Particulate Guanylate Cyclase C Peptide Blocking Peptide peptide (STJ504702)

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STJ504702-250
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Short Description :Particulate Guanylate Cyclase C Peptide Blocking Peptide is synthetically produced from the C-Term sequence and is suitable for use in western blot applications.
Applications:Immunodepletion/Immunocompetition
Note:STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Formulation:Liquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice.
Storage Instruction:Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol:Gucy2c
Gene ID:25711
Uniprot ID:GUC2C_RAT
Immunogen:Synthetic C-terminal peptide corresponding to unique amino acid sequences on Particulate Guanylyl Cyclase C protein.
Immunogen Region:C-Term
Post Translational Modifications Glycosylation at Asn-74 and/or Asn-78 is required for interaction with VIP36 while glycosylation at Asn-401 modulates ligand-mediated GC-C activation.
Function Guanylyl cyclase that catalyzes synthesis of cyclic GMP (cGMP) from GTP. Receptor for the E.coli heat-stable enterotoxin.E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GUCY2C.
Peptide Name Guanylyl Cyclase C
Gc-C
Heat-Stable Enterotoxin Receptor
Sta Receptor
Intestinal Guanylate Cyclase
Database Links Reactome: R-RNO-8935690
Cellular Localisation Cell Membrane
Single-Pass Type I Membrane Protein
Endoplasmic Reticulum Membrane
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
Alternative Peptide Names Guanylyl Cyclase C protein
Gc-C protein
Heat-Stable Enterotoxin Receptor protein
Sta Receptor protein
Intestinal Guanylate Cyclase protein
Gucy2c protein
Guc2c protein

Information sourced from Uniprot.org