When Recombinant Mouse Glypican 6 Fc Chimera (Catalog #9429-GP) is immobilized at 3 μg/mL, 100 μL/well, Recombinant Human FGF basic 146 aa (Catalog # 233-FB) binds with an ED50 of 2.5‑15 ng/mL.
Recombinant Mouse Glypican 6 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Glypican 6 Fc Chimera is immobilized at 3 μg/mL, 100 μL/well, the concentration of Recombinant Human FGF basic 146 aa (Catalog # 233-FB) that produces 50% of the optimal binding response is 2.5-15 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse Glypican 6 protein
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
83 kDa (Asp24-Val513/mFc), 44 kDa (Ser355-Val513/mFc) and 38 kDa (Asp24-Arg354). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
84-98 kDa (Asp24-Val513/mFc), 53-68 kDa (Asp24-Val513/mFc) and 33-40 kDa (Asp24-Arg354)
Publications
Read Publication using 9429-GP in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Glypican 6 Fc Chimera Protein, CF
Glypican 6
glypican proteoglycan 6
glypican-6
GPC6
MGC126288
OMIMD1
Background
The Glypicans (Glypiated Proteoglycans) are a small multigene family of GPI-linked heparan sulfate (HS) proteoglycans that likely play a key role in embryonic morphogenesis (1, 2, 3, 4). There are currently six known mammalian Glypicans. They all share a common-sized protein core of 60-70 kDa, an N-terminus which likely forms a compact globular domain, 14 conserved cysteines that form multiple intrachain disulfide bonds, and a number of C-terminal N- and O-linked carbohydrate attachment sites. Based on exon organization and the location of O-linked glycosylation sites, at least two subfamilies of Glypicans are known, with one subfamily containing Glypicans 1, 2, 4 and 6, and another subfamily containing Glypicans 3 and 5 (3, 5). Mouse Glypican 6 (GPC-6) is synthesized as a 555 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 aa mature region and a 25 aa C-terminal prosegment (5, 6). There are four consecutive Ser-Gly repeats that serve as a heparin sulfate attachment site. GPC-6 is reported to be as large as 110 kDa in size. This translates into approximately 50 kDa of proteoglycan. Mouse to human, there is 96% aa identity over the entire GPC-6 molecule (5). Glypican proteins are located in the extracellular matrix of cells and are important for tissue organization, cell proliferation, adhesion, migration and differentiation when they interact with extracellular or cytoplasmic ligands (7, 8). Glypicans act as co-receptors to enhance the activity of heparin-binding factors such as fibroblast growth factors and Wnt. Due to their ability to affect growth factor-mediated signaling, glypicans are known to have both pro- and anti-tumorigenic effects. GPC-6 overexpression has been associated with metastatic breast cancer, gastric cancer, and is known to regulate cardiomyocyte growth through the ERK1/2 signalling pathway where up-regulation is known to play a role in heart failure (9-11).
Song, H.H. and J. Filmus (2002) Biochim. Biophys. Acta 1573:241.
Filmus, J. (2001) Glycobiology 11:19R.
De Cat, B. and G. David (2001) Semin. Cell Dev. Biol. 12:117.
Filmus, J. (2003) Glycoconj. J. 19:319.
Veugelers, M. et al. (1999) J. Biol. Chem. 274:26968.
Paine-Saunders, S. et al. (1999) Genomics 57:455.
Kirn-Safran, C. et al. (2009) Cell. Mol. Life Sci. 66:3421.
Syrokou, A. et al. (1999) Cell Prolif. 32:85.
Dinccelik-Aslan, M. et al. (2015) Mol. Clin. Oncol. 3:584.
Yiu, G.K. et al. (2011) Biochem. J. 440:157.
Melleby, A.O. et al. (2016) PLoS One. 11:e0165079.
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