Recombinant Mouse Glypican 1 Protein, CF

Recombinant Mouse Glypican 1 Protein, CF Summary

Product Specifications

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.

Background: Glypican 1

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).

Related Research Areas

• Proteoglycans
• Wnt Signaling Modulators