Recombinant Mouse GUCY2C protein (rFc Tag)

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• Recombinant Mouse GUCY2C protein (rFc Tag) (Eg2871)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg2871

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Validation Data Gallery

• 

  Purity of Recombinant Mouse GUCY2C was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Mouse GUCY2C protein Val20-Met433 (Accession# Q3UWA6-1) with a rabbit IgG Fc tag at the C-terminus.
• GeneID: 14917
• Accession: Q3UWA6-1
• PredictedSize: 73.1 kDa
• SDS-PAGE: 85-125 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

GUCY2C is also named as GUC2C, STAR(Heat-stable enterotoxin receptor), Guanylyl cyclase C and belongs to the adenylyl cyclase class-4/guanylyl cyclase family. It is a receptor for the E.coli heat-stable enterotoxin and is considered to be the true apical membrane receptor for the endogenous ligands uroguanylin and guanylin. GUCY2C is not present in the endocrine pancreas, but is localized exclusively to the ductal system which fully corresponds to the GUCY2C activity detected in the exocrine ductal system, but particularly not in islets of Langerhans. GUCY2C with a molecular mass of 130 kDa is detected in pancreatic and intestinal extracts. The full-length protein is 123 kDa and has a signal peptide and nine glycosylation sites.

References:

1. Kulaksiz H. et al. (2001). J Endocrinol. 170(1):267-75.