Prouroguanylin Human (E. coli)

Description

Total 90 AA. MW: 10 kDa (calculated). Two N-Terminal extra AA (highlighted).

Amino Acid Sequence

Source

E. coli

Purity

>95%

SDS-PAGE gel

12% SDS-PAGE separation of Human Prouroguanylin 1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa 2. reduced and heated sample, 5μg/lane 3. non-reduced and non-heated sample, 5μg/lane

Formulation

Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 50mM Phosphate buffer pH7.4

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Storage, Stability/Shelf Life

Store lyophilized protein at –20°C. Lyophilized protein remains stable until the expiry date when stored at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

Applications

Western blotting

Note

This product is intended for research use only.

Introduction to the Molecule

Prouroguanylin is a 112-amino-acid prohormone precursor of uroguanylin- mature biologically active 16-amino-acid peptide cleaved from its C-terminus. Guanylin binds to receptor-guanylate cyclases (CG-C) resulting in increased intracellular cGMP levels leading to CFTCR (Cystic Fibrosis Transmembrane Conductance Regulator) activation and subsequent rise in fluid and electrolyte secretion into the lumen. Prouroguanyline knock-out mice showed impaired renal excretion of external NaCl leasing to elevated blood pressure independent of the level of diatary salt intake.

Prouroguanylin is the predominant circulating molecular form found in circulation and in biological fluids.

References

• Miyazato M, Nakazato M, Yamaguchi H, Date Y, Kojima M, Kangawa K, Matsuo H, Matsukura S. Cloning and characterization of a cDNA encoding a precursor for human uroguanylin.
• Miyazato M, Nakazato M, Matsukura S, Kangawa K, Matsuo H. Genomic structure and chromosomal localization of human uroguanylin.
• Nakazato M, Yamaguchi H, Kinoshita H, Kangawa K, Matsuo H, Chino N, Matsukura S. Identification of biologically active and inactive human uroguanylins in plasma and urine and the increases in renal insufficiency.
• Hamra FK, Fan X, Krause WJ, Freeman RH, Chin DT, Smith CE, Currie MG, Forte LR. Prouroguanylin and proguanylin: purification from colon, structure, and modulation of bioactivity by proteases.
• Cui L, Blanchard RK, Coy LM, Cousins RJ. Prouroguanylin overproduction and localization in the intestine of zinc-deficient rats.