Renin was detected in immersion fixed paraffin-embedded sections of human kidney using Sheep Anti-Human Renin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4090) at 10 µg/mL overnight at 4 °C. Tissue was ...read more
Renin was detected in immersion fixed paraffin-embedded sections of human kidney array using Sheep Anti-Human Renin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4090) at 10 µg/mL overnight at 4 °C. ...read more
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Immunogen affinity purified
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Renin Antibody
renin precursor, renal
Human Renin is a member of the aspartyl proteinase family produced largely in part by the juxtaglomerular cells in the kidney (1). Renin differs from the other members of this class by having a pH optimum near the neutral pH region with native substrates instead of a pH 2.0 to 3.4 range (2). This more neutral pH optimum allows it to be functional in the plasma. Renin also has a very high selectivity for substrates due to a long peptide recognition on either side of the peptide bond undergoing cleavage. An octapeptide substrate was the minimum length to be cleaved by Renin. Renin plays a crucial role in the regulation of blood pressure and salt balance through the cleavage of angiotensinogen, which is the only known physiological substrate of Renin. Renin releases the decapeptide angiotensin I, which in turn is further converted to vasoactive hormone angiotensin II by angiotensin converting enzyme (ACE). Renin is produced as prorenin with 43 pro residues at the N‑terminal of mature Renin. The inactive prorenin becomes activated proteolytically by trypsin, cathepsin B, or other proteinases.
Yokosawa, H. et al. (1980) J. Biol. Chem. 255:3498.
Fuminaki, S. et al. (2004) in Handbook of Proteolytic Enzymes, Barret, A. J. et al. eds. p.54.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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