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Recombinant Human GIPR Fc Chimera Protein, CF

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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 ...read more
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 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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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 ED50 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-terminusC-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
  • Bioactivity
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

  • gastric inhibitory polypeptide receptor
  • GIPR
  • GIP-R
  • Glucose-dependent insulinotropic polypeptide receptor
  • MGC126722
  • PGQTL2

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).
  1. YAMADA, Y. et al. (1995). Genomics 29:773.
  2. Parthier, C. et al. (2007). Proc.Natl. Acad. Sci. U.S.A. 104:13942.
  3. Sherman, S.K. et at. Surgery. (2013) 154(6): . doi:10.1016/j.surg.2013.04.052.
  4. Yagub, T. et al. (2010) Molecular Pharmacology. 77(4):547.
  5. Volz, A. et al. (1995) Febs Letters. 373(1):23.
  6. Kieffer, T.J. et al. (2003) Trends Pharmacol Sci 24:110.
  7. Torekov, S.S. et al. (2014) J Clin Endocrinol Metab. 99:E729.
  8. Shi, X, et al. (2021) Bioconjug Chem. 32:1763.

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