Renin cDNA ORF Clone, Human, C-HA tag General Information
Full length Clone DNA of Human rennin with C terminal HA tag.
Enhanced CMV promoter
HA Tag Sequence: TATCCTTACGACGTGCCTGACTACGCC
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Antibiotic in Mammalian cell
Stable or Transient mammalian expression
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**
Renin cDNA ORF Clone, Human, C-HA tag Alternative Names
FLJ10761 cDNA ORF Clone, Human;HNFJ2 cDNA ORF Clone, Human;REN cDNA ORF Clone, Human
Renin Background Information
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.
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.