GUCY2C (E6I2U) Rabbit mAb (BSA and Azide Free) #92931
- WB
- IHC
Supporting Data
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 145, 130 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
GUCY2C (E6I2U) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total GUCY2C protein. Non-specific staining was observed in acinar cells of the salivary gland and keratinized epithelium of the skin by immunohistochemistry.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys1046 of human GUCY2C protein.
Background
Guanylyl cyclase C (GUCY2C) is a type I transmembrane glycoprotein whose expression in normal tissue is largely restricted to the apical membranes of polarized epithelial cells of the intestine (1,2). The guanylyl cyclase activity within the intracellular domain of GUCY2C is activated by binding exogenous bacterial enterotoxins and the endogenous peptide hormone agonists, guanylin and uroguanylin, which facilitates production of the second messenger cGMP (3-5). GUCY2C signaling plays a critical role in regulating the metabolism, proliferation, and differentiation of intestinal epithelial cells. These processes are critical for epithelial barrier renewal, water, and ion balance (6-8). Research studies have shown that the GUCY2C signaling axis functions to suppress intestinal tumorigenesis, in part, by restraining AKT activity (9,10). Lesions in the GUCY2C signaling axis that frequently contribute to cellular transformation are associated with a loss of expression of its endogenous ligands, which promotes a compensatory increase in GUCY2C expression. Indeed, GUCY2C expression is maintained in a high percentage of primary and metastatic human colorectal tumors, which has raised interest in therapeutically targeting this receptor (11,12).
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- Kim, G.W. et al. (2013) Trends Endocrinol Metab 24, 165-73.
- Currie, M.G. et al. (1992) Proc Natl Acad Sci U S A 89, 947-51.
- Kita, T. et al. (1994) Am J Physiol 266, F342-8.
- Schulz, S. et al. (1990) Cell 63, 941-8.
- Li, P. et al. (2007) Am J Pathol 171, 1847-58.
- Li, P. et al. (2007) Gastroenterology 133, 599-607.
- Pitari, G.M. et al. (2001) Proc Natl Acad Sci U S A 98, 7846-51.
- Lin, J.E. et al. (2010) Gastroenterology 138, 241-54.
- Gibbons, A.V. et al. (2013) Cancer Res 73, 6654-66.
- Mathur, D. et al. (2020) Clin Cancer Res 26, 2188-2202.
- Magee, M.S. et al. (2018) Cancer Immunol Res 6, 509-516.
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