Description
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation. The protein encoded by this gene can bind to and inhibit the dipeptidyl peptidase activity of CD26, and it can induce apoptosis in certain cell types. Deletion mutations in this gene are associated with Simpson-Golabi-Behmel syndrome, also known as Simpson dysmorphia syndrome. Alternative splicing results in multiple transcript variants.
Bio-activity
Measured by its binding ability in a functional ELISA. When Recombinant Human Glypican 3 is immobilized at 0.5 μg/mL (100 μL/well), the concentration of Recombinant Human FGF basic 146 aa that produces 50% of the optimal binding response is approximately 0.6-3 ng/mL.
Notes
Glypican 3 is subject to endoproteolytic processing by proprotein convertases (PC). By amino acid sequencing, three peptides (the first with a blocked N-terminus most likely starts with Gln25, the second peptide starts with Ser359 after a furin cleavage site, and the third peptide starts with Val483) are present in the recombinant GPC3 preparation. Peptides 2 and 3 are detected at a 1:1 ratio. All three peptides remained associated via disulfide bonds.
Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 centigrade as supplied.
1 month, 2 to 8 centigrade under sterile conditions after reconstitution.
3 months, -20 to -70 centigrade under sterile conditions after reconstitution.
