Welcome to LookChem.com Sign In|Join Free
  • or

Encyclopedia

RENNIN

Base Information
  • Chemical Name:RENNIN
  • CAS No.:9015-94-5
  • Molecular Formula:
  • Molecular Weight:0
  • Hs Code.:
RENNIN

Synonyms:Angiotensinogenase;E.C. 3.4.23.15; E.C. 3.4.4.15; E.C. 3.4.99.19

Suppliers and Price of RENNIN
Supply Marketing:
Business phase:
The product has achieved commercial mass production*data from LookChem market partment
Manufacturers and distributors:
  • Manufacture/Brand
  • Chemicals and raw materials
  • Packaging
  • price
  • Usbiological
  • Renin
  • 96Tests
  • $ 879.00
  • Usbiological
  • Renin
  • 96Tests
  • $ 851.00
  • Usbiological
  • Renin
  • 96Tests
  • $ 669.00
  • Usbiological
  • Renin
  • 48Tests
  • $ 588.00
  • Usbiological
  • Renin
  • 200ul
  • $ 442.00
  • Usbiological
  • Renin
  • 10ug
  • $ 345.00
  • Usbiological
  • Renin
  • 10ug
  • $ 339.00
  • Usbiological
  • Renin
  • 10ug
  • $ 339.00
  • Cayman Chemical
  • Renin (human, recombinant)
  • 25μg
  • $ 315.00
Total 6 raw suppliers
Chemical Property of RENNIN
Chemical Property:
  • PSA:0.00000 
  • LogP:0.00000 
  • Storage Temp.:−20°C 
Purity/Quality:

98%,99%, *data from raw suppliers

Renin *data from reagent suppliers

Safty Information:
  • Pictogram(s):  
  • Hazard Codes:Xn 
  • Statements: 36/37/38-42 
  • Safety Statements: 22-24-26-36/37 
MSDS Files:
Useful:
  • General Description RENNIN, also known as angiotensinogenase (E.C. 3.4.23.15, 3.4.4.15, or 3.4.99.19), is an aspartic protease that plays a critical role in the renin-angiotensin system by cleaving angiotensinogen to produce angiotensin I. The study highlights the development of potent renin inhibitory peptides, where replacing the histidyl residue at the P-2 site with β-aspartyl or malic acid residues enhances hydrophilicity and reduces peptide size while maintaining subnanomolar inhibitory potency. Molecular modeling suggests that the interaction with Ser-229 is key for binding efficacy, with malic acid analogues demonstrating particularly strong inhibitory activity. These findings underscore the potential of modified peptides as effective renin inhibitors for therapeutic applications.
Refernces

Renin Inhibitory Peptides. A β-Aspartyl Residue as a Replacement for the Histidyl Residue at the P-2 Site

10.1021/jm00167a009

The study investigates the structure-activity relationship of renin inhibitory peptides with a focus on replacing the histidyl residue at the P-2 site with a β-aspartyl residue to increase hydrophilicity and decrease peptide size. The researchers synthesized a series of peptides containing β-aspartyl and malic acid residues at the P-2 site and tested their inhibitory potency against human plasma renin. The peptides exhibited potent inhibitory activities in the subnanomolar range. Molecular modeling was conducted to explore the interactions between the enzyme and the inhibitors, suggesting that the Ser-229 conformer, where the carboxylic acid group is close to Ser-229, is more favorable for binding. The study concludes that the β-aspartyl and malic acid-containing peptides are effective renin inhibitors, with the malic acid analogues showing enhanced potency.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1 Customer Service

What can I do for you?
Get Best Price

Get Best Price for 9015-94-5