Reactivity | HuSpecies Glossary |
Applications | WB, Flow |
Clonality | Polyclonal |
Host | Goat |
Conjugate | Biotin |
Concentration | LYOPH |
Immunogen | Mouse myeloma cell line NS0-derived recombinant human Glypican 1 Asp24-Ser530 Accession # P35052 |
Specificity | 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. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Goat |
Gene | GPC1 |
Purity Statement | Antigen Affinity-purified |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Readout System | ||
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 with BSA as a carrier protein. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.2 mg/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 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).
Secondary Antibodies |
Isotype Controls |
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