Renin Proteins, Antibodies, cDNA Clones Research Reagents

REN (Renin) is a protein coding gene located on human chromosome 1q32.1. REN is also known as HNFJ2. The human REN gene encodes a 45057 Da protein containing 406 amino acids. The REN protein is biasedly expressed in kidney, placenta and other tissues. Among its related pathways are Peptide hormone metabolism and Agents Acting on the Renin-Angiotensin System Pathway, Pharmacodynamics. REN is related to signaling receptor binding and endopeptidase activity. NAPSA is an important paralog of REN gene. REN is associated with some diseases, including Hyperuricemic Nephropathy, Familial Juvenile, 2 and Renal Tubular Dysgenesis.

Renin Protein (3)

    Renin Antibody (9)

      Renin cDNA Clone (26)


      Renin Lysate (3)

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        Renin Background

        Renin-1, also known as Ren-1, Angiotensinogenase and Kidney renin, is a member of the peptidase A1 family. Renin-1 is synthesized by the juxtaglomerular cells of the kidney in response to decreased blood pressure and sodium concentration. androgen and thyroid hormones influence levels of Renin-1 in mouse submandibular gland (SMG) primarily by regulating the amount of Renin-1 mRNA available for translation. Renin-1 is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. It is expressed at relatively low levels in mouse SMG and kidney. Ren-2 is expressed at high levels in the mouse SMG and at very low levels, if at all, in the kidney. Ren-1 and Ren-2 are closely linked on mouse chromosome 1, show extensive homology in coding and noncoding regions and provide a model for studying the regulation of gene expression.

        Renin References

        • McKeon F.D., et al.,(1986), Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319:463-468.
        • Fisher D.Z., et al., (1986), cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.Proc. Natl. Acad. Sci. U.S.A. 83:6450-6454.
        • Sylvius N., et al.,(2005), In vivo and in vitro examination of the functional significances of novel lamin gene mutations in heart failure patients.J. Med. Genet. 42:639-647.

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