Detects human Glypican 1 in Western blots. In Western blots, approximately 15% cross-reactivity with recombinant mouse Glypican 1 is observed and less than 1% cross-reactivity with recombinant human (rh)Glypican 5 and rhGlypican 6 is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human Glypican 1 Asp24-Ser530 Accession # P35052
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Detection of Glypican 1 in MDA‑MB‑231 Human Cell Line by Flow Cytometry.
MDA‑MB‑231 human breast cancer cell line was stained with Goat Anti-Human Glypican 1 Biotinylated Antigen Affinity‑purified Polyclonal Antibody (Catalog # BAF4519, filled histogram) or isotype control antibody (Catalog # BAF108, open histogram), followed by Streptavidin-Phycoerythrin (Catalog # F0040).
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
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.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 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). Human Glypican 1 (GPC-1) is synthesized as a 558 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 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 are potentially two heparan sulfate (HS) modifications on GPC-1 that could contribute to a native molecular weight of approximately 200 kDa (7, 8, 9). Mature human GPC-1 shares 91% aa identity with mature mouse GPC-1. There are two potential splice variants of human GPC-1. Both show an alternate start site at Met73, while one has an additional 65 aa substitution for the C-terminal 264 amino acids (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). This is accomplished 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 contract, 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).
Song, H.H. and J. Filmus (2002) Biochim. Biophys. Acta 1573:241.
Fransson, L-A. et al. (2004) Cell. Mol. Life Sci. 61:1016.
De Cat, B. and G. David (2001) Semin. Cell Dev. Biol. 12:117.
Lamoureux, F. et al. (2007) BioEssays 29:758.
Veugelers, M. et al. (1999) J. Biol. Chem. 274:26968.
GenBank Accession # P35052.
David, G. et al. (1990) J. Cell Biol. 111:3165.
Lories, V. et al. (1992) J. Biol. Chem. 267:1116.
Lories, V. et al. (1989) J. Biol. Chem. 264:7009.
GenBank Accession # EAW71184.
GenBank Accession # EAW71183.
Chernousov, M.A. et al. (2006) J. Neurosci. 26:508.
Wegrowski, Y. et al. (2006) Clin. Exp. Immunol. 144:485.
Qiao, D. et al. (2003) J. Biol. Chem. 278:16045.
Kayed, H. et al. (2006) Int. J. Oncol. 29:1139.
Selleck, S.B. (2006) SciSTKE, April 4:pe17.
Qiao, D. et al. (2003) J. Biol. Chem. 278:16045.
Su, G. et al. (2006) Am. J. Pathol. 168:2014.
Allen, B.L. and A.C. Rapraeger (2003) J. Cell Biol. 163:637.
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The data collected includes not only links to publications in PubMed,
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