Recombinant Human GIPR Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Biotinylated Human GIP Peptide is captured on a Streptavidin Coated Plate
(Catalog #
CP004), it binds to Recombinant Human GIPR Fc Chimera. The ED 50 for this binding is 20.0-100 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human GIPR protein Human GIPR (Gly26-Gln138) Accession # P48546.1 | IEGRMD | Human IgG1 Fc (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gly26 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
40 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. |
SDS-PAGE |
45-59 kDa, under reducing conditions. |
Packaging, Storage & Formulations
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.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human GIPR Fc Chimera Protein, CF
Background
Human Gastric Inhibitory Polypeptide Receptor (GIPR) is a
transmembrane G protein coupled receptor that is mainly found in beta-cells
within the pancreas (1). GIPR has 117 aa
extracellular domain on its N-terminus, a central region consisting of seven transmembrane
domains and a 68 aa C-terminal cytoplasmic domain that is responsible for
intracellular transduction with the G-Protein (2). GIPR has three known isoforms produced by
alternative splicing. The extracellular domain of human GIPR shows 76.3% and
81.2% amino acid identity with mouse and rat homolog, respectively. When
originally discovered, GIPR was thought to have a role of inhibiting the
secretion of gastrin and gastric acid (1). However, it was subsequently discovered that
GIPR's main function was to stimulate the release of insulin in the presence of
elevated blood glucose levels (1).
GIPR has been found to bind to glucagon-like peptide-1 (GIP) and
cascades downstream to release insulin (1). GIP and its receptor
(GIPR) are of high pharmacological interest, since expression of GIPR are found
in different organs and systems, especially in identification and design of new
molecules for the treatment of diabetes mellitus and obesity (3-6). GIPR has
also been shown to have an indirect relation with bone health and density. Mouse overexpressing GIP and GIPR had increased
levels of osteoblasts and an overall decrease in age-related bone loss, while mice
with GIPR knockout showed a decrease in overall bone mass and a higher level of
compromised bone mass (7). Targeted Radionuclide Therapy (TRT) against GIPR
positive cancer cells showed a significant increase of cell cycle arrest,
specifically at the G2 and M phase, along with extensive DNA damage (8).
- YAMADA, Y. et al. (1995). Genomics 29:773.
- Parthier, C. et al. (2007). Proc.Natl. Acad. Sci. U.S.A. 104:13942.
- Sherman, S.K. et at. Surgery. (2013) 154(6): . doi:10.1016/j.surg.2013.04.052.
- Yagub, T. et al. (2010) Molecular Pharmacology. 77(4):547.
- Volz, A. et al. (1995) Febs Letters. 373(1):23.
- Kieffer, T.J. et al. (2003) Trends Pharmacol Sci 24:110.
- Torekov, S.S. et al. (2014) J Clin Endocrinol Metab. 99:E729.
- Shi, X, et al. (2021) Bioconjug Chem. 32:1763.
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