Recombinant Human Glypican 3 Protein Best Seller
R&D Systems, part of Bio-Techne | Catalog # 2119-GP
Key Product Details
Source
NS0
Accession #
Structure / Form
Glypican 3 is subject to endoproteolytic processing by proprotein convertases (PC). By amino acid sequencing, three peptides (the first with a blocked N-terminus most likely starts with Gln25, the second peptide starts with Ser359 after a furin cleavage site, and the third peptide starts with Val483) are present in the recombinant GPC3 preparation. Peptides 2 and 3 are detected at a 1:1 ratio. All three peptides remained associated via disulfide bonds.
Conjugate
Unconjugated
Applications
Binding Activity
Product Specifications
Source
Mouse myeloma cell line, NS0-derived human Glypican 3 protein
Gln25-His559 with a C-terminal 6-His tag
Gln25-His559 with a C-terminal 6-His tag
Purity
>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
No results obtained: Gln25 predicted, Ser359 & Val483
Predicted Molecular Mass
61.6 kDa
SDS-PAGE
60-100 kDa, non-reducing conditions
Activity
Measured by its binding ability in a functional ELISA.
When Recombinant Human Glypican 3 is immobilized at 0.5 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 approximately 0.6-3 ng/mL.
When Recombinant Human Glypican 3 is immobilized at 0.5 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 approximately 0.6-3 ng/mL.
Scientific Data Images for Recombinant Human Glypican 3 Protein
Bioactivity of Human Glypican-3
Recombinant human Glypican 3 (2119-GP) binds recombinant human FGF basic 146 in a functional ELISA. The concentration of recombinant human FGF basic 146 that produces 50% of the optimal binding response is 0.6-3 ng/mL.Formulation, Preparation and Storage
Carrier Free
What does CF mean?CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
What formulation is right for me?In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
Carrier: 2119-GP
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Carrier Free: 2119-GP/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Glypican 3
Glypicans (GPC) are a family of heparan sulfate proteoglycans that are attached to the cell surface by a glycosylphosphatidylinositol (GPI) anchor. Six members of this family have been identified in mammals (GPC1-GPC6). All glypican core proteins contain an N-terminal signal peptide, a large globular cysteine-rich domain (CRD) with 14 invariant cysteine residues, a stalk-like region containing the heparan sulfate attachment sites, and a C-terminal GPI attachment site. While glypican proteins do not share strong amino acid sequence identity (they range from 17-63%), the conserved cysteine residues in their CRDs suggests similarity in their
three‑dimensional structure (1, 2).
Mutations in GPC3 cause a rare disorder in humans, Simpson-Golabi-Behmel Syndrome, which is characterized by pre and postnatal overgrowth of multiple tissues and organs and an increased risk for developing embryonic tumors (3). These features are also present in the mouse knock-out of GPC3 indicating that GPC3 regulates cell survival and inhibits cell proliferation during development (4). Glypican 3 has been implicated in regulating many different signaling pathways including: IGF, FGF, BMP and Wnt. An endoproteolytic processing of GPC3 by proprotein convertases is required for the modulation of Wnt signaling (5). Direct interaction with FGF-basic has been observed and is mediated by the heparan sulfate chains (6).
References
- Filmus, J. and S.B. Selleck (2001) J. Clinical Invest. 108:497.
- De Cat, B and G. David (2001) Seminars in Cell & Dev. Biol. 12:117.
- Pilia, G. et al. (1996) Nat. Genet. 12: 241.
- Cano-Gauci, D.F. et al. (1999) J. Cell Biol. 146: 255.
- De Cat, B. et al. (2003) J. Cell Biol. 163:625.
- Song, H.H. et al. (1997) J. Biol. Chem. 272:7574.
Alternate Names
GPC3
Gene Symbol
GPC3
UniProt
Additional Glypican 3 Products
Product Documents for Recombinant Human Glypican 3 Protein
Product Specific Notices for Recombinant Human Glypican 3 Protein
For research use only
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