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Prouroguanylin Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Guanylate cyclase activator 2B, Guanylate cyclase C-activating peptide 2, Guanylate cyclase C-activating peptide II, GCAP-II, Uroguanylin, UGN, GUCA2B
  • Species:Human
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Cat. No. Size Price


RD172069100 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 96 AA. MW: 10.7 kDa (calculated). N-Terminal His-tag (10 extra AA). UniprotKB acc.no. Q16661

Amino Acid Sequence

MKHHHHHHASVYIQYQGFRVQLESMKKLSDLEAQWAPSPRLQAQSLLPAVCHHPALPQDLQPVCASQEASSIFKTLRTIANDDCELCVNVACTGCL

Source

E. coli

Purity

Purity as determined by densitometric image analysis: >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, 2.5μg/lane
3. non-reduced and non-heated sample, 2.5μg/lane

Endotoxin

< 1.0 EU/ug

Formulation

0.2–0.7 mg/ml in 20mM TRIS, 50mM NaCl, 20% (v/v) glycerol, pH 7.5 – filtered (0.4 μm), frozen

Reconstitution

Defrost at ambient temperature.

Applications

Western blotting, ELISA

Shipping

On ice. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store protein at –80°C. Protein remains stable until the expiry date when stored at –80°C. Avoid repeated freezing/thawing cycles.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Oncology, Others, Renal disease

Summary

Prouroguanylin (about 9,7 kDa) is a biologically inactive form of uroguanylin circulating in a bloodstream. Uroguanylin is a small –molecular-weight peptide which has been shown to participate in the regulation of salt and water homeostasis in mammals via cGMP-mediated processes in the intestine, kidney and other epithelia. Prouroguanylin levels are markedly increased in chronic renal failure. The severity of chronic renal disease correlates with the magnitude of increases in plasma prouroguanylin concentrations. Uroguanylin/prou­roguanylin levels also increased in the nephrotic syndrome. It may be concluded that uroguanylin/prou­roguanylin is cleared from the circulation by the kidney and that reduced functioning renal mass and decreased glomerular filtration rates (GFR) lead to substantial increases in the concentrations of these peptides in serum and plasma. Circulating forms of uroguanylin and prouroguanylin are thought to be a major source of the urinary forms of biologically active uroguanylin. Both of these peptides can enter renal tubules by glomerular filtration. Prouroguanylin in the tubular lumen is than converted to active uroguanylin by tubular endoproteases because prouroguanylin is not detected in the urine. Studies of pathogenesis of colorectal cancer demonstrate that prouroguanylin may serve as marker of colon tumors in the body. Recent experiments also refer to possibility of prouroguanylin to play a significant role at diagnostic and treatment of heart diseases. Areas of investigation: Renal disease, Heart failure, Oncology

Summary References (7)

References to Prouroguanylin

  • Fan X. Wang Y, London RM, Eber SL, Krause WJ, Freeman RH, Forte LR: Signaling Pathways for Guanylin and Uroguanyiln in the Digestive, Renal, Central Nervous, Reproductive, and Lymphoid Systems. Endocrinology 138, 4636–4648 (1997).
  • Forte LR: A novel role for uroguanylin in the regulation of sodium balance. Am Clin Invest 112, 1138–1141 (2003).
  • Forte LR, Freeman RH, Krause WJ, London RM: Guanylin peptides: cyclic GMP signalling mechanisms. Braz J med Biol Res 32(11), 1329–1336 (1999).
  • Forte LR, London RM, Freeman RH, Krause WJ: Guanylin peptides: renal actions mediated by cyclic GMP. Am J Physiol Renal Physiol 278, 180–191 (2000).
  • Hamra FK, Fan X, Krause WJ, Freeman RH, Chin DT, Smith ChE, Currie MG, Forte LR: Prouroguanylin and proguanylin: Purification from Colon, Structure, and Modulation of Bioactivity by Proteases. Endocrinology 137, 257–265 (1996).
  • Hidaka Y, Shimono Ch, Ohno M, Okumura N, Adermann K, Forshmann W-G, Shimonishi Y: Dual Function of the Propeptide of Prouroguanylin in the Folding of the Mature Peptide. J Biol Chem 257, 25155–25162 (2000).
  • Shailubhai K, Yu HH, Karunanandaa K, Wang JY, Eber SL, Wang Y, Joo NS, Kim HD, Miedema BW, Abbas SZ, Boddupalli SS, Currie MG, Forte LR: Uroguanylin Treatment Suppresses Polyp Formation in the APCMin/+ Mouse and Induces Apoptosis in Human Colon Adenocarcinom Cells via Cyclic GMP. Cancer research 60, 5151–5157 (2000).
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