Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rmGlypican 1 at 3 µg/mL (100 µL/well) will bind rhFGF-basic with an apparent KD < 1 nM. |
Source | Mouse myeloma cell line, NS0-derived mouse Glypican 1 protein Asp24-Ser529, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | Asp24 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Gpc1 |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 56.4 kDa. 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. |
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SDS-PAGE | 57-62 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 500 μg/mL in sterile PBS. |
The Glypicans (glypiated proteoglycans) are a small multigene family of GPI-linked proteoglycans that play a key role in growth factor signaling (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. One subfamily contains Glypicans 1, 2, 4 and 6, while another subfamily contains Glypicans 3 and 5 (3, 5). Mouse Glypican 1 (GPC-1) is synthesized as a 557 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 506 aa mature segment, and a 28 aa C-terminal prosegment (6, 7). There are two potential N-linked, and four potential O-linked sites for glycosylation or glycanation. There is at least one heparan sulfate (HS) modification on GPC-1 that contributes to a native molecular weight of approximately 110 kDa (8, 9). Mature mouse GPC-1 shares 91% and 98% aa identity with mature human and rat GPC-1, respectively. There are two potential splice variants of mouse GPC-1. The first is truncated and shows a seven amino acid substitution for the first 294 aa; the second reveals an alternate start site at Met73 (10, 11). Cells known to express GPC-1 include neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumor-associated vascular endothelial cells (8, 9, 12 - 15). The function of GPC-1 is complex and varied. As a proteoglycan, it appears to make use of its HS adduct to impact select growth factor activity (16). GPC-1 accomplishes its co-receptor role by having juxtramembrane HS attachment sites and a flexible, GPI-linkage (17). Data suggests GPC-1 and sulfation enzymes may collaborate to regulate FGF signaling. HS modules that are rich in 2-O- and 6-O- sulfate upregulate FGF-2 activation of FGFR1c (18). Similarly, FGF-1 requires both 2-O- and 6-O-sulfation to bind to FGFR2c and 3c. By contrast, FGF-1 requires no sulfation to bind to FGFR2b, and FGF-8b needs only 6-O-sulfation to activate FGFR3c. Thus, many FGF receptor isoform specific effects may be attributed to an interaction between Glypican family members and the cell sulfation system (19).
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