Product Name :
Biotinylated Human GUCY2C/Guanylyl cyclase C Protein 3381
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 55-65 kDa based on Tris-Bis PAGE result.
Available Size :
100 µg, 500 µg
Endotoxin:
Less than 1EU per μg by the LAL method.
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.
Additional Information:
express systemHEK293|product tagC-His-Avi|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundGuanylyl 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 weightThe protein has a predicted MW of 48.8 kDa. Due to glycosylation, the protein migrates to 55-65 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Biotinylated Human GUCY2C/Guanylyl cyclase C Protein 3381proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceGuanylyl 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 namesGuanylyl cyclase C (GC-C) (EC 4.6.1.2) (Heat-stable enterotoxin receptor) (STA receptor) (hSTAR) (Intestinal guanylate cyclase)Protein family317FunctionGuanylyl 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 activityCATALYTIC 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=;Pathway211Subellular locationCell 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.StructureHomotrimer (PubMed:11123935). Interacts via its C-terminal region with NHERF4 (PubMed:11950846). Interacts with the lectin chaperone VIP36 (PubMed:23269669).Post-translational modificationGlycosylation 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.DomainThe protein kinase domain is predicted to be catalytically inactive.Target Relevance information above includes information from UniProt accession: P25092The UniProt Consortium|
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