Recombinant Mouse Guanylyl Cyclase C/GUCY2C His Protein, CF

2 μg/lane of Recombinant Mouse Guanylyl Cyclase C/GUCY2C His-tag Protein (Catalog # 11093-GC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 85-100 kDa.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Guanylyl Cyclase C/GUCY2C His Protein, CF Summary

• Additional Information: His-tag
• Details of Functionality: Bioassay data are not available.
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse Guanylyl Cyclase C/GUCY2C protein
  Val20-Gln430, with a C-terminal 6-His tag
• Accession #: Q3UWA6.1
• N-terminal Sequence: Val20
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Purity Statement: Antigen Affinity-purified
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 48 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: 85-100 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 Mouse Guanylyl Cyclase C/GUCY2C His Protein, CF

• DIAR6
• EC 4.6.1
• GCC
• GC-C
• guanylate cyclase 2C (heat stable enterotoxin receptor)
• Guanylate Cyclase C
• Guanylyl Cyclase C
• GUC2C
• GUC2CEC 4.6.1.2
• GUCY2C
• heat-stable enterotoxin receptor
• hSTAR
• Intestinal guanylate cyclase
• MUCIL
• STA Receptor
• StAR
• STARSTA receptor

Background

Guanylyl Cyclase C (GUCY2C), also known as heat-stable enterotoxin receptor, is a type I transmembrane protein of the guanylate cyclase (GC) family and helps regulate intestinal function (1, 8). There are 7 known members of the GC family (GC-A through GC-G) and they catalyze the conversion of guanosine triphosphate to cyclic guanosine monophosphate (cGMP) and pyrophosphate (1-4). Mature mouse GUCY2C consists of an extracellular domain (ECD) with a ligand binding domain, a transmembrane segment and a cytoplasmic region possessing a pseudokinase domain and a GC catalytic domain. The ECD of mature mouse GUCY2C shares 70% and 88% amino acid sequence identity with the ECD of human and rat GUCY2C, respectively. GUCY2C is primarily expressed in intestinal epithelial cells from the duodenum to rectum and binds to the endogenous gastrointestinal hormones guanylin and uroguanylin (1-4). Activation of GUCY2C signaling mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner (5). GUCY2C is also expressed in neurons, where it plays a role in attention deficiency/hyperactive behavior (6). GUCY2C is being investigated as a treatment for several gastrointestinal disorders including irritable bowel syndrome, obesity, colorectal cancer, and chronic idiopathic constipation (7, 8). Our Avi-tag Biotinylated GUCY2C features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

1. Arshad, N. and Visweswariah S.S. (2012) FEBS Lett. 586:2835.
2. Potter, L.R. (2011) Cell Signal. 2011 23:1921.
3. Arshad, N. et al. (2013) J. Biol. Chem. 288:3907.
4. Gibbons, A.V. et al. (2013) Cancer Res. 73:22.
5. Lucas, K. et al. (2000) Pharmacol Rev. 52:375.
6. Gong, R. et al. (2011) Science. 333:1642.
7. Waldman, S.A. and Camilleri, M. (2018) Gut. 67:1543.
8. Kim, G.W. et al. (2013) Trends Endocrinol Metab. 24(4):165.

Bioinformatics

• Uniprot:
  • Q3UWA6.1()