular matrix (ECM) in various tissues in adulthood.^3,5,6 Versican levels are increased in tumor tissue or peritumoral stromal cells in a wide range of cancers and are associated with poor outcomes.⁷ Mutations in VCAN, the gene encoding versican, are the cause of Wagner syndrome, a hereditary vitreoretinopathy characterized by early-onset syneresis and accelerated liquefaction of the vitreous.⁸ Cayman's Versican G1 Domain (human, recombinant) protein can be used for binding assay, ELISA, and Western blot (WB) applications.

WARNING This product is not for human or veterinary use.

1. Zimmerman, D.R., and Ruoslahti, E. Multiple domains of the large fibroblast proteoglycan, versican. EMBO J. 8(10), 2975-2981 (1989).

2. Wu, Y.J., La Pierre, D.P., Wu, J., et al. The interaction of versican with its binding partners. Cell Res. 15(7), 483-494 (2005).

3. Wight, T.N., Day, A.J., Kang, I., et al. V3: An enigmatic isoform of the proteoglycan versican. Am. J. Physiol. Cell Physiol. 325(2), C519-C537 (2023).

4. Bode-Lesniewska, B., Dours-Zimmermann, M.T., Odermatt, B.F., et al. Distribution of the large aggregating proteoglycan versican in adult human tissues. J. Histochem. Cytochem. 44(4), 303-312 (1996).

5. Islam, S., and Watanabe, H. Versican: A dynamic regulator of the extracellular matrix. J. Histochem. Cytochem. 68(11), 763-775 (2020).

6. Watanabe, H. Versican and versikine: The dynamism of the extracellular matrix. Proteoglycan Res. 1(4), e13 (2023).

7. Ricciardelli, C., Sakko, A.J., Ween, M.P., et al. The biological role and regulation of versican levels in cancer. Cancer Metastasis Rev. 28(1-2), 233-245 (2009).

8. Ghoraba, H.H., Sears, J., and Traboulsi, E.I. Hereditary vitreoretinopathies: Molecular diagnosis, clinical presentation and management. Clin. Exp. Ophthalmol. 53(3), 281-291 (2025).