Recombinant Human Glypican 3 Fc Chimera Protein, CF Summary
Product Specifications
Human Glypican 3 (Gln25-His559) Accession # P51654.1 | IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
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.
11078-GP
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in 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.
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Scientific Data
![](https://aeroglobalimagesuat.blob.core.windows.net/images/datasheets/11078-gp_recombinant-human-glypican-3-fc-chimera-protein-cf-binding-activity-32202284244.jpg)
When Recombinant Human FGF basic/FGF2/bFGF (233-FB) is immobilized at 0.500 µg/mL (100 µL/well), Recombinant Human Glypican 3 Fc Chimera Protein (Catalog # 11078-GP) binds with an ED50 of 0.0120-0.120 µg/mL.
Reconstitution Calculator
Background: Glypican 3
Glypican 3 (GPC3), also known as OCI5 and MXR7, is a member of the heparan sulfate proteoglycan (HSPG) family (1). In mammals, six glypican family members have been identified, all sharing a structurally common extracellular domain (ECD) with 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. The ECD of GPC3 can be cleaved by furin to produce two subunits that are linked by disulfide bonds: a 40 kDa N‑terminal alpha subunit that can be secreted into the blood and a 30 kDa membrane-bound C‑terminal beta subunit containing two HS glycan chains (1-3). Within ECD, human GPC3 shares 96% amino acid sequence identity with both mouse and rat GPC3. Several isoforms of GPC3 due to alternative splicing have been reported (1). GPC3 is widely expressed on the membrane of various embryonic cells, but not on those in adult liver, and is involved in the regulation of growth and development of the body (4). GPC3 is over-expressed in hepatocellular carcinomas and binding of GPC3 to CD81 promotes development of carcinomas by activation of Hippo pathways in hepatocytes (5). GPC3 is an important biomarker present in the serum of hepatocellular carcinoma patients, which distinguishes benign from cancerous nodules (6). Loss-of-function mutations in GPC3 are associated with Simpson-Golabi-Behmel (SGB) syndrome, a condition characterized by tissue overgrowth (dysmorphogenesis) (7).
- Ho, M. and Kim, H. (2012) Eur. J. Cancer. 47:333.
- Haruyama, Y. and Kataoka, H. (2016) World J. Gastroenterol. 22:275.
- Shimizu, Y. et al. (2019) Front Oncol. 9:248.
- Gonzales, A.D. et al. (1998) J. Cell Biol. 141:1407.
- Xue, Y. et al. (2018) Am J Pathol. 188(6):1469.
- Ge, S. et al. (2018) Filmus, Int J Clin Exp Pathol. 11(12):5774.
- Pilia, G. et al. (1996) Nature Genet.12:241.
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