Recombinant Human GIPR Fc Chimera Protein, CF Summary
Accession # P48546.1
|IEGRMD||Human IgG1 Fc|
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||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.
When Biotinylated Human GIP Peptide is captured on a Streptavidin Coated Plate (CP004), it binds to Recombinant Human GIPR Fc Chimera Protein (Catalog # 11088-GI). The ED50 for this binding is 20.0‑100 ng/mL.
2 μg/lane of Recombinant Human GIPR Fc Chimera Protein (Catalog # 11088-GI) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 45-59 kDa and 90-120 kDa, respectively.
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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