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Human GUCY2C/Guanylyl cyclase C Protein 5197

$315.00$1,050.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Ser24-Gln430
SKU: 5197parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

P25092

express system

HEK293

product tag

C-His-Avi

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

Guanylyl cyclase C (GUCY2C) has canonical centrality in defense of key intestinal homeostatic mechanisms, encompassing fluid and electrolyte balance, epithelial dynamics, antitumorigenesis, and intestinal barrier function. GUCY2C may represent a new target for anti-obesity pharmacotherapy.

molecular weight

The protein has a predicted MW of 48.8 kDa. Due to glycosylation, the protein migrates to 70-80 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human GUCY2C/Guanylyl cyclase C Protein 5197

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Guanylyl cyclase C (GUCY2C) has canonical centrality in defense of key intestinal homeostatic mechanisms, encompassing fluid and electrolyte balance, epithelial dynamics, antitumorigenesis, and intestinal barrier function. GUCY2C may represent a new target for anti-obesity pharmacotherapy.
Protein names
Guanylyl cyclase C (GC-C) (EC 4.6.1.2) (Heat-stable enterotoxin receptor) (STA receptor) (hSTAR) (Intestinal guanylate cyclase)
Protein family
317
Function
Guanylyl cyclase that catalyzes synthesis of cyclic GMP (cGMP) from GTP (PubMed:11950846, PubMed:1718270, PubMed:22436048, PubMed:22521417, PubMed:23269669). Receptor for the E.coli heat-stable enterotoxin; E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GUCY2C (PubMed:1680854, PubMed:1718270). Also activated by the endogenous peptides guanylin and uroguanylin (PubMed:8381596).
Catalytic activity
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence=; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666; Evidence=;
Pathway
211
Subellular location
Cell membrane ; Single-pass type I membrane protein. Endoplasmic reticulum membrane ; Single-pass type I membrane protein. Note=The 145 kDa plasma membrane form of GUCY2C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form.
Structure
Homotrimer (PubMed:11123935). Interacts via its C-terminal region with NHERF4 (PubMed:11950846). Interacts with the lectin chaperone VIP36 (PubMed:23269669).
Post-translational modification
Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GUCY2C activation.
Domain
The protein kinase domain is predicted to be catalytically inactive.
Target Relevance information above includes information from UniProt accession: P25092
The UniProt Consortium

Data

ELISA with Human GUCY2C/Guanylyl cyclase C Protein
Immobilized Human GUCY2C, His Tag at 5µg/ml (100µl/Well) on the plate. Dose response curve for Anti-GUCY2C Antibody, hFc Tag with the EC50 of 8.9ng/ml determined by ELISA.
HPLC of Human GUCY2C/Guanylyl cyclase C Protein
The purity of Human GUCY2C is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human GUCY2C/Guanylyl cyclase C Protein
Human GUCY2C on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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Protocols

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Documents

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